ID   HSE1_CHAGB              Reviewed;         713 AA.
AC   Q2GT05;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN   Name=HSE1; ORFNames=CHGG_08899;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408034; EAQ84885.1; -; Genomic_DNA.
DR   RefSeq; XP_001226826.1; XM_001226825.1.
DR   AlphaFoldDB; Q2GT05; -.
DR   SMR; Q2GT05; -.
DR   STRING; 38033.XP_001226826.1; -.
DR   EnsemblFungi; EAQ84885; EAQ84885; CHGG_08899.
DR   GeneID; 4395291; -.
DR   eggNOG; KOG2199; Eukaryota.
DR   HOGENOM; CLU_010104_1_1_1; -.
DR   InParanoid; Q2GT05; -.
DR   OMA; AHALCQN; -.
DR   OrthoDB; 906159at2759; -.
DR   Proteomes; UP000001056; 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: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; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR002014; VHS_dom.
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..713
FT                   /note="Class E vacuolar protein-sorting machinery protein
FT                   HSE1"
FT                   /id="PRO_0000292492"
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          225..284
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          141..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..414
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..569
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  75997 MW;  BEB83FB82BBC4AD5 CRC64;
     MFRAAAAGPY DEAINKATDE NQTSEDWGAI MEICDRVAGD ANGPKESVAS LIKRLAHRNA
     NVQLYTLEVA NALSQNCGKN MHRELSSRAF TDALLKLAND RNTHTQVKAK ILERMKDWSD
     MFKSDPDLGI MYDAFYRLKQ SNPTLQPPSA PQKNSLTDQD RQKEEDELQI ALKLSLQEEE
     RKKKPAQAAP AAAPSGAGGP ATAGPATQQQ PAAPIQPMPS GTTAATVSRV RALYDFAPSE
     PGELEFKKGD VIAVLESVYK DWWRGSLKGK TGIFPLNYVE KLTDPTPDEL QREAQMEAEV
     FAEIKNVEKL LTLLSASNTA PREEDNEEIS KFIKARRDYE ALLESSMSHP PGPTYHQYAM
     RPQIPQGYPP PGQNYGAPPP QQQDAQRFYT PAPAQEPSQY PPSSPPPNNF QRPGPGATPA
     PFYVAGAEVP SQQNQIPPPT PQQQSQQPQQ PQYAQRPSEQ RVPSGGKQPA PLQTSSSPPP
     ANQYTPYQAP QSSARPQSTY GSGPQELSTS VYDSPIAPQN ANPAAPYPPS AYATPDEDPY
     TAAAASNSSV PTAPTVPPPS VPAPSAPSPE LQQPSYGQPY SAYHAHPPQQ TPYRAPGGVG
     VGASGSYDAA TVDGPRPHQQ QPLPSGLTMS PPPLHPSGPA YDARQSLPSR VGGPSGPGSG
     GGAPAMGGAP PQPQYKAYVP PGSSSAPGLP PADDGPTAPT APAAEGYYRT AAY