HSE1_CANAL
ID HSE1_CANAL Reviewed; 498 AA.
AC Q5A895; A0A1D8PRX0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN Name=HSE1; OrderedLocusNames=CAALFM_CR01210CA;
GN ORFNames=CaO19.10743, CaO19.3233;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW30882.1; -; Genomic_DNA.
DR RefSeq; XP_717924.1; XM_712831.1.
DR AlphaFoldDB; Q5A895; -.
DR SMR; Q5A895; -.
DR BioGRID; 1223501; 1.
DR STRING; 237561.Q5A895; -.
DR PRIDE; Q5A895; -.
DR GeneID; 3640407; -.
DR KEGG; cal:CAALFM_CR01210CA; -.
DR CGD; CAL0000197264; HSE1.
DR VEuPathDB; FungiDB:CR_01210C_A; -.
DR eggNOG; KOG2199; Eukaryota.
DR HOGENOM; CLU_010104_2_0_1; -.
DR InParanoid; Q5A895; -.
DR OMA; FASEVRV; -.
DR OrthoDB; 906159at2759; -.
DR PRO; PR:Q5A895; -.
DR Proteomes; UP000000559; Chromosome R.
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; 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; PF02809; UIM; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00726; UIM; 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..498
FT /note="Class E vacuolar protein-sorting machinery protein
FT HSE1"
FT /id="PRO_0000292490"
FT DOMAIN 11..142
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 164..183
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 212..272
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 136..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 56597 MW; CE46CE0567CF9389 CRC64;
MTSLDVLINK ATDPTLTSDN WQYILDVCDR ISADPETETK RTITILKTKL TSKDANVVLR
SLSLLISIAE NCGSRVKQEI ATKSFLQDAL VKRLSDKKLH ATVKYKICEV LTQLYNAFKG
DPSLKPMTDA YNKARSEHPR YFSKQTQGPS KPAKKERTQQ DKDREEDELQ RALKLSLQEF
EQQKTGKKEP DVNKPLPEIQ PEPESPPVET VATVSKVRAL YDLVSYEPDE LSFRKGDVIT
VIESVYRDWW RGSLPSGKIG IFPLNYVTPI VNKSPQDIAK EIEIENKLIT EEQRKIERLL
AILSSQQIET INEDEVTHLY NEIIPLRIQL GNSIDKYGAR QEELKVLNQS LNSEIKLYNE
LLDKSISSRA KHNTGGAMYQ MSPYPTEQFP GQSQPQLSQQ QQHQPYAQPQ QTSNYAQQSQ
TVPPQFTQSQ QTQPQYHQSH TRTGSHQEVP QYSGYNSNNI PPPATTFNQY PPSQLQQQDT
SAGFGNDVYN RAAPGQPY
