ID K9FA31_PEND1 Unreviewed; 613 AA.
AC K9FA31;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1 {ECO:0000256|ARBA:ARBA00017923};
DE AltName: Full=Class E vacuolar protein-sorting machinery protein hse1 {ECO:0000256|ARBA:ARBA00018978};
GN ORFNames=PDIP_80060 {ECO:0000313|EMBL:EKV06295.1};
OS Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV06295.1, ECO:0000313|Proteomes:UP000009886};
RN [1] {ECO:0000313|Proteomes:UP000009886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC receptor for ubiquitinated cargo proteins at the multivesicular body
CC (MVB). {ECO:0000256|ARBA:ARBA00002654}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC {ECO:0000256|ARBA:ARBA00011446}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. 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 STAM family.
CC {ECO:0000256|ARBA:ARBA00009666}.
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:EKV06295.1}.
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DR EMBL; AKCU01000483; EKV06295.1; -; Genomic_DNA.
DR RefSeq; XP_014532163.1; XM_014676677.1.
DR AlphaFoldDB; K9FA31; -.
DR GeneID; 26236322; -.
DR KEGG; pdp:PDIP_80060; -.
DR HOGENOM; CLU_010104_1_1_1; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000009886; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0016197; P:endosomal transport; IEA:UniProt.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR CDD; cd21386; GAT_Hse1; 1.
DR CDD; cd11805; SH3_GRB2_like_C; 1.
DR CDD; cd16978; VHS_HSE1; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR PANTHER; PTHR45929:SF3; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 16..145
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 223..282
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 67960 MW; 512317FFFEF5CC70 CRC64;
MFRAQQNQFD DAVAKATDEN LTSENWEYIL DVCDKVGSEE SGAKEAVAAM IKRLAHRNAN
VQLYTLELGN SLSQNCGLKI HRELASRSFT DALLRLANDR NTHQQVKSKI LERMEEWTEM
FASNPDFGIM EQAYMKLKTT NPNLQPPSKP GKREITDVDR QMEEEELQMA LALSIKDKAT
PAAAVAAAPR AEALSTAVTS VSAPSNQREP AETQPVLSGT SVATVSRVRA LFDFQPSEPG
ELQFRKGDTI AVLESVYKDW WKGSLRGQTG IFPLNYVEKL PDPTVDELQR EAQMEADVFG
QIKSVEKLLT LLSTRNTDLN VQENEEITSL YQATLAIRPK LIELIGKYSQ KKDEFTQLNE
KFIKARRDYE SLLEASLAHP AQPQYGRHAQ PQYGYSSAAP AGYPSAPQAD PRYYTPRPQD
TMPTQANAYA PYPTSEQAGP YRPASHSPGP RHQVQAGPSQ QPPHADPYQP VSHRPQSTYD
HPQELGTSVY DSPVDHPAPG QRMPYPPTSQ APPAAHQQFQ QQQQDYSSSA YSAEETVQIP
HQFQQQQQQS PYPDSPGAHK PPPSHQPPPA PGATQQPQYT PYNPAPPAAS TSEYQAYQPP
QGGAGSNPAS FYR
//
