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| | PROZ | Vitamin K-dependent protein Z; Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids; Belongs to the peptidase S1 family. (422 aa) |
| | PREP | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. (710 aa) |
| | TMPRSS9 | Transmembrane protease serine 9; Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-Pro-Ala-AMC are not significantly hydrolyzed; Belongs to the peptidase S1 family. (1059 aa) |
| | PRSS51 | Serine protease 51. (265 aa) |
| | ENSP00000493607 | Uncharacterized protein. (631 aa) |
| | PRSS41 | Serine protease 41; Belongs to the peptidase S1 family. (318 aa) |
| | PARL-2 | Presenilins-associated rhomboid-like protein, mitochondrial. (408 aa) |
| | PRSS2 | Trypsin-2; In the ileum, may be involved in defensin processing, including DEFA5; Belongs to the peptidase S1 family. (261 aa) |
| | OVCH2 | Ovochymase-2; Ovochymase 2. (565 aa) |
| | FURIN | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. (794 aa) |
| | PAMR1 | Inactive serine protease PAMR1; May play a role in regeneration of skeletal muscle. Belongs to the peptidase S1 family. (737 aa) |
| | PCSK6 | Proprotein convertase subtilisin/kexin type 6; Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway, with unique restricted distribution in both neuroendocrine and non-neuroendocrine tissues. (969 aa) |
| | TPSB2 | Tryptase beta 2; Belongs to the peptidase S1 family. (275 aa) |
| | PRSS57 | Serine protease 57; Serine protease that cleaves preferentially after Arg residues. Can also cleave after citrulline (deimidated arginine) and methylarginine residues ; Belongs to the peptidase S1 family. (283 aa) |
| | PRSS56 | Serine protease 56; Serine protease required during eye development. (603 aa) |
| | TMPRSS7 | Transmembrane protease serine 7; Serine protease which preferentially hydrolyzes peptides with Arg at the P1 position; Belongs to the peptidase S1 family. (717 aa) |
| | KLK11 | Kallikrein-11 inactive chain 1; Possible multifunctional protease. Efficiently cleaves 'bz- Phe-Arg-4-methylcoumaryl-7-amide', a kallikrein substrate, and weakly cleaves other substrates for kallikrein and trypsin. Cleaves synthetic peptides after arginine but not lysine residues. (282 aa) |
| | KLK13 | Kallikrein-13; Kallikrein related peptidase 13. (277 aa) |
| | KLK7 | Kallikrein-7; May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines. (253 aa) |
| | KLK9 | Kallikrein-9; Kallikrein related peptidase 9. (250 aa) |
| | KLK15 | Kallikrein-15; Protease whose physiological substrate is not yet known; Belongs to the peptidase S1 family. Kallikrein subfamily. (256 aa) |
| | SEC11C | Signal peptidase complex catalytic subunit SEC11C; Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. (192 aa) |
| | CFD | Complement factor D; Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway; Belongs to the peptidase S1 family. (260 aa) |
| | ELANE | Neutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis. Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae ; Belongs to the peptidase S1 family. Elastase subfamily. (267 aa) |
| | MMP12 | Macrophage metalloelastase; May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3; Belongs to the peptidase M10A family. (470 aa) |
| | CTRL | Chymotrypsin-like protease CTRL-1; Chymotrypsin like; Belongs to the peptidase S1 family. (264 aa) |
| | ADAM8 | Disintegrin and metalloproteinase domain-containing protein 8; Possible involvement in extravasation of leukocytes. (824 aa) |
| | SEC11A | SEC11 homolog A, signal peptidase complex subunit. (185 aa) |
| | PRSS58 | Serine protease 58; Belongs to the peptidase S1 family. (241 aa) |
| | PCSK5 | Proprotein convertase subtilisin/kexin type 5; Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive and regulated secretory pathways. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha-integrins; Belongs to the peptidase S8 family. (1860 aa) |
| | C1R | Complement C1r subcomponent heavy chain; C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system; Belongs to the peptidase S1 family. (719 aa) |
| | HPR | Haptoglobin-related protein; Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF-1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribute to the clearance of cell-free hemoglobin to allow hepatic recycling of heme iron. (348 aa) |
| | TMPRSS13 | Transmembrane serine protease 13; Belongs to the peptidase S1 family. (567 aa) |
| | E9PLN8_HUMAN | VKc domain-containing protein. (166 aa) |
| | HGFAC | Hepatocyte growth factor activator short chain; Activates hepatocyte growth factor (HGF) by converting it from a single chain to a heterodimeric form; Belongs to the peptidase S1 family. (662 aa) |
| | ENSP00000418875 | Probable threonine protease PRSS50. (385 aa) |
| | CFB | Complement factor B Ba fragment; Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes. (764 aa) |
| | TMPRSS4 | Transmembrane protease serine 4; Probable protease. Seems to be capable of activating ENaC (By similarity). (437 aa) |
| | MST1 | Hepatocyte growth factor-like protein alpha chain; Macrophage stimulating 1. (725 aa) |
| | TMPRSS3 | Transmembrane protease serine 3; Probable serine protease that plays a role in hearing. Acts as a permissive factor for cochlear hair cell survival and activation at the onset of hearing and is required for saccular hair cell survival (By similarity). Activates ENaC (in vitro). (454 aa) |
| | B4E1Z4_HUMAN | cDNA FLJ55673, highly similar to Complement factor B; Belongs to the peptidase S1 family. (1266 aa) |
| | PRSS45P | Serine protease 45, pseudogene. (308 aa) |
| | PRSS48 | Serine protease 48; Belongs to the peptidase S1 family. (328 aa) |
| | PREPL | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. (727 aa) |
| | C1S | Complement C1s subcomponent heavy chain; C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4. (688 aa) |
| | IMMP2L | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO; Belongs to the peptidase S26 family. IMP2 subfamily. (175 aa) |
| | TMPRSS6 | Transmembrane protease serine 6; Serine protease which hydrolyzes a range of proteins including type I collagen, fibronectin and fibrinogen. Can also activate urokinase-type plasminogen activator with low efficiency. May play a specialized role in matrix remodeling processes in liver. Through the cleavage of HJV, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis. (824 aa) |
| | F11 | Coagulation factor XIa heavy chain; Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. (625 aa) |
| | MASP2 | Mannan-binding lectin serine protease 2 A chain; Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. (686 aa) |
| | TMPRSS2 | Transmembrane protease serine 2 non-catalytic chain; Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike gl [...] (529 aa) |
| | TMPRSS12 | Transmembrane serine protease 12; Belongs to the peptidase S1 family. (348 aa) |
| | CFI | Complement factor I heavy chain; Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha- chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired [...] (591 aa) |
| | RHBDD1 | Rhomboid-related protein 4; Intramembrane-cleaving serine protease that cleaves single transmembrane or multi-pass membrane proteins in the hydrophobic plane of the membrane, luminal loops and juxtamembrane regions. Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded membrane proteins. Required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfe [...] (315 aa) |
| | KLK8 | Kallikrein-8; Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte [...] (305 aa) |
| | KLK14 | Kallikrein-14; Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression incl [...] (267 aa) |
| | KLK6 | Kallikrein-6; Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neu [...] (244 aa) |
| | TPP2 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity). (1262 aa) |
| | CTRC | Chymotrypsin-C; Regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. Has chymotrypsin-type protease activity and hypocalcemic activity. (268 aa) |
| | CELA2B | Chymotrypsin-like elastase family member 2B; Acts upon elastin; Belongs to the peptidase S1 family. Elastase subfamily. (269 aa) |
| | F7 | Coagulation factor VII; Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium. (466 aa) |
| | F10 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. (488 aa) |
| | PLAU | Urokinase-type plasminogen activator short chain A; Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. (431 aa) |
| | MMP9 | 67 kDa matrix metalloproteinase-9; May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. Belongs to the peptidase M10A family. (707 aa) |
| | CTSS | Cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. (331 aa) |
| | HTRA1 | Serine protease HTRA1; Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF- binding proteins. Inhibits sign [...] (480 aa) |
| | CD5L | CD5 antigen-like; Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflamed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. Able to inhibit lipid droplet size in adipocytes. Following incorporation into mature adipocytes via CD36- mediated endocytosis, associates with cytosolic FASN, inhibiting fatty acid synthase activity and leading to lipolysis, the degradation of triacylglycerols into glycerol and free fatty acids (FFA). CD5L-induced lipolysis occurs with progression o [...] (347 aa) |
| | PRSS38 | Serine protease 38. (326 aa) |
| | CTRB1 | Chymotrypsinogen B1; Belongs to the peptidase S1 family. (263 aa) |
| | PRSS3 | Trypsin-3; Digestive protease that cleaves proteins preferentially after an Arg residue and has proteolytic activity toward Kunitz-type trypsin inhibitors. Belongs to the peptidase S1 family. (304 aa) |
| | LONP1 | Lon protease homolog, mitochondrial; ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand- specific manner. May regulate mi [...] (959 aa) |
| | DPP4 | Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...] (766 aa) |
| | CELA2A | Chymotrypsin-like elastase family member 2A; Acts upon elastin. (269 aa) |
| | TLL2 | Tolloid-like protein 2; Protease which specifically processes pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. (1015 aa) |
| | TMPRSS11F | Transmembrane protease serine 11F; Probable serine protease; Belongs to the peptidase S1 family. (438 aa) |
| | HP | Haptoglobin alpha chain; As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity, and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. (406 aa) |
| | MBTPS1 | Membrane-bound transcription factor site-1 protease; Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg-Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysos [...] (1052 aa) |
| | TPSAB1 | Tryptase alpha/beta-1; Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates. (275 aa) |
| | CELA3B | Chymotrypsin-like elastase family member 3B; Efficient protease with alanine specificity but only little elastolytic activity. (270 aa) |
| | KLK5 | Kallikrein-5; May be involved in desquamation; Belongs to the peptidase S1 family. Kallikrein subfamily. (293 aa) |
| | TMPRSS11A | Transmembrane protease serine 11A; Probable serine protease which may play a role in cellular senescence. Overexpression inhibits cell growth and induce G1 cell cycle arrest. (421 aa) |
| | PRSS55 | Serine protease 55; Probable serine protease. (352 aa) |
| | TMPRSS11B | Transmembrane protease serine 11B; Serine protease. (416 aa) |
| | OVCH1 | Ovochymase-1; Ovochymase 1. (1134 aa) |
| | PRSS50 | Probable threonine protease PRSS50; May be involved in proteolysis through its threonine endopeptidase activity; Belongs to the peptidase S1 family. (385 aa) |
| | KLK4 | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). (254 aa) |
| | PCSK7 | Proprotein convertase subtilisin/kexin type 7; Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway. (785 aa) |
| | PARL | Presenilins-associated rhomboid-like protein, mitochondrial; Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals (By similarity). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Promotes changes in mitochondria morphology regulated by phosphorylation of P- beta domain. (379 aa) |
| | MMP1 | 22 kDa interstitial collagenase; Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. (469 aa) |
| | RHBDF2 | Inactive rhomboid protein 2; Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. Belongs to the peptidase S54 family. (856 aa) |
| | LPA | Apolipoprotein(a); Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330; Belongs to the peptidase S1 family. Plasminogen subfamily. (2040 aa) |
| | PRSS8 | Prostasin heavy chain; Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G). (343 aa) |
| | KLK3 | Prostate-specific antigen; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. (261 aa) |
| | KLK2 | Kallikrein-2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin; Belongs to the peptidase S1 family. Kallikrein subfamily. (261 aa) |
| | MMP19 | Matrix metalloproteinase-19; Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin. (508 aa) |
| | KLK10 | Kallikrein-10; Has a tumor-suppressor role for NES1 in breast and prostate cancer; Belongs to the peptidase S1 family. Kallikrein subfamily. (276 aa) |
| | PLG | Plasmin heavy chain A, short form; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invas [...] (810 aa) |
| | PRSS1 | Alpha-trypsin chain 1; Has activity against the synthetic substrates Boc-Phe-Ser- Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg- Mec. The single-chain form is more active than the two-chain form against all of these substrates; Belongs to the peptidase S1 family. (247 aa) |
| | F2 | Activation peptide fragment 1; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family. (622 aa) |
| | MMP14 | Matrix metalloproteinase-14; Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiog [...] (582 aa) |
| | PCSK1 | Neuroendocrine convertase 1; Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP; Belongs to the peptidase S8 family. Furin subfamily. (753 aa) |
| | TMPRSS11E | Transmembrane protease serine 11E non-catalytic chain; Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position. (423 aa) |
| | PRSS27 | Serine protease 27. (290 aa) |
| | HTRA4 | Serine protease HTRA4; Serine protease; Belongs to the peptidase S1C family. (476 aa) |
| | BMP1 | Bone morphogenetic protein 1; Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD). Responsible for the proteolytic activation of lysyl oxidase LOX. (986 aa) |
| | CTRB2 | Chymotrypsinogen B2; Belongs to the peptidase S1 family. (263 aa) |
| | HTRA3 | Serine protease HTRA3; Serine protease that cleaves beta-casein/CSN2 as well as several extracellular matrix (ECM) proteoglycans such as decorin/DCN, biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF- beta family proteins possibly indirectly by degradation of these ECM proteoglycans (By similarity). May act as a tumor suppressor. Negatively regulates, in vitro, trophoblast invasion during placental development and may be involved in the development of the placenta in vivo. May also have a role in ovarian development, granulosa cell differentiation and luteinization. [...] (453 aa) |
| | PCSK9 | Proprotein convertase subtilisin/kexin type 9; Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non- proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes t [...] (692 aa) |
| | KLK1 | Kallikrein-1; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin; Belongs to the peptidase S1 family. Kallikrein subfamily. (262 aa) |
| | PCSK4 | Proprotein convertase subtilisin/kexin type 4; Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues (By similarity). In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm capacitation, acrosome reaction and binding of sperm to zona pellucida (By similarity). Plays also a role in female fertility, involved in the regulation of trophoblast migration and placental development, may be throu [...] (755 aa) |
| | TMPRSS5 | Transmembrane protease serine 5; May play a role in hearing; Belongs to the peptidase S1 family. (457 aa) |
| | MMP3 | Stromelysin-1; Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase; Belongs to the peptidase M10A family. (477 aa) |
| | TPP1 | Tripeptidyl-peptidase 1; Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. (563 aa) |
| | C2 | Complement C2a fragment; Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase; Belongs to the peptidase S1 family. (752 aa) |
| | PRSS37 | Probable inactive serine protease 37; Plays a role in male fertility (By similarity). May have a role in sperm migration or binding to zona-intact eggs (By similarity). Involved in the activation of the proacrosin/acrosin system ; Belongs to the peptidase S1 family. (235 aa) |
| | PRSS12 | Neurotrypsin; Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations; Belongs to the peptidase S1 family. (875 aa) |
| | APEH | Acylamino-acid-releasing enzyme; This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser; Belongs to the peptidase S9C family. (732 aa) |
| | MASP1 | Mannan binding lectin serine peptidase 1. (728 aa) |
| | PRSS33 | Serine protease 33; Serine protease that has amidolytic activity, cleaving its substrates before Arg residues. (280 aa) |
| | CELA1 | Chymotrypsin-like elastase family member 1; Acts upon elastin. (258 aa) |
| | CELA3A | Chymotrypsin-like elastase family member 3A; Efficient protease with alanine specificity but only little elastolytic activity; Belongs to the peptidase S1 family. Elastase subfamily. (270 aa) |
| | RHBDL2 | Rhomboid-related protein 2, C-terminal fragment; Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Known substrate: EFNB3; Belongs to the peptidase S54 family. (303 aa) |
| | TYSND1 | Peroxisomal leader peptide-processing protease, 15 kDa form; Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids. (566 aa) |
| | LONP2 | Lon protease homolog 2, peroxisomal; ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import (By similarity). May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1. (852 aa) |
| | TMPRSS15 | Enteropeptidase non-catalytic heavy chain; Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. (1019 aa) |
| | TMPRSS11D | Transmembrane protease serine 11D non-catalytic chain; May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) spike glycoprotein which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create s [...] (418 aa) |
| | PRSS53 | Serine protease 53; In vitro can degrade the fibrinogen alpha chain of as well as pro-urokinase-type plasminogen activator. (553 aa) |
| | PRSS23 | Serine protease 23; Belongs to the peptidase S1 family. (383 aa) |
| | MMP10 | Stromelysin-2; Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase; Belongs to the peptidase M10A family. (476 aa) |
| | ST14 | Suppressor of tumorigenicity 14 protein; Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing. (855 aa) |
| | IMMP1L | Mitochondrial inner membrane protease subunit 1; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO. (166 aa) |
| | HABP2 | Hyaluronan-binding protein 2 27 kDa light chain alternate form; Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII. May function as a tumor suppressor negatively regulating cell proliferation and c [...] (560 aa) |
| | GZMA | Granzyme A; Abundant protease in the cytosolic granules of cytotoxic T- cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA. Belongs to the peptidase S1 family. Granzym [...] (262 aa) |
| | CORIN | Atrial natriuretic peptide-converting enzyme, activated protease fragment; Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB [...] (1042 aa) |
| | CTSK | Cathepsin K; Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. (329 aa) |
| | RHBDL3 | Rhomboid-related protein 3; May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors; Belongs to the peptidase S54 family. (404 aa) |
| | AZU1 | Azurocidin; This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram- negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this [...] (251 aa) |
| | LTF | Lactotransferrin; Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG- binding site. Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows pr [...] (710 aa) |
| | GZMK | Granzyme K; Belongs to the peptidase S1 family. Granzyme subfamily. (264 aa) |
| | CTSC | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. (463 aa) |
| | PLAT | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration; Belongs to the peptidase S1 family. (562 aa) |
| | CTSH | Cathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family. (335 aa) |
| | RHBDL1 | Rhomboid-related protein 1; May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. (438 aa) |
| | PRSS54 | Serine protease 54. (395 aa) |
| | MMP2 | 72 kDa type IV collagenase; Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta- type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3 [...] (660 aa) |
| | F9 | Coagulation factor IXa heavy chain; Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. Belongs to the peptidase S1 family. (461 aa) |
| | GZMB | Granzyme B; This enzyme is necessary for target cell lysis in cell- mediated immune responses. It cleaves after Asp. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis; Belongs to the peptidase S1 family. Granzyme subfamily. (247 aa) |
| | GZMH | Granzyme H; Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication. (246 aa) |
| | CTSG | Cathepsin G; Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe-CH2Cl and phenylmethylsulfonyl fluoride. (255 aa) |
| | ACR | Acrosin heavy chain; Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome. (421 aa) |
| | PRSS36 | Polyserase-2; Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg- AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala- Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1; Belongs to the peptidase S1 family. (855 aa) |
| | C1RL | Complement C1r subcomponent-like protein; Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum; Belongs to the peptidase S1 family. (487 aa) |
| | KLKB1 | Plasma kallikrein heavy chain; The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin; Belongs to the peptidase S1 family. Plasma kallikrein subfamily. (638 aa) |
| | GZMM | Granzyme M; Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells. (257 aa) |
| | HPN | Serine protease hepsin non-catalytic chain; Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2. Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization. Belongs to the peptidase S1 family. (417 aa) |
| | PCSK2 | Neuroendocrine convertase 2; Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Responsible for the release of glucagon from proglucagon in pancreatic A cells; Belongs to the peptidase S8 family. Furin subfamily. (638 aa) |
| | RHBDF1 | Inactive rhomboid protein 1; Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. (855 aa) |
| | MMP13 | Collagenase 3; Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bon [...] (471 aa) |
| | MMP7 | Matrilysin; Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. (267 aa) |
| | CTSV | Cathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family. (334 aa) |
| | RHBDD3 | Rhomboid domain containing 3. (386 aa) |
| | MMP11 | Stromelysin-3; May play an important role in the progression of epithelial malignancies. (488 aa) |
| | TPSD1 | Tryptase delta; Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type; Belongs to the peptidase S1 family. Tryptase subfamily. (242 aa) |
| | FAP | Antiplasmin-cleaving enzyme FAP, soluble form; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, [...] (760 aa) |
| | PRSS22 | Brain-specific serine protease 4; Preferentially cleaves the synthetic substrate H-D-Leu-Thr- Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. (317 aa) |
| | TLL1 | Tolloid-like protein 1; Protease which processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. (1013 aa) |
| | RHBDD2 | Rhomboid domain containing 2; Belongs to the peptidase S54 family. (364 aa) |
| | PRSS21 | Testisin; Could regulate proteolytic events associated with testicular germ cell maturation. (314 aa) |
| | HTRA2 | Serine protease HTRA2, mitochondrial; Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase- independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive; Belongs to the peptidase S1C family. (458 aa) |
| | F12 | Coagulation factor XIIa heavy chain; Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa. (615 aa) |
| | CMA1 | Chymase; Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. (247 aa) |
| | KLK12 | Kallikrein-12; Kallikrein related peptidase 12; Belongs to the peptidase S1 family. Kallikrein subfamily. (254 aa) |
| | CLPP | ATP-dependent Clp protease proteolytic subunit, mitochondrial; Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion. (277 aa) |
| | MMP8 | Neutrophil collagenase; Can degrade fibrillar type I, II, and III collagens; Belongs to the peptidase M10A family. (467 aa) |
| | TPSG1 | Tryptase gamma 1. (321 aa) |
| | PRTN3 | Myeloblastin; Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177. Belongs to the peptidase S1 family. Elastase subfamily. (256 aa) |
| | PROC | Vitamin K-dependent protein C heavy chain; Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function ; Belongs to the peptidase S1 family. (461 aa) |
