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 27-MAR-2024, entry version 91. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS027052; EAW11305.1; -; Genomic_DNA. DR RefSeq; XP_001272731.1; XM_001272730.1. DR AlphaFoldDB; A1CEK6; -. DR SMR; A1CEK6; -. DR STRING; 344612.A1CEK6; -. 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; QVYRDWW; -. DR OrthoDB; 620063at2759; -. 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: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; PR00452; SH3DOMAIN. DR PRINTS; PR01887; SPECTRNALPHA. 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; 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 //