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Database: UniProt
Entry: C5M4H7_CANTT
LinkDB: C5M4H7_CANTT
Original site: C5M4H7_CANTT 
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
//
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