HSE1_ASPCL
ID HSE1_ASPCL Reviewed; 599 AA.
AC A1CEK6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein hse1;
GN Name=hse1; ORFNames=ACLA_089980;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027052; EAW11305.1; -; Genomic_DNA.
DR RefSeq; XP_001272731.1; XM_001272730.1.
DR AlphaFoldDB; A1CEK6; -.
DR SMR; A1CEK6; -.
DR STRING; 5057.CADACLAP00008355; -.
DR EnsemblFungi; EAW11305; EAW11305; ACLA_089980.
DR GeneID; 4705069; -.
DR KEGG; act:ACLA_089980; -.
DR VEuPathDB; FungiDB:ACLA_089980; -.
DR eggNOG; KOG2199; Eukaryota.
DR HOGENOM; CLU_010104_1_1_1; -.
DR OMA; AHALCQN; -.
DR OrthoDB; 906159at2759; -.
DR Proteomes; UP000006701; 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: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..599
FT /note="Class E vacuolar protein-sorting machinery protein
FT hse1"
FT /id="PRO_0000292486"
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 215..274
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 177..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 66319 MW; 587E0488CE3587C8 CRC64;
MFRAQQNAFD DAVAKATDEN LTSENWEYIL DVCDKVAAEE SGAKDAVAAM IKRLAHRNAN
VQLYTLELAN ALAQNCGPKI HRELASRSFT DALLRLANDR NTHQQVKSKI LERMHDWTRM
FSSNPDFGIM EQAYMKLKTQ NPNLQPPSKP VKKEITQADR QKEEEELQMA LALSIREKSD
AGPAPQAESS APASAPVSQT QAAAPQAVPS GTSAATVSRV RALFDFQPSE PGELQFRKGD
IIAVLESVYK DWWKGSLRGQ TGIFPLNYVE KLPDPTVEEL QREAQMEADV FGQIKNVEKL
LTLLSTRSSE LNVQDNEEIT ALYHSTLAIR PKLIELIGKY SQKKDEFTQL NEKFIKARRD
YESLLEASMS HPPQPQYARP GQPPYGYPAP TGPHGYPQGA PQPDPQRYFS PRPQDQTHMY
PPTSQSPDPR GRTPPAGPTM QQQQQQPPAE SFQPMHHRPE STYDNPQELG TSVYDSPVEY
PPANQRFQYP PGASAPPGVH QQLQQQQQEY SPSNYSPEDT TNPPTANFPP QPQQSQLPYP
TGPAGHQAPP SHQPPPVPGG ASKPSPYPSL TPGAPSAGEY QAYNPSQASA SSNPASFYR
