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Database: UniProt
Entry: H0GS82_SACCK
LinkDB: H0GS82_SACCK
Original site: H0GS82_SACCK 
ID   H0GS82_SACCK            Unreviewed;       479 AA.
AC   H0GS82;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Ent1p {ECO:0000313|EMBL:EHN03381.1};
GN   ORFNames=VIN7_5998 {ECO:0000313|EMBL:EHN03381.1};
OS   Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS   (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN03381.1, ECO:0000313|Proteomes:UP000009009};
RN   [1] {ECO:0000313|EMBL:EHN03381.1, ECO:0000313|Proteomes:UP000009009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN7 {ECO:0000313|EMBL:EHN03381.1,
RC   ECO:0000313|Proteomes:UP000009009};
RX   PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT   genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT   origins.";
RL   FEMS Yeast Res. 12:88-96(2012).
CC   -!- SIMILARITY: Belongs to the epsin family.
CC       {ECO:0000256|ARBA:ARBA00010130}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHN03381.1}.
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DR   EMBL; AGVY01000153; EHN03381.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0GS82; -.
DR   HOGENOM; CLU_012678_0_1_1; -.
DR   PhylomeDB; H0GS82; -.
DR   Proteomes; UP000009009; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0051179; P:localization; IEA:UniProt.
DR   CDD; cd16991; ENTH_Ent1_Ent2; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR12276:SF110; EPSIN-1-RELATED; 1.
DR   PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1.
DR   Pfam; PF01417; ENTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50330; UIM; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121}.
FT   DOMAIN          43..175
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   REGION          172..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  55435 MW;  01502EDD2382BE16 CRC64;
     MTNRSLKNKR KEPFVHMRFS SGRKGRTRGT RIMSKQFVRS AKNLVKGYSS TQVLVRNATS
     NDNHQVSKDS LIELAEKSYD SADFFEIMDM LDKRLNDKGK YWRHIAKALT VLDYLIRFGS
     ENCVLWCKEN LYIIKTLKEF RHEDDEGVDQ GQIVRVKAKE LTTLLSDDER LNEERNMNIK
     GRSRKGRKRR GTGRNDEDDD DLQRAIDASR MTAEEDERRR KQDEDYETAL QLSKEEEELK
     RLQDLQRMQQ VHAQQQQQQP MYYDIFGNPI TPEEYAQFQL QQQQQQQQQQ LQQQQQQQEA
     MYYDVFGNPI SPEELAHFQQ QQYIASLQQQ QQVPSNNPFA KPNQEVTSQK EDQSFMASSS
     MQQQPLTQTR TGNQSMTDKY GKLNELLATG TGIDTFGNVG DSRVPAQHTK TGTFINSQGT
     GYRQVSNDPK QNPFLNSQYT GLPSTNIVPT QTGYGFGNQP QQQSQNNRSN SQGYTLIDL
//
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