BAG6_ARATH
ID BAG6_ARATH Reviewed; 1043 AA.
AC O82345;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=BAG family molecular chaperone regulator 6 {ECO:0000303|Ref.3};
DE AltName: Full=Bcl-2-associated athanogene 6 {ECO:0000303|Ref.3};
DE AltName: Full=CaM-binding protein 1 {ECO:0000303|PubMed:16003391};
DE Contains:
DE RecName: Full=Cleaved BAG6 {ECO:0000303|PubMed:26739014};
GN Name=BAG6 {ECO:0000303|Ref.3};
GN Synonyms=CAMBP1 {ECO:0000303|PubMed:16003391};
GN OrderedLocusNames=At2g46240 {ECO:0000312|Araport:AT2G46240};
GN ORFNames=T3F17.11 {ECO:0000312|EMBL:AAC62882.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP FUNCTION, INTERACTION WITH CAM1; CAM2; CAM3; CAM4; CAM6 AND CAM7,
RP INDUCTION, AND MUTAGENESIS OF ILE-575.
RX PubMed=16003391; DOI=10.1038/sj.cdd.4401712;
RA Kang C.H., Jung W.Y., Kang Y.H., Kim J.Y., Kim D.G., Jeong J.C., Baek D.W.,
RA Jin J.B., Lee J.Y., Kim M.O., Chung W.S., Mengiste T., Koiwa H., Kwak S.S.,
RA Bahk J.D., Lee S.Y., Nam J.S., Yun D.J., Cho M.J.;
RT "AtBAG6, a novel calmodulin-binding protein, induces programmed cell death
RT in yeast and plants.";
RL Cell Death Differ. 13:84-95(2006).
RN [5]
RP GENE FAMILY, FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 INDUCTION.
RX PubMed=19352026; DOI=10.1271/bbb.80809;
RA Nishizawa-Yokoi A., Yoshida E., Yabuta Y., Shigeoka S.;
RT "Analysis of the regulation of target genes by an Arabidopsis heat shock
RT transcription factor, HsfA2.";
RL Biosci. Biotechnol. Biochem. 73:890-895(2009).
RN [7]
RP INDUCTION BY HEAT, AND FUNCTION.
RX PubMed=26580143; DOI=10.1111/pce.12664;
RA Echevarria-Zomeno S., Fernandez-Calvino L., Castro-Sanz A.B., Lopez J.A.,
RA Vazquez J., Castellano M.M.;
RT "Dissecting the proteome dynamics of the early heat stress response leading
RT to plant survival or death in Arabidopsis.";
RL Plant Cell Environ. 39:1264-1278(2016).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, PROTEOLYTIC PROCESSING, MUTAGENESIS OF
RP ASP-760, AND INTERACTION WITH APCB1 AND BAGP1.
RX PubMed=26739014; DOI=10.1105/tpc.15.00626;
RA Li Y., Kabbage M., Liu W., Dickman M.B.;
RT "Aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and
RT fungal resistance in plants.";
RL Plant Cell 28:233-247(2016).
CC -!- FUNCTION: Co-chaperone that regulates diverse cellular pathways, such
CC as programmed cell death and stress responses (PubMed:16003391).
CC Involved in plant basal resistance (PubMed:16636050, PubMed:26739014).
CC Involved in basal heat response through the regulation of the heat
CC induced small HSP (sHSP) transcriptional cascade (PubMed:26580143).
CC {ECO:0000269|PubMed:16003391, ECO:0000269|PubMed:16636050,
CC ECO:0000269|PubMed:26580143, ECO:0000269|PubMed:26739014}.
CC -!- FUNCTION: [Cleaved BAG6]: Induces autophagy.
CC {ECO:0000269|PubMed:26739014}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones (By
CC similarity). Interacts with calmodulins CAM1, CAM2, CAM3, CAM4, CAM6
CC and CAM7 (PubMed:16003391). Interacts with BAGP1 and APCB1
CC (PubMed:26739014). {ECO:0000250, ECO:0000269|PubMed:16003391,
CC ECO:0000269|PubMed:26739014}.
CC -!- INTERACTION:
CC O82345; P25069: CAM5; NbExp=4; IntAct=EBI-1397246, EBI-1397259;
CC -!- TISSUE SPECIFICITY: Detected in stems, leaves, flowers and roots.
CC {ECO:0000269|PubMed:16636050}.
CC -!- INDUCTION: By heat shock, by salicylic acid (SA), by abscisic acid
CC (ABA), by calcium, by hydrogen peroxide, and by pathogen B.cinerea
CC attack. Up-regulated by HSFA2. {ECO:0000269|PubMed:16003391,
CC ECO:0000269|PubMed:16636050, ECO:0000269|PubMed:19352026,
CC ECO:0000269|PubMed:26580143}.
CC -!- DOMAIN: IQ domain mediates interaction with calmodulin.
CC -!- DISRUPTION PHENOTYPE: Early flowering and shorter vegetative and
CC reproductive phases, with more branched roots and inflorescences
CC (PubMed:16636050). Early senescence (PubMed:16636050). Hypersensitivity
CC to light (PubMed:16636050). Enhanced susceptibility to B.cinerea and
CC permissive fungal growth (PubMed:16636050, PubMed:26739014).
CC {ECO:0000269|PubMed:16636050, ECO:0000269|PubMed:26739014}.
CC -!- MISCELLANEOUS: Overexpression of BAG6 results in a lesion mimic
CC phenotype. Processed by APCB1 during lesion mimic development. The
CC cleavage is triggered by pathogen infection or by pathogen-associated
CC molecular patterns (PAMPs). {ECO:0000269|PubMed:26739014}.
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DR EMBL; AC005397; AAC62882.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10664.1; -; Genomic_DNA.
DR PIR; D84900; D84900.
DR RefSeq; NP_182147.1; NM_130187.4.
DR AlphaFoldDB; O82345; -.
DR SMR; O82345; -.
DR BioGRID; 4567; 1.
DR IntAct; O82345; 4.
DR STRING; 3702.AT2G46240.1; -.
DR PaxDb; O82345; -.
DR PRIDE; O82345; -.
DR ProteomicsDB; 240738; -.
DR EnsemblPlants; AT2G46240.1; AT2G46240.1; AT2G46240.
DR GeneID; 819232; -.
DR Gramene; AT2G46240.1; AT2G46240.1; AT2G46240.
DR KEGG; ath:AT2G46240; -.
DR Araport; AT2G46240; -.
DR TAIR; locus:2062887; AT2G46240.
DR eggNOG; ENOG502QRHM; Eukaryota.
DR HOGENOM; CLU_292287_0_0_1; -.
DR InParanoid; O82345; -.
DR OMA; WIPHENA; -.
DR OrthoDB; 264887at2759; -.
DR PhylomeDB; O82345; -.
DR PRO; PR:O82345; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82345; baseline and differential.
DR Genevisible; O82345; AT.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IPI:TAIR.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0012502; P:induction of programmed cell death; IMP:TAIR.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR040400; BAG5/6/7/8.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR PANTHER; PTHR33322; PTHR33322; 1.
DR Pfam; PF02179; BAG; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Calmodulin-binding; Chaperone; Coiled coil; Reference proteome;
KW Stress response.
FT CHAIN 1..1043
FT /note="BAG family molecular chaperone regulator 6"
FT /id="PRO_0000415526"
FT CHAIN 1..760
FT /note="Cleaved BAG6"
FT /id="PRO_0000436006"
FT DOMAIN 568..597
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 595..672
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 253..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 971..1024
FT /evidence="ECO:0000255"
FT COMPBIAS 267..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 575
FT /note="I->N,S: Abolishes interaction with CaM."
FT /evidence="ECO:0000269|PubMed:16003391"
FT MUTAGEN 760
FT /note="D->A: Abolishes processing by caspase-1."
FT /evidence="ECO:0000269|PubMed:26739014"
SQ SEQUENCE 1043 AA; 116758 MW; B5E271A02299177B CRC64;
MMPVYMDPSQ PCQMRPQEYY YQGFGNNSQH MAMDAPPPCH GSCVHGNFPA YWPPCYPPQV
PYHQCCMNRS AFHPPHASYA PSCYVHPPFP VGYQPWFDVE KDVPGKHHCG KCSSQMCDLK
KDRGVVIEEH EPEIEKGEAV LPVRSTNCPY PIIWIPHENA RNQEYRSSLG LGKHNQPPAE
VRAPDNMTIQ KSFPESWRGC FPFDESSMKS LVQNQDSKKA QNGKTVEAPF DISKFKSLLQ
GQDMKEAQIQ KNKEELGQLT YPTSWVPSRR KRDDVEASES SNEDRKKMQN GKTVEYPFDI
SMIKSLIQGQ DVKEAQNQKN KEEPGQVPYP IFWIPSYGKR KDVEASESKE SSNEGRNLES
CPSDLHRNEG QITQAKGKEG NFECNVLSDA EEKSSVINIP VANHLQEPRN IPVKLSENHL
PKPTEPTKRI AKNEPVKSTK KEQSSSSSEA SKLPPVCLRV DPLPKERNGG SKSVSHPKRM
EKSKETKIAA PLSSKKAESR TVPEACNVKC EDANAEMKMA EGSLNALRTE KGSVESNSNL
QEESNGEIIK PCEAKENREQ PAKKSFTEEE AARIIQSMYR GYDVRRWEPI KKLKEIATVR
EQMGDVKKRI EALEASTDQH IEEKEIVVNG ELVMNLLLKL DAVEGLHPSI REFRKALATE
LSSIQDKLDS LKNSCASAEK EAVKEQVEIK SQPSDSPVNL EHSQLTEENK MVSDTNLEKV
LRLSPEEHPM SVLNRTDEKQ AESAAETEEG YGLFETLATD SKQATENAAA ASSTTIPEKI
GEVETVVPGN PPSADGNGMT VTNVEENKAM VVESLEEPIN ELPQMVEETE TNSIRDPENA
SEVSEAETNS SENENRKGED DIVLHSEKNV ELSELPVGVI DEETQPLSQD PSSSYTREGN
MTAMDPKTAS QEETEVDHSP NNSKGIGQQT SEPQDEKEQS PETEVIVKEQ PLETEVILNE
QAPEPEITEP GISKETKKLM EENQRFKETM ETLVKAGREQ LEVISKLTSR VKSLEKKLSH
KKKTQIRRRA SKPMSVSPTD AVL
