GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Catalytic subunit of mitochondrial inner membrane peptidase complex; required for maturation of mitochondrial proteins of the intermembrane space; complex contains two catalytic subunits (Imp1p and Imp2p that differ in substrate specificty) and Som1p.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Maintenance of telomere capping protein 5; Subunit of SEACAT, a subcomplex of the SEA complex; Mtc1p, along with Rtc1p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; relative distribution to the vacuolar membrane decreases upon DNA replication stress.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Nitrogen permease regulator 2; Subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Npr2p may have a structural or regulatory role, supporting Iml1p function as a GAP for the Rag family GTPase Gtr1p, and resulting in inhibition of TORC1 signaling in response to amino acid deprivation; SEACIT is required for non-nitrogen-starvation-induced autophagy; homolog of human tumor suppressor NPRL2.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Nitrogen permease regulator 3; Subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of SEAC, a coatomer-related complex that associates dynamically with the vacuole; Npr3p may have a structural or regulatory role, supporting Iml1p function as a GAP for the Rag family GTPase Gtr1p, and leading to inhibition of TORC1 signaling in response to amino acid deprivation; SEACIT is required for non-nitrogen-starvation-induced autophagy; null mutant has meiotic defects; human NPRL3 homolog.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Restriction of telomere capping protein 1; Subunit of SEACAT, a subcomplex of the SEA complex; Rtc1p, along with Mtc5p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; has N-terminal WD-40 repeats and a C-terminal RING motif; null suppresses cdc13-1.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

SEH-associated protein 4; Subunit of SEACAT, a subcomplex of the SEA complex; Sea4p, along with Rtc1p and Mtc5p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; contains an N-terminal beta-propeller fold and a C-terminal RING motif.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Protein transport protein SEC13; Structural component of 3 complexes; subunit of the Nup84p nuclear pore subcomplex that contributes to nucleocytoplasmic transport and NPC biogenesis; subunit of the COPII vesicle coat required for ER-to-Golgi transport; subunit of SEACAT, a subcomplex of the coatomer-related, vacuolar-associated SEA complex, that inhibits the TORC1 inhibitory role of SEACIT (Iml1p-Npr2p-Npr3p), a GAP for Gtr1p, thereby resulting in activation of TORC1 signaling; human SEC13 homolog.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Nucleoporin SEH1; Subunit of the Nup84 nuclear pore and SEACAT subcomplexes; involved in nucleocytoplasmic transport and NPC biogenesis in the nuclear pore subcomplex; subunit of SEACAT, a subcomplex of the SEA complex that inhibits the TORC1 inhibitory role of SEACIT (Iml1p-Npr2p-Npr3p), a GAP for Gtr1p in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; human SEH1 homolog.

Catalytic subunit of mitochondrial inner membrane peptidase complex; required for maturation of mitochondrial proteins of the intermembrane space; complex contains two catalytic subunits (Imp1p and Imp2p that differ in substrate specificty) and Som1p.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Catalytic subunit of mitochondrial inner membrane peptidase complex; required for maturation of mitochondrial proteins of the intermembrane space; complex contains two catalytic subunits (Imp1p and Imp2p that differ in substrate specificty) and Som1p.

Maintenance of telomere capping protein 5; Subunit of SEACAT, a subcomplex of the SEA complex; Mtc1p, along with Rtc1p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; relative distribution to the vacuolar membrane decreases upon DNA replication stress.

Catalytic subunit of mitochondrial inner membrane peptidase complex; required for maturation of mitochondrial proteins of the intermembrane space; complex contains two catalytic subunits (Imp1p and Imp2p that differ in substrate specificty) and Som1p.

Nitrogen permease regulator 2; Subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Npr2p may have a structural or regulatory role, supporting Iml1p function as a GAP for the Rag family GTPase Gtr1p, and resulting in inhibition of TORC1 signaling in response to amino acid deprivation; SEACIT is required for non-nitrogen-starvation-induced autophagy; homolog of human tumor suppressor NPRL2.

Catalytic subunit of mitochondrial inner membrane peptidase complex; required for maturation of mitochondrial proteins of the intermembrane space; complex contains two catalytic subunits (Imp1p and Imp2p that differ in substrate specificty) and Som1p.

Restriction of telomere capping protein 1; Subunit of SEACAT, a subcomplex of the SEA complex; Rtc1p, along with Mtc5p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; has N-terminal WD-40 repeats and a C-terminal RING motif; null suppresses cdc13-1.

Subunit of the Lst4p-Lst7p GTPase activating protein complex for Gtr2p; stimulates the GTPase activity of Rag family GTPase Gtr2p, within the context of the Gtr1p-Gtr2p heterodimer, after amino acid stimulation; required for activation of TORC1 in response to amino acid stimulation; recruited to the vacuolar membrane during amino acid starvation and released from the membrane by TORC1; required for the transport of amino acid permease Gap1p from the Golgi to the cell surface.

Maintenance of telomere capping protein 5; Subunit of SEACAT, a subcomplex of the SEA complex; Mtc1p, along with Rtc1p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; relative distribution to the vacuolar membrane decreases upon DNA replication stress.

Subunit of the Lst4p-Lst7p GTPase activating protein complex for Gtr2p; stimulates the GTPase activity of Rag family GTPase Gtr2p, within the context of the Gtr1p-Gtr2p heterodimer, after amino acid stimulation; required for activation of TORC1 in response to amino acid stimulation; recruited to the vacuolar membrane during amino acid starvation and released from the membrane by TORC1; required for the transport of amino acid permease Gap1p from the Golgi to the cell surface.

Nitrogen permease regulator 3; Subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of SEAC, a coatomer-related complex that associates dynamically with the vacuole; Npr3p may have a structural or regulatory role, supporting Iml1p function as a GAP for the Rag family GTPase Gtr1p, and leading to inhibition of TORC1 signaling in response to amino acid deprivation; SEACIT is required for non-nitrogen-starvation-induced autophagy; null mutant has meiotic defects; human NPRL3 homolog.

Subunit of the Lst4p-Lst7p GTPase activating protein complex for Gtr2p; stimulates the GTPase activity of Rag family GTPase Gtr2p, within the context of the Gtr1p-Gtr2p heterodimer, after amino acid stimulation; required for activation of TORC1 in response to amino acid stimulation; recruited to the vacuolar membrane during amino acid starvation and released from the membrane by TORC1; required for the transport of amino acid permease Gap1p from the Golgi to the cell surface.

Restriction of telomere capping protein 1; Subunit of SEACAT, a subcomplex of the SEA complex; Rtc1p, along with Mtc5p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; has N-terminal WD-40 repeats and a C-terminal RING motif; null suppresses cdc13-1.

Subunit of the Lst4p-Lst7p GTPase activating protein complex for Gtr2p; stimulates the GTPase activity of Rag family GTPase Gtr2p, within the context of the Gtr1p-Gtr2p heterodimer, after amino acid stimulation; required for activation of TORC1 in response to amino acid stimulation; recruited to the vacuolar membrane during amino acid starvation and released from the membrane by TORC1; required for the transport of amino acid permease Gap1p from the Golgi to the cell surface.

SEH-associated protein 4; Subunit of SEACAT, a subcomplex of the SEA complex; Sea4p, along with Rtc1p and Mtc5p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; contains an N-terminal beta-propeller fold and a C-terminal RING motif.

Subunit of the Lst4p-Lst7p GTPase activating protein complex for Gtr2p; stimulates the GTPase activity of Rag family GTPase Gtr2p, within the context of the Gtr1p-Gtr2p heterodimer, after amino acid stimulation; required for activation of TORC1 in response to amino acid stimulation; recruited to the vacuolar membrane during amino acid starvation and released from the membrane by TORC1; required for the transport of amino acid permease Gap1p from the Golgi to the cell surface.

Protein transport protein SEC13; Structural component of 3 complexes; subunit of the Nup84p nuclear pore subcomplex that contributes to nucleocytoplasmic transport and NPC biogenesis; subunit of the COPII vesicle coat required for ER-to-Golgi transport; subunit of SEACAT, a subcomplex of the coatomer-related, vacuolar-associated SEA complex, that inhibits the TORC1 inhibitory role of SEACIT (Iml1p-Npr2p-Npr3p), a GAP for Gtr1p, thereby resulting in activation of TORC1 signaling; human SEC13 homolog.

Subunit of the Lst4p-Lst7p GTPase activating protein complex for Gtr2p; stimulates the GTPase activity of Rag family GTPase Gtr2p, within the context of the Gtr1p-Gtr2p heterodimer, after amino acid stimulation; required for activation of TORC1 in response to amino acid stimulation; recruited to the vacuolar membrane during amino acid starvation and released from the membrane by TORC1; required for the transport of amino acid permease Gap1p from the Golgi to the cell surface.

Protein SLM4; Component of the EGO and GSE complexes; essential for integrity and function of EGO; EGO is involved in the regulation of microautophagy and GSE is required for proper sorting of amino acid permease Gap1p; gene exhibits synthetic genetic interaction with MSS4.

Maintenance of telomere capping protein 5; Subunit of SEACAT, a subcomplex of the SEA complex; Mtc1p, along with Rtc1p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; relative distribution to the vacuolar membrane decreases upon DNA replication stress.

GTPase-activating protein (GAP) subunit of the Iml1p/SEACIT complex; SEACIT (Iml1p-Npr2p-Npr3p) is a subcomplex of the SEA complex, a coatomer-related complex that associates dynamically with the vacuole; Iml1p functions in the SEACIT complex as a GAP for the Rag family GTPase Gtr1p (EGOC subunit), resulting in the inhibition of TORC1 signaling in response to amino acid deprivation; the Iml1p/SEACIT complex is required for non-nitrogen-starvation (NNS)-induced autophagy.

Maintenance of telomere capping protein 5; Subunit of SEACAT, a subcomplex of the SEA complex; Mtc1p, along with Rtc1p and Sea4p, redundantly inhibit the TORC1 inhibitory role of the Iml1p/SEACIT (Iml1p-Npr2p-Npr3p) subcomplex, a GAP for GTPase Gtr1p (EGOC subunit) in response to amino acid limitation, thereby resulting in activation of TORC1 signaling; SEA is a coatomer-related complex that associates dynamically with the vacuole; relative distribution to the vacuolar membrane decreases upon DNA replication stress.

Catalytic subunit of mitochondrial inner membrane peptidase complex; required for maturation of mitochondrial proteins of the intermembrane space; complex contains two catalytic subunits (Imp1p and Imp2p that differ in substrate specificty) and Som1p.