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ENV11_YEAST
ID   ENV11_YEAST             Reviewed;         860 AA.
AC   P53246; D6VUK4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Late endosome and vacuole interface protein 11;
GN   Name=ENV11; OrderedLocusNames=YGR071C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=12096123; DOI=10.1074/mcp.m100024-mcp200;
RA   Wilson W.A., Wang Z., Roach P.J.;
RT   "Systematic identification of the genes affecting glycogen storage in the
RT   yeast Saccharomyces cerevisiae: implication of the vacuole as a determinant
RT   of glycogen level.";
RL   Mol. Cell. Proteomics 1:232-242(2002).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19466415; DOI=10.1007/s00294-009-0251-0;
RA   Watanabe M., Watanabe D., Nogami S., Morishita S., Ohya Y.;
RT   "Comprehensive and quantitative analysis of yeast deletion mutants
RT   defective in apical and isotropic bud growth.";
RL   Curr. Genet. 55:365-380(2009).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=21912603; DOI=10.1371/journal.pone.0023696;
RA   Ricarte F., Menjivar R., Chhun S., Soreta T., Oliveira L., Hsueh T.,
RA   Serranilla M., Gharakhanian E.;
RT   "A genome-wide immunodetection screen in S. cerevisiae uncovers novel genes
RT   involved in lysosomal vacuole function and morphology.";
RL   PLoS ONE 6:E23696-E23696(2011).
CC   -!- FUNCTION: Involved in vacuolar processing and morphology.
CC       {ECO:0000269|PubMed:12096123, ECO:0000269|PubMed:21912603}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- DISRUPTION PHENOTYPE: Exhibits cold sensitivity, a significant increase
CC       in cells with fragmented vacuoles, internal accumulation of precursor
CC       CPY, increased glycogen accumulation, and displays elongated buds.
CC       {ECO:0000269|PubMed:19466415, ECO:0000269|PubMed:21912603}.
CC   -!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VID22 family. {ECO:0000305}.
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DR   EMBL; Z72856; CAA97073.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08165.1; -; Genomic_DNA.
DR   PIR; S64366; S64366.
DR   RefSeq; NP_011585.3; NM_001181200.3.
DR   AlphaFoldDB; P53246; -.
DR   BioGRID; 33314; 108.
DR   DIP; DIP-5521N; -.
DR   IntAct; P53246; 6.
DR   MINT; P53246; -.
DR   STRING; 4932.YGR071C; -.
DR   MaxQB; P53246; -.
DR   PaxDb; P53246; -.
DR   PRIDE; P53246; -.
DR   EnsemblFungi; YGR071C_mRNA; YGR071C; YGR071C.
DR   GeneID; 852962; -.
DR   KEGG; sce:YGR071C; -.
DR   SGD; S000003303; ENV11.
DR   VEuPathDB; FungiDB:YGR071C; -.
DR   eggNOG; ENOG502RKC9; Eukaryota.
DR   GeneTree; ENSGT00940000176412; -.
DR   HOGENOM; CLU_008135_0_0_1; -.
DR   InParanoid; P53246; -.
DR   OMA; TKVKCKH; -.
DR   BioCyc; YEAST:G3O-30784-MON; -.
DR   PRO; PR:P53246; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53246; protein.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005773; C:vacuole; IEA:GOC.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006624; P:vacuolar protein processing; IMP:SGD.
DR   GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR   InterPro; IPR003656; Znf_BED.
DR   Pfam; PF02892; zf-BED; 1.
DR   PROSITE; PS50808; ZF_BED; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..860
FT                   /note="Late endosome and vacuole interface protein 11"
FT                   /id="PRO_0000202806"
FT   ZN_FING         84..138
FT                   /note="BED-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   REGION          19..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
SQ   SEQUENCE   860 AA;  98109 MW;  308D65E456C8FF3B CRC64;
     MNTALDDLHG DLVTLEDNEI INNSDHSSSH STSHEEEDEE EDDTEDIELI EKDGNKILSS
     RIHPEDEIIN DGLNIWIPVQ MLKKNIAKFW SHFLAIEKKL TKVKCKHCGE ILTRSDASLT
     KTFRSHLKTK HNISANKNFY SMNFTVGDSN LKNNTSSTEI TRRHGYDSLT FNSDQSFKCF
     DIGKLQSSNY LSISQLVAIV IASENLPLNF FENVSFKSLL SKFHRIPPLT TNIIEESIIG
     LSKSIDELIR RSISRNDTQL PFTIHLSDSK ESNQPLYLKY SREIRAQLSN LDLSHLISVN
     FTELAGKRSL FSLQLFDNTN KVSKGLPLSI FVRKTTDIDI SVWQEQLNNL YSKYPGLQKS
     VISITLPQSH YTMVLENRNS HNFTFHSGSV REIKYHTCIV SELLHCFLQP LFNVPTESML
     SSFSVAKENH SGGSLLDSLI DFSHIDLSST ILGKICCLIE EVNLNDSLKS DFLLYCQNYT
     QPNCNELTSI LSCNCDRFSA LKSILEKFAN LVPFFKSINS HLENESLSES DFRLINTVEE
     TLRTFEQSIE YFASSAPLKF THTLVFIIKF ELYLTEIIRS FKFTKSKKPF EKILARLLKV
     KDLYLLDDVN LIGAFLYPSI FQSKSLLNEI FGTTSVNKIV HNMTKIVLRY LKNFINITNF
     RSSNSGGESG RNSGNNLLSD YEAIFMKESR DVELLCNTKL TAPLTEDSLL VQIIRDDLLR
     YVNRIAHELP NAYHDYLNDN DISFDGSHFT KHELSEENDS NSGEWCLNPM EETFDIHIPI
     SDSIWNNYIS SKNKIEVIDI LLQLLSVNST SSIRSELSSL TANQDFSTKL SEETIKIKLL
     NSQFNLEKIN FHSGSIFDAC
 
 
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