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Database: UniProt
Entry: VPS27_CANGA
LinkDB: VPS27_CANGA
Original site: VPS27_CANGA 
ID   VPS27_CANGA             Reviewed;         603 AA.
AC   Q6FQJ1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Vacuolar protein sorting-associated protein 27;
GN   Name=VPS27; OrderedLocusNames=CAGL0I05830g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- DOMAIN: The FYVE domain is involved in the binding to
CC       phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the
CC       association to endosomal membranes.
CC   -!- DOMAIN: Both IUM domains are necessary for efficient binding to
CC       ubiquitin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS27 family. {ECO:0000305}.
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DR   EMBL; CR380955; CAG60440.1; -; Genomic_DNA.
DR   RefSeq; XP_447503.1; XM_447503.1.
DR   AlphaFoldDB; Q6FQJ1; -.
DR   SMR; Q6FQJ1; -.
DR   STRING; 284593.Q6FQJ1; -.
DR   EnsemblFungi; CAGL0I05830g-T; CAGL0I05830g-T-p1; CAGL0I05830g.
DR   GeneID; 2889348; -.
DR   KEGG; cgr:CAGL0I05830g; -.
DR   CGD; CAL0132704; VPS27.
DR   VEuPathDB; FungiDB:CAGL0I05830g; -.
DR   eggNOG; KOG1818; Eukaryota.
DR   HOGENOM; CLU_011862_2_0_1; -.
DR   InParanoid; Q6FQJ1; -.
DR   OMA; RTAFSFM; -.
DR   Proteomes; UP000002428; Chromosome I.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
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:0006886; P:intracellular protein transport; IEA:UniProt.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IEA:EnsemblFungi.
DR   GO; GO:0140504; P:microlipophagy; 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:0045053; P:protein retention in Golgi apparatus; 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; cd21385; GAT_Vps27; 1.
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; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00726; UIM; 2.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50330; UIM; 2.
DR   PROSITE; PS50179; VHS; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..603
FT                   /note="Vacuolar protein sorting-associated protein 27"
FT                   /id="PRO_0000292512"
FT   DOMAIN          18..149
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          254..273
FT                   /note="UIM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          292..311
FT                   /note="UIM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         170..230
FT                   /note="FYVE-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          233..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ   SEQUENCE   603 AA;  68711 MW;  095F5ECF6B9E51E9 CRC64;
     MATTSSEEFS EVIERATSES IPNGELNLPV ALEISDILRS RRIAPKDGMR CLKKRITNTT
     NNPNTQLSSW KLVEICIKNG GIPFLREICS REFMDTMEHT ILKYDDSDEV VELVTTMLYE
     LYLAFQNDSQ LNYVSRVYDK LRQRGVKFPE GAPISSNVNA LFDSKTPADW IDSDACMICS
     KKFSLLNRRH HCRSCGGVFC QDHSSKSIPL PDLGIYDSVR VCDNCYDDYD YKKGSGSQGK
     KRKHRKSHRH ATEDEDEDLR KAIELSLRAS NSSVEPVIPV VESEPQIPAV EEEDPDLKAA
     IEASLREAEE EKRRREEHAQ QQNTNAYPQQ FRPPANELTP ADEEDIYLFA SLVERMKTRP
     PSEILDDPQL QQLAQKVFAS KPRLGNTLNS KIQKYNTLVD MNGKISHIMN TYDNLLEQEL
     RNINLSERFN VPQAQADPYS QYSQYNQPAI QNNTSQTNNV VNNKPLSQRE SEPQYTAPTD
     SQTIESKAYE RQLENLVQPP SNVNNERVAS EPPYPNEELN DITSIQLNSE RAGKYEENAV
     PPGSIPYPIE NDDQDETTRT KKNDNITNFD FPTVPARKLP ENNVEQVEDK PQDSQEEALL
     IEL
//
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