HSE1_COCIM
ID HSE1_COCIM Reviewed; 612 AA.
AC Q1E878; J3KIZ1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN Name=HSE1; ORFNames=CIMG_01235;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704911; EAS35881.3; -; Genomic_DNA.
DR RefSeq; XP_001247464.1; XM_001247463.2.
DR AlphaFoldDB; Q1E878; -.
DR SMR; Q1E878; -.
DR STRING; 246410.Q1E878; -.
DR EnsemblFungi; EAS35881; EAS35881; CIMG_01235.
DR GeneID; 4567917; -.
DR KEGG; cim:CIMG_01235; -.
DR VEuPathDB; FungiDB:CIMG_01235; -.
DR InParanoid; Q1E878; -.
DR OMA; AHALCQN; -.
DR OrthoDB; 906159at2759; -.
DR Proteomes; UP000001261; 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..612
FT /note="Class E vacuolar protein-sorting machinery protein
FT HSE1"
FT /id="PRO_0000292493"
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 215..274
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 176..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 68320 MW; AD2921E6ACE35990 CRC64;
MFRAQQNAYD DIVAKATDEN LTSENWEYIL DVCDKVSADE SGAKDAVASM IKRLAHRNAN
VQLYTFELAN ALSQNCGPKA HRELASKSFT DALLRLANDR NTHPQVKSKI LEHMEQWTEM
FSSNPDFGIM EHAYMKLKSQ NPNIQPPSKP TKRQITELDR QKEEEELQMA LALSIKEKQS
ETSKQQDGSS QHVVTTSAQA EAAPSQGIPS GTTAATVSRV RALYDFQPSE PGELQFRKGD
IIAVLESVYK DWWKGSLRGQ VGIFPLNYVE KLSDPTQEEL QREAQMEAEV FAEIKNVEKL
LALLSTSSPE LNVQENEEIT KLYHSTLAIR PKLIELIGKY SKKKDDFTQL NEKFIKARRD
YEALLEASMT HPAQSHYNRP AQPPFAYPPS GTHPGYPHHA PPQQEPQRYY TPRPSQDPQS
APHNTPGYYG AEPSTLPYPP DSQSPDFRKH TATGSMQLPQ QQPSQPPQDA YSQGATTHYP
PKTTYDHPQE LGTSVYDSPQ GNAPQAIQHS YHPAMQQELQ QQQATGAEPT QRPYSPQENP
PPQAPSSNPP YPVQTPQEPP QQSFAPPAPM HQPPPIPSVA PSQGAYGGGY QAYQPPTTQQ
HSPTSNPAAF YR
