ID   HSE1_DEBHA              Reviewed;         512 AA.
AC   Q6BNP6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN   Name=HSE1; OrderedLocusNames=DEHA2E19976g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382137; CAG88447.2; -; Genomic_DNA.
DR   RefSeq; XP_460174.2; XM_460174.1.
DR   AlphaFoldDB; Q6BNP6; -.
DR   SMR; Q6BNP6; -.
DR   STRING; 4959.XP_460174.2; -.
DR   EnsemblFungi; CAG88447; CAG88447; DEHA2E19976g.
DR   GeneID; 2901988; -.
DR   KEGG; dha:DEHA2E19976g; -.
DR   eggNOG; KOG2199; Eukaryota.
DR   HOGENOM; CLU_010104_2_0_1; -.
DR   InParanoid; Q6BNP6; -.
DR   OMA; AHALCQN; -.
DR   OrthoDB; 906159at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
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..512
FT                   /note="Class E vacuolar protein-sorting machinery protein
FT                   HSE1"
FT                   /id="PRO_0000292495"
FT   DOMAIN          22..153
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          175..194
FT                   /note="UIM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          255..315
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          153..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  58084 MW;  26ED73333450F6B3 CRC64;
     MFGGRQSNNK SNDSLEQLIN RATDETLTND NWQYILDVCD NISSNPEEGT KQGIKVVSSR
     LASKDANIIL RTLSLLVAMA ENCGSRMRQE IATTSFVQES LLKKFTDRRL HKTVKFRVAE
     VIKQLHDSFK TDPSLKPMTD AYNRLVNDYS QYSAETADGP AKPAKKERSR QDKKKEEDEL
     QRVLKLSLQE YEREQTVKKS YLNNKPLPQA QNESQYQEQP RQQQQQQQVL QNQPMHSTPT
     GQQSTQSPAE SQTIATVSKV RALYDLISYE PDELSFRKGD IITVIESVYR DWWRGSLVNG
     KTGIFPLNYV TPVVTKTPQE LSRELDEENR LLAVDSKRID KLLALLSSNP ETINEDEITR
     LYGDIIPLRT SLGKFIDKYN VRKEELSVLN SQLNNEVKLY NDLMDSSISQ RVTHQPSGMS
     MAPYPTGVAS PTHSSFSQAN PSMLHQQPTS SGFGNARGNS SNEYFHSQQV PPTSFNQQSQ
     PHSQPQPPQQ SGPQRHNTEF SNINNFPNVN NI