ID A0A167C393_9ASCO Unreviewed; 586 AA.
AC A0A167C393;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN Name=VPS27 {ECO:0000313|EMBL:ANB11165.1};
GN ORFNames=AWJ20_3966 {ECO:0000313|EMBL:ANB11165.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB11165.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB11165.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB11165.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC receptor for ubiquitinated cargo proteins at the multivesicular body
CC (MVB) and recruits ESCRT-I to the MVB outer membrane.
CC {ECO:0000256|PIRNR:PIRNR036956}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC {ECO:0000256|PIRNR:PIRNR036956}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004125,
CC ECO:0000256|PIRNR:PIRNR036956}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125, ECO:0000256|PIRNR:PIRNR036956};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125,
CC ECO:0000256|PIRNR:PIRNR036956}. 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 VPS27 family.
CC {ECO:0000256|ARBA:ARBA00008597, ECO:0000256|PIRNR:PIRNR036956}.
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DR EMBL; CP014500; ANB11165.1; -; Genomic_DNA.
DR RefSeq; XP_018733642.1; XM_018881008.1.
DR AlphaFoldDB; A0A167C393; -.
DR GeneID; 30036045; -.
DR KEGG; slb:AWJ20_3966; -.
DR OrthoDB; 922060at2759; -.
DR Proteomes; UP000189580; Chromosome c.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProt.
DR CDD; cd16979; VHS_Vps27; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 6.10.140.100; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR InterPro; IPR049425; Vps27_GAT-like.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF00790; VHS; 1.
DR Pfam; PF21356; Vps27_GAT-like; 1.
DR PIRSF; PIRSF036956; Hrs_Vps27; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00726; UIM; 3.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|PIRNR:PIRNR036956};
KW Membrane {ECO:0000256|PIRNR:PIRNR036956};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189580};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 19..150
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 168..228
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 230..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 65655 MW; 866FE0ADB6756328 CRC64;
MSWFSSVVSI DERIEKATSE SLPSGEQDLA LNLEICDLIR SKTVPPKDAM RSLKKRLNHK
NPNVQLLTLH LIDICIKNGG SHFLTEIASR EFMDSFVSVL QPSSGLVNRD VKELMLEYLQ
NWANAFEGQI QLVYVNKVYE KLKKDGFHFP SGAKISSSFI DSSAPPEWVD ADECMECNTP
FSFVNRKHHC RNCGGVYIQK HCNNYTTLPH YGINQPVRVC DSCFNKLRGS SSGGPSSRVH
NSNDQVRSHT TSNNRDLSSV DDDNDSDLQR ALKLSLEESQ NPGLTKPSPN RAPTNHLVQN
DDDDEDMKAA IAASLRDMEN EGKAIPSGTD TTNPSNNLYQ LAPPSVSIAD VEPKSVENTV
LSIVDDEFTS VDAEIIHRYV QIVESLQRNP SAFAIRDTKL ELLHNNVLSL RPKLSKDLRR
TVEKCDQLED LHGKLTAIVR YYDKLLEDRF SYSMKKYGHM DEGNQYTSSV VSSQMPGGQY
HQYQTGSGPV TYPEGNSPYY PPVQDSDPHY GVNTETYYQQ QHDGPLPSEP PLPEGNAGYQ
GFYPALDERG NISQNQSIQD PDNQSSEPNY SKPGTKEEEE PILIEL
//
