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Database: UniProt
Entry: A0A0P1BEE0_9BASI
LinkDB: A0A0P1BEE0_9BASI
Original site: A0A0P1BEE0_9BASI 
ID   A0A0P1BEE0_9BASI        Unreviewed;       709 AA.
AC   A0A0P1BEE0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH14191.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH14191.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) 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). {ECO:0000256|ARBA:ARBA00002654}.
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}.
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DR   EMBL; CCYA01000240; CEH14191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BEE0; -.
DR   STRING; 401625.A0A0P1BEE0; -.
DR   OrthoDB; 620063at2759; -.
DR   Proteomes; UP000054845; 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; IPR003903; UIM_dom.
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; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF89009; GAT-like domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50179; VHS; 1.
PE   3: Inferred from homology;
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          14..116
FT                   /note="VHS"
FT                   /evidence="ECO:0000259|PROSITE:PS50179"
FT   DOMAIN          361..420
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          186..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..664
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   709 AA;  76612 MW;  C23C19E10DEA0C32 CRC64;
     MSVTNPYDEI VTKATNENLT SENWELNLDV CDKVSGEGEV GARSCVHSIS KRLQHRSAHV
     QIYALTLCDA LSKNCGSIAQ KELDSRTFAE ALRRLIVDRN ASIEVKKKSW ALMKEWVAES
     NAETGRVLKE TLDGLSAQNI NYDVEPEAAP EPSSEQLRQE DEELRRVLEL SKSDVGGRYG
     ANGWFEMPGE TSGASGSGST NRAGSSRAEQ SVTAAAAGEA VSSTVASTLS SRPNEPSSIA
     STTAEISRPD ATGYIARPSA AAAQNDVRPV IQPTTAATTS APPYASRQST IIPPATSVAA
     QNQAETQQAA SRPNIATSHT ATAVPAAPQA QNAVPAANTT APPAPSAVAS PIANDAAATP
     SAPSRVRALY DFAPTEAGEL AFSKGDIIRV LDSVYEHWWR GELRGNAGIF PVNYVEVLPN
     PTPAELQREA ELEARLFAQS GSIDNLITKL NELDPDHDNL AENEELQELY QTALSLRPKI
     VKLIDRYSVK LAELRAMNEK FTRARGTFDT AMEQSLAKYN PGAPTSTYTE VRPEYSQQVQ
     RQQQQQQHDY SQQWAQWYAA NGYTQAQQQQ QPHPNDPNYA AWYYAQQQQQ QYAQAQHGVS
     AQTGQHQPHA HIPASLTEMQ GSAPVNAPQS QPVASPQPQP QQVAGGPSAP QPPSQSPLPQ
     PPAQSSEAPH DDEKKRLFER ARAEAEAYHR AAQQHLQSQA QDSGAGPST
//
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