ID HSE1_PHANO Reviewed; 618 AA.
AC Q0U6X7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN Name=HSE1; ORFNames=SNOG_12487;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT80300.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445348; EAT80300.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001802709.1; XM_001802657.1.
DR AlphaFoldDB; Q0U6X7; -.
DR SMR; Q0U6X7; -.
DR STRING; 321614.Q0U6X7; -.
DR GeneID; 5979618; -.
DR KEGG; pno:SNOG_12487; -.
DR VEuPathDB; FungiDB:JI435_124870; -.
DR eggNOG; KOG2199; Eukaryota.
DR InParanoid; Q0U6X7; -.
DR OMA; QVYRDWW; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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 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..618
FT /note="Class E vacuolar protein-sorting machinery protein
FT HSE1"
FT /id="PRO_0000292501"
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 139..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 66902 MW; 1D3E0ECF17237AF0 CRC64;
MFRAQSNIFD DVVVKATDEN LTSENWEYIL DVCDKVGSSD TGAKDAVAAM IKRLAHRNAN
VQLYTLELAN ALSQNCGIQM HKELASRSFT DAMLRLANDR NTHQAVKAKI LERMGEWSEM
FSRDPDLGIM EGAYMKLKTQ NPNLRAPSKP QKTQISDSDR QKEEEELQMA LAMSIKESKG
ATPSAAKANA PQESNAGSSS QAAPAPQPVQ PGTTAATVSR VRALFDFQPS EPGELQFKKG
DIIAVLESVY KDWWKGSLRG NTGIFPLNYV EKLQDPTREE LEKEAQTEAE VFAQIRNVEK
LLALLSTNTQ AGGGDGRDNE EITELYHSTL AIRPKLIELI GKYSQKKDDF TQLNEKFIKA
RRDYESLLEA SMSQPPQPSY GSRPPYGYNA PPPSNYTGYP PSSPPPQQYG YGAGAPPQGS
APQYPPVGAN PAFFMVPPAG EQRPQQQTPQ PGPPSDPYSL PQGRVPIGGR PQSYAPQELA
TAHYDSPVDN RHSFAGPSQP QGAPSAPQGY EYPPSQAPPG YPPQQGAPLQ GPPPGQQNPY
EQISSPPTHQ QPPSDPYSQP PPQVGHGYPP QQPAHAPPAP PGASSSPAPA QGYLPYRPPG
QAPSAPPVGG GGDEGFYR
//
