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   25-MAY-2022, entry version 81.
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; 13684.SNOT_12487; -.
DR   GeneID; 5979618; -.
DR   KEGG; pno:SNOG_12487; -.
DR   eggNOG; KOG2199; Eukaryota.
DR   InParanoid; Q0U6X7; -.
DR   OMA; AHALCQN; -.
DR   OrthoDB; 906159at2759; -.
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   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..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