ID X0D615_FUSOX Unreviewed; 742 AA.
AC X0D615;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN ORFNames=FOQG_01451 {ECO:0000313|EMBL:EXK98584.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK98584.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK98584.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK98584.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH658363; EXK98584.1; -; Genomic_DNA.
DR AlphaFoldDB; X0D615; -.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_011862_1_0_1; -.
DR Proteomes; UP000030663; 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; 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; 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:UP000030663};
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..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 81598 MW; AA65676A465744ED CRC64;
MMSWWSSSAN TALDEQIEKA TSSSLEDIAL NLEISDVIRS KTVAPKEAMR SLKKRIGNRN
PNTQLSALNL TDTCVKNGGS HFLAEVASRE FMDNLVSLLQ AVGGGAVNSD VKTKILELIQ
SWAGATEGRY ELSYIGEVYR TLQRDGYQFP PKISVASSMI DSSAPPEWTD SDVCMRCRTP
FTFTNRKHHC RNCGNCFDQQ CSAKVVALPH LGIMTPVRVD DGCYAKLTNK GHKIPNPSLD
RSPTYPHKTR STSAMQPRNA RVDDGFDEDL KKALAMSLEE VKTHSHGYAG PAQTSYATNG
DASAAKQAEE DDADLKAAIA ASLADMEEQK KRHAAALKEQ TSSSMDASAT TNFVLPKNDY
ELTPVEAENI NLFSTLVDRL QTQPPGTILR EPQIQELYDS IGTLRPKLAR TYGETMSKHD
TLLDLHAKLS TVVRYYDRML EDRLSKAYSQ QNLGGYNLPP PRQAAGPYPS IPSQMPSNPA
GAESFYTGQQ RASYQAPQHQ HYQQPPPHAT PQPQYPSYGS APEAQPGQYP PPQQVQRTDS
WQNRAPSAPQ DPYQQQQQQP QKPNDPNLQT QNPQQPQAPN ASDPNASYYF TPQQPQQTPL
GPSAPGSAPD ANQSPYPNLQ QPSQYPGGSV SAPSQPTPGQ APAQVAQPVQ PVQTPQQPVQ
SPHMQHAQPP QPPQPQPPQP TQQAPPPQQQ AYWQPSMPQS HQQPPVAPQN WAYGGYTQDS
FPSVPQQEPV KQPVKEEALI EF
//
