HSE1_NEUCR
ID HSE1_NEUCR Reviewed; 745 AA.
AC Q7S6J4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein hse1;
GN Name=hse1; ORFNames=NCU04841;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002241; EAA31164.1; -; Genomic_DNA.
DR RefSeq; XP_960400.1; XM_955307.3.
DR AlphaFoldDB; Q7S6J4; -.
DR SMR; Q7S6J4; -.
DR STRING; 5141.EFNCRP00000004591; -.
DR EnsemblFungi; EAA31164; EAA31164; NCU04841.
DR GeneID; 3876538; -.
DR KEGG; ncr:NCU04841; -.
DR VEuPathDB; FungiDB:NCU04841; -.
DR HOGENOM; CLU_010104_1_1_1; -.
DR InParanoid; Q7S6J4; -.
DR OMA; FASEVRV; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
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; IPR003903; UIM_dom.
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; PS50330; UIM; 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..745
FT /note="Class E vacuolar protein-sorting machinery protein
FT hse1"
FT /id="PRO_0000292500"
FT DOMAIN 17..146
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 163..182
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 238..297
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 142..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 78615 MW; 07BBC4616C7299AF CRC64;
MFRAAAAGPY DEAINKATDE NLTSEDWGAI MEVCDRVATD ANGAKEAVNS MIKRLAHRNA
NVQLYTLEVA NALSQNCGKN MHRELSSRAF TDALLKLAND RNTHTQVKAK ILERMKEWSD
MFKSDSDLGI MYDAYYRLKQ SNPTLQPPSA PQKNVLTDAD RQKEEEELQM ALQLSLQEEE
RKKRPAGASG ATASSSSGGA AAGPSNAGGA VASGEGTNST AGQAEATPQP VPSSTTAATV
SRVRALYDFV PSEPGELEFK KGDVIAVLKS VYKDWWSGSL KGKTGIFPLN YVEKLADPTP
EELQREAQME AEVFAEIKNV EKLLTLLSAG NTGPREEDNE EISKLYHQTL AIRPKLIKLI
EKYSQKKDDF TQLNEKFIKA RRDYEALLES SMSHPPGPTY HQYAMRPPMT NSYGSGGYGA
PPPQQQQEPP RFYNPAPAQD APQYPATSPS PNPNHFIRPA GTPAPYYMGG AEGPGQLQHQ
QQPPYPQQQP QPAYGAPSRP QDQQRNPSGP SPMAPAPLNT TSSPPPGNQY TPYQAPGASG
ANNRTNSYSS TNGGAPQELS TSAYDSPIAQ HSTNPLSNPS YNAPSAPSYS QGRPGAPTDD
PYGPTSPGAG SSNNVGSAPP PPSGPAPSGP APSAPSAPSA PSAPGAPNSY TQGAYHSQNP
YAAAAAAAAA AASRTHVPGV YDGAGSEVSS TAPQPPAALQ PGGGAQPQYK AYVPPGAPSA
PGSGQEGPSA PGQNDGLADY YRSAY
