ID M1W702_CLAP2 Unreviewed; 746 AA.
AC M1W702;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN ORFNames=CPUR_01955 {ECO:0000313|EMBL:CCE35027.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE35027.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE35027.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE35027.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCE35027.1}.
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DR EMBL; CAGA01000189; CCE35027.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W702; -.
DR STRING; 1111077.M1W702; -.
DR VEuPathDB; FungiDB:CPUR_01955; -.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_011862_1_0_1; -.
DR OrthoDB; 922060at2759; -.
DR PhylomeDB; M1W702; -.
DR Proteomes; UP000016801; 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; 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:UP000016801};
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..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..515
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 82473 MW; 6C8B5F5F49C4051B CRC64;
MMSWWSSSAN TALDEQIEKA TSSSLEDIAL NLEISDIIRS KTVAPKEAMR SLKKRIGNKN
PNTQLGALNL TDTCVKNGGS HFLAEIASRE FMDNLVSLLQ AVGPAAVNSD VRFRMLELIQ
SWAVATDGRH ELSYIGQVYR TLQQEGHQFP PRVTVASSMI DSSAPPEWAD SDVCMRCRTA
FTFTNRKHHC RNCGNCFDQQ CSSKTIPLPH LGIQAAVRVD DGCYAKLTGK GYKELGPPDR
STPTYPHKTR SSTSTLQPRN ARVDDGFDED LKKALAMSLE EVKSSTRGYQ EPTRRVFAAP
QKTPSKQEEE EEEDADLKSA IAASIADMEE QKKRHAAALK QQTSNPPAGQ ASGSFVLPKN
DYELTPVEAE NINLFATLVD RLQTQPPGTI LREPQIQELY DSIGTLRPKL ARTYGETMSK
HDTLLDLHAK LSTVVRHYDR MLEERLSKAY GQQNLGGYNL RQPSRPYPSM PSHTPTAAGG
AESFYTGQQA APPHFQPPAA LQYHHPPPQA TPQAQHPYDQ PPESQTGQFV QPQRTGSWQA
RGTPGPSAPV DSYPQQQQHT SQEPQRRMQT PQQQAASPSA ESRESYYYTT QPQQTPLQLP
SGPSAPTMAP DSSSSPYPTL PQHSLQYGQN AAVSTPGQTN NPVQAHSQPS QPTRRSSHHQ
PQSRVPMAPQ QLQQQQQQQT TAPAPANQHA PAQEPYWQPQ YAQQVSQPPA ASQSKAYTGY
THDSFPSVPQ HDPVKDHVQE EALIEL
//
