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BAG7_ARATH
ID   BAG7_ARATH              Reviewed;         446 AA.
AC   Q9LVA0;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=BAG family molecular chaperone regulator 7;
DE   AltName: Full=Bcl-2-associated athanogene 7;
GN   Name=BAG7; OrderedLocusNames=At5g62390; ORFNames=MMI9.22;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   DOI=10.1016/S0168-9452(03)00121-3;
RA   Juqiang Y., Cixin H., Hong Z.;
RT   "The BAG-family proteins in Arabidopsis thaliana.";
RL   Plant Sci. 165:1-7(2003).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=16636050; DOI=10.1074/jbc.m511794200;
RA   Doukhanina E.V., Chen S., van der Zalm E., Godzik A., Reed J.,
RA   Dickman M.B.;
RT   "Identification and functional characterization of the BAG protein family
RT   in Arabidopsis thaliana.";
RL   J. Biol. Chem. 281:18793-18801(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-443, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   HSP70-11/BIP2.
RX   PubMed=20231441; DOI=10.1073/pnas.0912670107;
RA   Williams B., Kabbage M., Britt R., Dickman M.B.;
RT   "AtBAG7, an Arabidopsis Bcl-2-associated athanogene, resides in the
RT   endoplasmic reticulum and is involved in the unfolded protein response.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:6088-6093(2010).
CC   -!- FUNCTION: Co-chaperone that regulates diverse cellular pathways, such
CC       as programmed cell death and stress responses. Necessary for the proper
CC       maintenance of the unfolded protein response (UPR) during heat and cold
CC       tolerance. {ECO:0000269|PubMed:20231441}.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones (By
CC       similarity). Interacts with HSP70-11/BIP2. {ECO:0000250,
CC       ECO:0000269|PubMed:20231441}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:20231441}.
CC   -!- DOMAIN: IQ domain mediates interaction with calmodulin. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Susceptibility to heat and cold stress.
CC       {ECO:0000269|PubMed:20231441}.
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DR   EMBL; AB019235; BAA97203.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97603.1; -; Genomic_DNA.
DR   EMBL; AY093078; AAM13077.1; -; mRNA.
DR   EMBL; AY128766; AAM91166.1; -; mRNA.
DR   RefSeq; NP_201045.1; NM_125633.5.
DR   AlphaFoldDB; Q9LVA0; -.
DR   SMR; Q9LVA0; -.
DR   BioGRID; 21604; 6.
DR   IntAct; Q9LVA0; 1.
DR   STRING; 3702.AT5G62390.1; -.
DR   iPTMnet; Q9LVA0; -.
DR   MetOSite; Q9LVA0; -.
DR   PaxDb; Q9LVA0; -.
DR   PRIDE; Q9LVA0; -.
DR   ProteomicsDB; 240712; -.
DR   EnsemblPlants; AT5G62390.1; AT5G62390.1; AT5G62390.
DR   GeneID; 836360; -.
DR   Gramene; AT5G62390.1; AT5G62390.1; AT5G62390.
DR   KEGG; ath:AT5G62390; -.
DR   Araport; AT5G62390; -.
DR   TAIR; locus:2167943; AT5G62390.
DR   eggNOG; ENOG502QRXB; Eukaryota.
DR   HOGENOM; CLU_038879_2_0_1; -.
DR   InParanoid; Q9LVA0; -.
DR   OMA; LIDPYTC; -.
DR   OrthoDB; 795297at2759; -.
DR   PhylomeDB; Q9LVA0; -.
DR   PRO; PR:Q9LVA0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LVA0; baseline and differential.
DR   Genevisible; Q9LVA0; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0070417; P:cellular response to cold; IMP:TAIR.
DR   GO; GO:0034605; P:cellular response to heat; IMP:TAIR.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IMP:TAIR.
DR   GO; GO:0006457; P:protein folding; IMP:TAIR.
DR   InterPro; IPR040400; BAG5/6/7/8.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   PANTHER; PTHR33322; PTHR33322; 2.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Calmodulin-binding; Chaperone; Endoplasmic reticulum;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..446
FT                   /note="BAG family molecular chaperone regulator 7"
FT                   /id="PRO_0000415527"
FT   DOMAIN          303..332
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          330..407
FT                   /note="BAG"
FT   REGION          230..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         443
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   446 AA;  51567 MW;  95E3125F4CCC67F8 CRC64;
     MTLFHRLDLI DPYTCTPLIV RETSIVEPSS LFLGFPSFID EDIEDLFEFS SPNPLDLFET
     VTDLVKIKKS PSSCKYKVIR RRLEPEYPLK YLCDRVSDLE SKFDRLVSPK SDRKYTLTKE
     IKGSGERKYK WEAEIQGPLE RKYKLEAEIE GSGERKYRWT TEIKGGKKDE EGLKLAALKK
     EKAKAKAIAA AEAEKKKNKN KKKSYNWTTE VKSERENGEV SHTYIIKATT GGEKKKKHEE
     KEKKEKIETK SKKKEKTRVV VIEEEEEEDD ESSEHGAIVL RKAFSRRNGA VRTKKGKNKE
     MPPEYAAVMI QRAFKAYLIR RSKSLRALRD LAIAKTKLKE LRASFHNFSY RRLIARDGEE
     RQKFSEKIIV LLLTVDAIEG VDVMVRGAKR SMVDELEAML DVVDPQPQGK SLSMRRRTFD
     MPDSLIRKEI AEGVTQIVQM LETEEE
 
 
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