HSE1_YARLI
ID HSE1_YARLI Reviewed; 685 AA.
AC Q6C2N2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN Name=HSE1; OrderedLocusNames=YALI0F06446g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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}.
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DR EMBL; CR382132; CAG77887.1; -; Genomic_DNA.
DR RefSeq; XP_505080.1; XM_505080.1.
DR AlphaFoldDB; Q6C2N2; -.
DR SMR; Q6C2N2; -.
DR STRING; 4952.CAG77887; -.
DR PRIDE; Q6C2N2; -.
DR EnsemblFungi; CAG77887; CAG77887; YALI0_F06446g.
DR GeneID; 2908387; -.
DR KEGG; yli:YALI0F06446g; -.
DR VEuPathDB; FungiDB:YALI0_F06446g; -.
DR HOGENOM; CLU_010104_1_1_1; -.
DR InParanoid; Q6C2N2; -.
DR OMA; GENFRGT; -.
DR Proteomes; UP000001300; Chromosome F.
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; IPR003903; UIM_dom.
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; 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..685
FT /note="Class E vacuolar protein-sorting machinery protein
FT HSE1"
FT /id="PRO_0000292505"
FT DOMAIN 18..148
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 165..184
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 250..309
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 144..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 73584 MW; EE01267D03D7CDDC CRC64;
MFRSSEPVSP LDDVVTKATD ENLTTENWQY ILDVCDEVNN DPENGAKNVI TSVTKRLNKK
FANTQLYALT LVISLSSNCG SKMQQAIASK AFVKTLMKLA NDSAVHKSVK SKVLEVLEQL
TDEYKKDPSL RLIEEAYDEL SRKKPDLKAP AKPEKHKITE QERQREEEEL QMVLALSLSE
TNTSGSFQQH HQTNSQIQPP VNNSHFATDP HQQQQQQQQQ HNQQDYGQQS NNANTNNNAP
AVEDPTPTVA TVSRVKALYD LNATEPGELS FRKGDIITVL ESVFRDWWRG SLRGQVGIFP
LNYVMPIAEP TPAEIEKEAQ EELSVFSQSR NIEKLLALLS SQDAARLNLA ENEELQSLYH
STLAIRPKLV KLIDKYAQRK DDLVELNEKF VKARRVYDDL MEASMPQYGG AAAAGGYAGG
AQGGAPAGYP SAQGAPAGYP GTSGTPGTPG YPPQYPPQQQ QQQQQQQQQQ PPYPVQPLQT
HQQQPQQQQQ QTPYPVHQYD NTQAHGRQGS TDSGRSQRMY SQGGQGGQGP TDLHPATTGG
SGYGFPPQYG GGAPSAPSAP HGGAGGPGGP GGPSAPSGAH SGAPSAPPSH APAASAPHGY
GSPSTAHSAP YGTSPAASAP ARHSPYINGT PTSNLGQQSP VTSQSIPIPN NNNLAAPPVQ
GLYSHGTSPP PPVPNAGPPP SNFYE
