BAG4_ARATH
ID BAG4_ARATH Reviewed; 269 AA.
AC Q8RX71; O65021; Q8LDA0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=BAG family molecular chaperone regulator 4;
DE AltName: Full=Bcl-2-associated athanogene 4;
GN Name=BAG4; OrderedLocusNames=At3g51780; ORFNames=ATEM1.3;
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=10645728; DOI=10.1023/a:1006395324818;
RA Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M.,
RA Grellet F.;
RT "Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1
RT locus on chromosome III.";
RL Plant Mol. Biol. 41:687-700(1999).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 GENE FAMILY, INTERACTION WITH HSP70-1, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, INDUCTION, AND MUTAGENESIS OF GLU-179 AND ASP-189.
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).
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 (By
CC similarity). Interacts with HSP70-1. {ECO:0000250,
CC ECO:0000269|PubMed:16636050}.
CC -!- TISSUE SPECIFICITY: Detected in stems, leaves, flowers and roots.
CC {ECO:0000269|PubMed:16636050}.
CC -!- INDUCTION: By cold, by salicylic acid (SA), by abscisic acid (ABA) and
CC by pathogen B.cinerea attack. {ECO:0000269|PubMed:16636050}.
CC -!- DISRUPTION PHENOTYPE: Early flowering and shorter vegetative and
CC reproductive phases, with more branched roots and inflorescences. Early
CC senescence. Enhanced susceptibility to salt stress. Hypersensitivity to
CC light. {ECO:0000269|PubMed:16636050}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF049236; AAC14405.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78842.1; -; Genomic_DNA.
DR EMBL; AY090347; AAL91253.1; -; mRNA.
DR EMBL; AY143837; AAN28776.1; -; mRNA.
DR EMBL; AY086123; AAM63329.1; ALT_INIT; mRNA.
DR PIR; T51149; T51149.
DR RefSeq; NP_190746.2; NM_115037.8.
DR PDB; 4HWH; X-ray; 1.90 A; A/B/C/D/E=138-223.
DR PDBsum; 4HWH; -.
DR AlphaFoldDB; Q8RX71; -.
DR SMR; Q8RX71; -.
DR BioGRID; 9659; 3.
DR IntAct; Q8RX71; 3.
DR STRING; 3702.AT3G51780.1; -.
DR PaxDb; Q8RX71; -.
DR PRIDE; Q8RX71; -.
DR ProteomicsDB; 240737; -.
DR EnsemblPlants; AT3G51780.1; AT3G51780.1; AT3G51780.
DR GeneID; 824341; -.
DR Gramene; AT3G51780.1; AT3G51780.1; AT3G51780.
DR KEGG; ath:AT3G51780; -.
DR Araport; AT3G51780; -.
DR TAIR; locus:2074353; AT3G51780.
DR eggNOG; KOG4361; Eukaryota.
DR HOGENOM; CLU_043370_1_1_1; -.
DR InParanoid; Q8RX71; -.
DR OMA; KARCSNP; -.
DR OrthoDB; 1358754at2759; -.
DR PhylomeDB; Q8RX71; -.
DR PRO; PR:Q8RX71; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RX71; baseline and differential.
DR Genevisible; Q8RX71; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IPI:TAIR.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IPI:TAIR.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IGI:TAIR.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IGI:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12329; PTHR12329; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome.
FT CHAIN 1..269
FT /note="BAG family molecular chaperone regulator 4"
FT /id="PRO_0000415524"
FT DOMAIN 46..122
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 138..219
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 179
FT /note="E->G: Abolishes interaction with HSP70-1."
FT /evidence="ECO:0000269|PubMed:16636050"
FT MUTAGEN 189
FT /note="D->S: Abolishes interaction with HSP70-1."
FT /evidence="ECO:0000269|PubMed:16636050"
FT CONFLICT 26
FT /note="A -> T (in Ref. 1; AAC14405)"
FT /evidence="ECO:0000305"
FT HELIX 138..164
FT /evidence="ECO:0007829|PDB:4HWH"
FT HELIX 171..189
FT /evidence="ECO:0007829|PDB:4HWH"
FT HELIX 198..221
FT /evidence="ECO:0007829|PDB:4HWH"
SQ SEQUENCE 269 AA; 29211 MW; 58E4903942E324FB CRC64;
MMHNSTEESE WEVRPGGMLV QRRDDAASSD HKPLQDPDSA SAAFAQTIRI TVSHGSSHHD
LHISAHATFG DVKKALVQKT GLEASELKIL FRGVERDDAE QLQAAGVKDA SKLVVVVEDT
NKRVEQQPPV VTKEMEKAIA AVNAVTGEVD KLSDRVVALE VAVNGGTQVA VREFDMAAEL
LMRQLLKLDG IEAEGDAKVQ RKAEVRRIQN LQEAVDKLKA RCSNPFVDQS KAAAVSTEWE
SFGNGVGSLN PPPPASPSAN VTQDWEKFD
