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ERO1L ERO1L CANX CANX CALR CALR PGAP1 PGAP1 TMX2 TMX2 TXNDC11 TXNDC11 PDILT PDILT CLGN CLGN CALR3 CALR3 ADAM2 ADAM2 TPST2 TPST2
"PDILT" - protein disulfide isomerase-like, testis expressed in Homo sapiens
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PDILTprotein disulfide isomerase-like, testis expressed; Probable redox-inactive chaperone involved in spermatogenesis (584 aa)    
Predicted Functional Partners:
CLGN
calmegin; Probably plays an important role in spermatogenesis. Binds calcium ions (610 aa)
      score_image score_image   score_image   0.963
CALR3
calreticulin 3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR (384 aa)
      score_image score_image   score_image   0.952
CALR
calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity) (417 aa)
      score_image score_image   score_image   0.932
ERO1L
ERO1-like (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of g [...] (468 aa)
        score_image   score_image   0.891
ADAM2
ADAM metallopeptidase domain 2; Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein (735 aa)
            score_image   0.884
CANX
calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] (592 aa)
      score_image score_image   score_image   0.726
TXNDC11
thioredoxin domain containing 11; May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation (958 aa)
      score_image score_image   score_image   0.694
TPST2
tyrosylprotein sulfotransferase 2; Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides (377 aa)
            score_image   0.653
TMX2
thioredoxin-related transmembrane protein 2 (296 aa)
            score_image   0.647
PGAP1
post-GPI attachment to proteins 1; Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi (By similarity) (922 aa)
            score_image   0.644
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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