BAG8_ARATH
ID BAG8_ARATH Reviewed; 551 AA.
AC Q9LIB3;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=BAG family molecular chaperone regulator 8, chloroplastic;
DE AltName: Full=Bcl-2-associated athanogene 8;
DE Flags: Precursor;
GN Name=BAG1; OrderedLocusNames=At3g29310; ORFNames=MUO10.1;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
CC -!- FUNCTION: Co-chaperone that regulates diverse cellular pathways, such
CC as programmed cell death and stress responses. {ECO:0000250}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DOMAIN: IQ domain mediates interaction with calmodulin. {ECO:0000250}.
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DR EMBL; AP001309; BAB02575.1; -; Genomic_DNA.
DR EMBL; AP002045; BAB02575.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77566.1; -; Genomic_DNA.
DR EMBL; AY078969; AAL84966.1; -; mRNA.
DR EMBL; AY149937; AAN31091.1; -; mRNA.
DR RefSeq; NP_189577.2; NM_113856.4.
DR AlphaFoldDB; Q9LIB3; -.
DR SMR; Q9LIB3; -.
DR BioGRID; 7918; 1.
DR IntAct; Q9LIB3; 1.
DR STRING; 3702.AT3G29310.1; -.
DR iPTMnet; Q9LIB3; -.
DR PaxDb; Q9LIB3; -.
DR PRIDE; Q9LIB3; -.
DR ProteomicsDB; 240713; -.
DR EnsemblPlants; AT3G29310.1; AT3G29310.1; AT3G29310.
DR GeneID; 822589; -.
DR Gramene; AT3G29310.1; AT3G29310.1; AT3G29310.
DR KEGG; ath:AT3G29310; -.
DR Araport; AT3G29310; -.
DR TAIR; locus:2093782; AT3G29310.
DR eggNOG; ENOG502QVMA; Eukaryota.
DR HOGENOM; CLU_036545_0_0_1; -.
DR InParanoid; Q9LIB3; -.
DR OMA; DCVVKRY; -.
DR OrthoDB; 1011399at2759; -.
DR PhylomeDB; Q9LIB3; -.
DR PRO; PR:Q9LIB3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIB3; baseline and differential.
DR Genevisible; Q9LIB3; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR InterPro; IPR040400; BAG5/6/7/8.
DR PANTHER; PTHR33322; PTHR33322; 2.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Chaperone; Chloroplast; Phosphoprotein; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..551
FT /note="BAG family molecular chaperone regulator 8,
FT chloroplastic"
FT /id="PRO_0000415528"
FT DOMAIN 131..160
FT /note="IQ"
FT DOMAIN 147..228
FT /note="BAG"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..517
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
SQ SEQUENCE 551 AA; 61496 MW; F42360988AEEE863 CRC64;
MASHHHHNHN HVCSRHQNHH NNTPQFATSP NCCNKSNHPS PPPAEDNLLH LVATYLQNHQ
QETQCSCETS CQNFNVIRSQ NRVLRQHKNV PREYDQVVLS CLLRKIDDLE SSLNKFSSFY
DKRRDRHSTL RDSAARVIQT HFRSYLVHRS ISFRQLKELA MIKASFLSLK SSVSGKLIFP
FKVVSRKATD LLLQLDSIQG RIDPMIRSSK RSLSRDLVRF VQYVDDCVVK RYGFVVKSGS
GIKLNGKKPQ GFGTSSEDED NNADMSDDSE EVPVSSIDKR KVASSKSRTG VVIEGDVVKP
PVMKFVVLDK NRNVCQVYGN RHDLTSSAED DSVDGDEETL VMSRDNGRKQ SLKARNGVSV
KGGGGKTTRV VKTVSFDENG NVCKVYGDTH DLTSSAEDDD SVDVGEETLV MCRDEGKRRS
SKTGSRVLVK GSGGKTNRVV KTVSFDENGN VYKAYGDTPE SSIISEEDDS TSGSNEGNGE
EKGNVNEVEE IKYVPKENES FEEEEEKETD SENEVSSSEG SEGDKRVTKK EVQHQKGSLM
FSPPLPLKME P
