HSE1_MAGO7
ID HSE1_MAGO7 Reviewed; 718 AA.
AC A4RF61; G4NC25;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN Name=HSE1; ORFNames=MGG_00455;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001235; EHA49028.1; -; Genomic_DNA.
DR RefSeq; XP_003718612.1; XM_003718564.1.
DR AlphaFoldDB; A4RF61; -.
DR SMR; A4RF61; -.
DR STRING; 318829.MGG_00455T0; -.
DR PRIDE; A4RF61; -.
DR EnsemblFungi; MGG_00455T0; MGG_00455T0; MGG_00455.
DR GeneID; 2674892; -.
DR KEGG; mgr:MGG_00455; -.
DR VEuPathDB; FungiDB:MGG_00455; -.
DR eggNOG; KOG2199; Eukaryota.
DR HOGENOM; CLU_010104_1_1_1; -.
DR InParanoid; A4RF61; -.
DR OMA; AHALCQN; -.
DR OrthoDB; 906159at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
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; 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..718
FT /note="Class E vacuolar protein-sorting machinery protein
FT HSE1"
FT /id="PRO_0000292498"
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 234..293
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 142..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..718
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 190..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 76839 MW; 28ADD0FB8491EFF6 CRC64;
MFRAQATTPY DTAIAKATDE NLTSEDWGAI MEVCDRVAGD DNGAKEAVQA LIRRLAHRNA
NVQLYTLEVA NALSQNCGKP MHRELASRAF TEALLKLANE RNTHNQVKAK ILEGTKEWSD
MFKDDADLGI MYDAYYRLKQ TNPQLQPPSA PQKNSLTDVD RQKEEEELQI ALKLSLQEEE
RKKQQTPAGP SGAAGPSSSS APDQAGTPSG QGADAGAGAA AVPLQPTGTG TTAATVSRVR
ALYDFVPSED GELEFKKGDV IAVLESVYKD WWRGSLKGKT GIFPLNYVEK LADPTPDELQ
REAQMEAEVF SEIKNVEKLL TLLSTSSKDE DSEEIAKLYQ QTSAIRPKLI KLIEKYSQKK
DDFTQLNEKF IKARRDYEAL LETSMSHPPQ PSYHQYAVRP QGYGGSPTPY PTQGPPQQDP
QRFYPPGPHP DQYPPSSPSP HLQRPGGTPG PGAQAPFYVA GAEVPSHGGP HPNQNFPPRD
PGQRIPSAGK QPARLQTQQA SSSPPPSAPY AAYSQPPAQQ GSYGNPQELS TSAYDSPVAS
HPHPNPLGSN APFAPATYPA EERYGTPSAA PAPLNPGGGQ QQPYQYNSYQ NQTPPQPANT
QPPQGGMYSG QGYNDSSDAV GNVPPQPTSA APPPPVPGSQ RVHSPVYGGP PGAADSRFSL
PSRMGPGAPS APLGGPSSPG EQPQYKAYVP PGSSGPSAPS APSVPADYYR QPGGTANY
