HSE1_ASPNC
ID HSE1_ASPNC Reviewed; 611 AA.
AC A2QW93;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein hse1;
GN Name=hse1; ORFNames=An11g04310;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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DR EMBL; AM270233; CAK40663.1; -; Genomic_DNA.
DR RefSeq; XP_001394426.1; XM_001394389.2.
DR AlphaFoldDB; A2QW93; -.
DR SMR; A2QW93; -.
DR PaxDb; A2QW93; -.
DR PRIDE; A2QW93; -.
DR EnsemblFungi; CAK40663; CAK40663; An11g04310.
DR GeneID; 4984662; -.
DR KEGG; ang:ANI_1_590094; -.
DR HOGENOM; CLU_010104_1_1_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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: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 Gene3D; 1.25.40.90; -; 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 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; SSF48464; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW Endosome; Membrane; Protein transport; Reference proteome; SH3 domain;
KW Transport.
FT CHAIN 1..611
FT /note="Class E vacuolar protein-sorting machinery protein
FT hse1"
FT /id="PRO_0000292488"
FT DOMAIN 16..145
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 162..181
FT /note="UIM"
FT /evidence="ECO:0000305"
FT DOMAIN 216..275
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 140..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 67705 MW; AA8FDC22F662689E CRC64;
MFRAQQNAFD DAVAKATDEN LTSENWEYIL DVCDKVGAEE SGAKDAVAAM IKRLAHRNAN
VQLYTLELAN ALAQNCGPKI HRELASRSFT DALLRLANDR NTHQQVKSKI LERMQEWTEM
FASNPDFGIM EQAYMKLKTQ NPNLQPPSKP GKREITDADR QKEEEELQMA LALSIREKAT
IAPAPQAEAS SSAAPVNQTQ APAATSQAVP SGTSAATVSR VRALFDFQPS EPGELQFRKG
DVIAVLESVY KDWWKGSLRG QTGIFPLNYV EKLPDPTVEE LQREAQMEAD VFGQIKNVEK
LLTLLSTRSS ELNVQDNEEI TALYHSTLAI RPKLIELIGK YSQKKDEFTQ LNEKFIKARR
DYESLLEASM AHPAQSQYGR PAQPPYGYPG AAPVGYPQGP PQADPQRYFS PRPQETQAPP
ANAPAFYGTE QAHAYPPTSQ SPDPRQTPPA GAPYQQPQPQ QQRQPSSESY QPVYHRPEST
YENPQELGTS VYDSPVEHPA SQRPPYPGAV QVPAAVQQHF QQQQQQPQQQ SQQPHPEYPA
SGYTPEDASR PPAHQAQPPY PSHQPPPMHQ PPPVPGTSTT PTPYPALNAG GGYQAYNPSQ
TDVSNPASFY R
