ID   HSE1_ASPTN              Reviewed;         597 AA.
AC   Q0CJU8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Class E vacuolar protein-sorting machinery protein hse1;
GN   Name=hse1; ORFNames=ATEG_06036;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476601; EAU33797.1; -; Genomic_DNA.
DR   RefSeq; XP_001215214.1; XM_001215214.1.
DR   AlphaFoldDB; Q0CJU8; -.
DR   SMR; Q0CJU8; -.
DR   STRING; 341663.Q0CJU8; -.
DR   PRIDE; Q0CJU8; -.
DR   EnsemblFungi; EAU33797; EAU33797; ATEG_06036.
DR   GeneID; 4321440; -.
DR   VEuPathDB; FungiDB:ATEG_06036; -.
DR   eggNOG; KOG2199; Eukaryota.
DR   HOGENOM; CLU_010104_1_1_1; -.
DR   OMA; AHALCQN; -.
DR   OrthoDB; 906159at2759; -.
DR   Proteomes; UP000007963; 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; 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..597
FT                   /note="Class E vacuolar protein-sorting machinery protein
FT                   hse1"
FT                   /id="PRO_0000292489"
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          224..283
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          140..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..414
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..461
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..567
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  65592 MW;  6889980721DD6CEE CRC64;
     MFRAQQNAFD DAVAKATDEN LTSENWEYIL DVCDKVAAEE SGAKDAVAAL IKRLAHRNAN
     VQLYTLELGN ALAQNCGPKI HRELASRSFT DALLRLANDR NTHQQVKAKI LERMQEWTEM
     FASNPDFGIM EQAYMKLKTQ NPNLQPPSKP GKREITEADR QKEEEELQMA LALSIREKPS
     TAPHPQAESS ASAAAAATTP TGAASAGQAQ PAASQAVPSG TSAATVSRVR ALFDFQPSEP
     GELQFRKGDV IAVLESVYKD WWKGSLRGQT GIFPLNYVEK LPDPTVEELQ REAQMEAEVF
     GQIKNVEKLL TLLSTRSSEP NVQDNEEITA LYHSTLAIRP KLIELIGKYS QKKDEFTQLN
     EKFIKARRDY EALLEASMSH PAQPQYGRPG QPQYPYPGPG APMGYPPGGP QPDQRYFSPR
     PQGHMYPPTS QSPGPRNHTP PAAAPYQQAP SHPPAQPQQH TAPDAYPPQH HRPESTYDHP
     QELSTSVYDS PVEQRPPYPG AQIPAAIHQH FQQQQQQQQD YSPSVYSPDE SKPPGTQQVP
     YPATPAANQP PPMHQPPPVP GAAAAPTPYP VNAPGASYQA YKPPQGGPAS NPASFYQ