VPS27_YARLI
ID VPS27_YARLI Reviewed; 565 AA.
AC Q6CFT4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=VPS27; OrderedLocusNames=YALI0B04070g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382128; CAG82705.1; -; Genomic_DNA.
DR RefSeq; XP_500478.1; XM_500478.1.
DR AlphaFoldDB; Q6CFT4; -.
DR SMR; Q6CFT4; -.
DR STRING; 4952.CAG82705; -.
DR EnsemblFungi; CAG82705; CAG82705; YALI0_B04070g.
DR GeneID; 2906618; -.
DR KEGG; yli:YALI0B04070g; -.
DR VEuPathDB; FungiDB:YALI0_B04070g; -.
DR HOGENOM; CLU_011862_2_1_1; -.
DR InParanoid; Q6CFT4; -.
DR OMA; SDMVRSK; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:1904669; P:ATP export; IEA:EnsemblFungi.
DR GO; GO:0140504; P:microlipophagy; 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; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
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 Pfam; PF01363; FYVE; 1.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF00790; VHS; 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; SSF48464; 1.
DR SUPFAM; SSF57903; SSF57903; 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..565
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292525"
FT DOMAIN 19..148
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 262..281
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 293..312
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 170..230
FT /note="FYVE-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 565 AA; 60936 MW; 817D34564A8D3BCC CRC64;
MSWWSSTPSI DEQVEKATSE SLPSGESDLA LNLEICDLIR SKTVPAKDAM RSLKRRLLNR
NPNVQLAALQ LTDVCIKNGG SHFLVEIASR EFVDPLMAIA RNDDANPEVR QRVLQLLQQW
AVAFAGQLQL QQVENAVTQL KSEGVSFPSA SHDNAAVTST FIDTKAPPEW IDSDVCMESG
VAFSFLNRKH HCRNCGGVFT QACCQNYITL PHFGINVPVR VCNGCFKNLK KGKSDAPIHK
PVPGATTTAP SSAPPANSAP NDDEDDIQKA IRLSLQEQES YKPPPPAAAT SNDDDEDMKA
AIAASLRDME NERQTGQTSA SAGGLSSAST TVMAPSLTDL TATEESNINL LSLLVERLKG
EPQGTILREP KIQELYDTVG NLRPKLARTM GETISKYDSL VDMHAKMTTV IRYYDALLEE
KLNQAYTNRQ SGGYAPQPHL SHQMTGQPPH LAPHLTGQIT GQPHMGYQHT GQAPYLTGQV
TGQAPYLSNQ PTGHLTNHYT GSAPSAPQYG GPPAQNVYNA PSYQYSGAPE YDYASSPSAP
SAPGGPSAPS APAQPKEESA PLIEL
