ID C5M4H7_CANTT Unreviewed; 481 AA.
AC C5M4H7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1 {ECO:0000256|ARBA:ARBA00017923};
DE AltName: Full=Class E vacuolar protein-sorting machinery protein hse1 {ECO:0000256|ARBA:ARBA00018978};
GN ORFNames=CTRG_00967 {ECO:0000313|EMBL:EER36227.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER36227.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER36227.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC receptor for ubiquitinated cargo proteins at the multivesicular body
CC (MVB). {ECO:0000256|ARBA:ARBA00002654}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the STAM family.
CC {ECO:0000256|ARBA:ARBA00009666}.
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DR EMBL; GG692395; EER36227.1; -; Genomic_DNA.
DR RefSeq; XP_002546185.1; XM_002546139.1.
DR AlphaFoldDB; C5M4H7; -.
DR STRING; 294747.C5M4H7; -.
DR EnsemblFungi; CTRG_00967-t43_1; CTRG_00967-t43_1-p1; CTRG_00967.
DR GeneID; 8297277; -.
DR KEGG; ctp:CTRG_00967; -.
DR VEuPathDB; FungiDB:CTRG_00967; -.
DR eggNOG; KOG2199; Eukaryota.
DR HOGENOM; CLU_010104_2_0_1; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IEA:EnsemblFungi.
DR GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IEA:EnsemblFungi.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblFungi.
DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:1904669; P:ATP export; IEA:EnsemblFungi.
DR GO; GO:0030447; P:filamentous growth; IEA:UniProt.
DR GO; GO:0045324; P:late endosome to vacuole transport; IEA:EnsemblFungi.
DR GO; GO:0016237; P:lysosomal microautophagy; IEA:EnsemblFungi.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:EnsemblFungi.
DR GO; GO:1903319; P:positive regulation of protein maturation; IEA:EnsemblFungi.
DR GO; GO:0009306; P:protein secretion; IEA:EnsemblFungi.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:EnsemblFungi.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR CDD; cd11805; SH3_GRB2_like_C; 1.
DR CDD; cd16978; VHS_HSE1; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR PANTHER; PTHR45929:SF3; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 11..142
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 213..273
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 141..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..362
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 481 AA; 54584 MW; 499C4688D52126D8 CRC64;
MPSLESLINK ATDPTLTSDN WQYIFDVCDK ISNDPETATK EAIATLKTKL ASKDANVVLR
TLALLTAVAE NCGSRVKQEI ATKSFLQDCL IKRLSDKKLH PAVKTKICEV LSQLYNTFKV
DPSLKPMTDA YNKAKHDYPQ YFNKKVEGPS KPAKKERTKQ DKDREEEELQ RALKLSLHEY
EQQSKIEKKE YLNNKPLPEP KPEPESPPVE TVATVSKVRA LYDLISYEPD ELSFRKGDVI
TVIESVYRDW WRGSLTNGKV GIFPLNYVTP IVNKSPAEIA KELELENRLI NGEKKKIEKL
LAILSSQNID NINEDEVTSL YNEIIPLRIQ LGAAIDKYSV RKEELLGLNQ QLNNEVKLYN
ELLDKSISSR AQQNTGGLMY QQTAPYPMQQ QQHQGPSQTQ QSQIPQQHTQ SQQLPPQYTQ
SQPLHQQQQQ YSGYAGANNM PPPATTFNQY VPPQLQELQP QETSAGFGNA VYNRPQPTSQ
Q
//