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Database: UniProt
Entry: A0A1Y2LUT7_EPING
LinkDB: A0A1Y2LUT7_EPING
Original site: A0A1Y2LUT7_EPING 
ID   A0A1Y2LUT7_EPING        Unreviewed;       761 AA.
AC   A0A1Y2LUT7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN   ORFNames=B5807_10065 {ECO:0000313|EMBL:OSS47329.1};
OS   Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX   NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS47329.1, ECO:0000313|Proteomes:UP000193240};
RN   [1] {ECO:0000313|EMBL:OSS47329.1, ECO:0000313|Proteomes:UP000193240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS47329.1,
RC   ECO:0000313|Proteomes:UP000193240};
RA   Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT   "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT   strain isolated from New Zealand.";
RL   Genome Announc. 0:0-0(2017).
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|ARBA:ARBA00003067, ECO:0000256|PIRNR:PIRNR036956}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC       {ECO:0000256|ARBA:ARBA00011446, 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; KZ107849; OSS47329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2LUT7; -.
DR   STRING; 105696.A0A1Y2LUT7; -.
DR   InParanoid; A0A1Y2LUT7; -.
DR   OMA; DQQCSAK; -.
DR   OrthoDB; 922060at2759; -.
DR   Proteomes; UP000193240; Unassembled WGS sequence.
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; cd15735; FYVE_spVPS27p_like; 1.
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; 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 {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:UP000193240};
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          26..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..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..539
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..567
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..702
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  84322 MW;  7D7D6F7AD66623B1 CRC64;
     MAGWFGSSTN SALDEQIERA TTSSLEDMPL NLEISDVIRS KTVQPKDAMR SLKKRIGHKN
     PNVQLAALNL TDTCVKNGGA HFIQEIASRE FLDNMTSLMK APGSAGANHD VRNKMLELIQ
     SWATAAEGRS NLSYINEVYR GLQREGYQFP PRENISSSML DSSAPPEWTD SDVCMRCRTA
     FTFTNRKHHC RNCGNVFCGA CSSNSIPLPH LGIMDPVRVD DGCHAKLTDR SRANTFAPAP
     PRFDAPQPSK TLYQGSMEPR NPRVEDSFDA DLKRALEMSL EDAKGNSSSG FVPQAQLKSQ
     SKPNGTAKKP EPELELDADL EAAIAASLAD MEEQKKKYAT DFRQQATSSS SGTPFVAPKN
     DFELSPVEAE NINLFSTLVD RLQHQPPGAI LREPQIQELY ESIGKLRPKL ARTYGETMSK
     HETLLDLHAK LSTVVRYYDR MLEERLSSTY NPAGAMYGMP RPTSNVYPQI PSGAPAYTGS
     ENYYSSNPTP SDPYGRPQPT YQSQPQQPYP QFDQHAPPPQ SYASPDPYQQ QPQPQQPSQP
     YPNLASYGAG APPQQQPPQP SYQQPPSPQL QRQPSTQYSQ QPPSGYQSQA PPSNVSDTEG
     ANYYYNDSAP TPLQRTQSYT SQPPQSSSPQ LYSHAPPQHH QQQQAPISPP EQPATAWQNP
     PYPQGNAPPQ QHQQQAPPPQ QQQQAPPQHQ QQAPPPQQQW QPPPQQQQQQ QQQQPPPLQQ
     QQSNWNPATP YAMGGYGPES FPSAPQAAPQ PLRAEEPLID L
//
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