CB60G_ARATH
ID CB60G_ARATH Reviewed; 563 AA.
AC F4K2R6; F4K2R7; Q2VYG1;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Calmodulin-binding protein 60 G {ECO:0000303|PubMed:11782485};
GN Name=CBP60G {ECO:0000303|PubMed:11782485};
GN OrderedLocusNames=At5g26920 {ECO:0000312|Araport:AT5G26920};
GN ORFNames=F2P16.9 {ECO:0000312|EMBL:AF007270};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 [MRNA] OF 4-563 (ISOFORM 1).
RA Kang Y.H., Kim M.C., Kang C.H., Koo Y.D., Choi M.S., Cho M.J.;
RT "Isolation of pathogen induced calmodulin binding protein in Arabidopsis.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11782485; DOI=10.1074/jbc.m111626200;
RA Reddy V.S., Ali G.S., Reddy A.S.N.;
RT "Genes encoding calmodulin-binding proteins in the Arabidopsis genome.";
RL J. Biol. Chem. 277:9840-9852(2002).
RN [5]
RP INDUCTION BY OPDA.
RX PubMed=16258017; DOI=10.1104/pp.105.067058;
RA Taki N., Sasaki-Sekimoto Y., Obayashi T., Kikuta A., Kobayashi K.,
RA Ainai T., Yagi K., Sakurai N., Suzuki H., Masuda T., Takamiya K.,
RA Shibata D., Kobayashi Y., Ohta H.;
RT "12-oxo-phytodienoic acid triggers expression of a distinct set of genes
RT and plays a role in wound-induced gene expression in Arabidopsis.";
RL Plant Physiol. 139:1268-1283(2005).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS SYRINGAE AND
RP FLG22, INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF PHE-25; VAL-28;
RP VAL-29 AND VAL-32.
RC STRAIN=cv. Columbia;
RX PubMed=19214217; DOI=10.1371/journal.ppat.1000301;
RA Wang L., Tsuda K., Sato M., Cohen J.D., Katagiri F., Glazebrook J.;
RT "Arabidopsis CaM binding protein CBP60g contributes to MAMP-induced SA
RT accumulation and is involved in disease resistance against Pseudomonas
RT syringae.";
RL PLoS Pathog. 5:E1000301-E1000301(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS SYRINGAE,
RP INTERACTION WITH CALMODULIN, AND DNA-BINDING.
RX PubMed=20921422; DOI=10.1073/pnas.1005225107;
RA Zhang Y., Xu S., Ding P., Wang D., Cheng Y.T., He J., Gao M., Xu F., Li Y.,
RA Zhu Z., Li X., Zhang Y.;
RT "Control of salicylic acid synthesis and systemic acquired resistance by
RT two members of a plant-specific family of transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18220-18225(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CALMODULIN.
RC STRAIN=cv. Columbia;
RX PubMed=21615571; DOI=10.1111/j.1365-313x.2011.04655.x;
RA Wang L., Tsuda K., Truman W., Sato M., Nguyen L.V., Katagiri F.,
RA Glazebrook J.;
RT "CBP60g and SARD1 play partially redundant critical roles in salicylic acid
RT signaling.";
RL Plant J. 67:1029-1041(2011).
RN [9]
RP FUNCTION IN TRANSCRIPTION REGULATION, AND INDUCTION BY FLG22.
RX PubMed=23153277; DOI=10.1186/1471-2229-12-216;
RA Truman W., Glazebrook J.;
RT "Co-expression analysis identifies putative targets for CBP60g and SARD1
RT regulation.";
RL BMC Plant Biol. 12:216-216(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22466450; DOI=10.1007/s00299-012-1247-7;
RA Wan D., Li R., Zou B., Zhang X., Cong J., Wang R., Xia Y., Li G.;
RT "Calmodulin-binding protein CBP60g is a positive regulator of both disease
RT resistance and drought tolerance in Arabidopsis.";
RL Plant Cell Rep. 31:1269-1281(2012).
RN [11]
RP INDUCTION BY PIRIFORMOSPORA INDICA.
RX PubMed=23118477; DOI=10.1093/mp/sss101;
RA Venus Y., Oelmueller R.;
RT "Arabidopsis ROP1 and ROP6 influence germination time, root morphology, the
RT formation of F-actin bundles, and symbiotic fungal interactions.";
RL Mol. Plant 6:872-886(2013).
RN [12]
RP FUNCTION, AND INTERACTION WITH V.DAHLIAE SCP41.
RX PubMed=29757140; DOI=10.7554/elife.34902;
RA Qin J., Wang K., Sun L., Xing H., Wang S., Li L., Chen S., Guo H.S.,
RA Zhang J.;
RT "The plant-specific transcription factors CBP60g and SARD1 are targeted by
RT a Verticillium secretory protein VdSCP41 to modulate immunity.";
RL Elife 7:e34902-e34902(2018).
CC -!- FUNCTION: Transcription activator that binds DNA in a sequence-specific
CC manner, 5'-GAAATTTTGG-3', to promote the expression of target genes
CC (PubMed:20921422, PubMed:21615571, PubMed:23153277, PubMed:29757140).
CC Recruited to the promoter of ICS1 and other defense-related genes (e.g.
CC PR1, PR2 and EDS5) in response to both biotic (e.g. Pseudomonas
CC syringae pv. maculicola ES4326, P. syringae pv. tomato DC3000, and
CC microbe-associated molecular patterns (MAMPs) such as flg22) and
CC abiotic stresses (e.g. UV-B, drought and abscisic acid), thus
CC triggering rapid defense responses by stimulating salicylic acid (SA)
CC biosynthesis. Involved in basal and systemic acquired resistance to P.
CC syringae and Hyaloperonospora arabidopsidis (PubMed:20921422,
CC PubMed:21615571, PubMed:22466450, PubMed:19214217). Mediates resistance
CC to drought and sensitivity to abscisic acid (ABA), especially for ABA-
CC mediated signaling process that regulates early seedling growth
CC (PubMed:22466450). {ECO:0000269|PubMed:19214217,
CC ECO:0000269|PubMed:20921422, ECO:0000269|PubMed:21615571,
CC ECO:0000269|PubMed:22466450, ECO:0000269|PubMed:23153277,
CC ECO:0000269|PubMed:29757140}.
CC -!- SUBUNIT: Interacts with calmodulin (CaM) in the presence of calcium
CC ions; this interaction is required for defense responses.
CC {ECO:0000269|PubMed:19214217, ECO:0000269|PubMed:20921422,
CC ECO:0000269|PubMed:21615571}.
CC -!- SUBUNIT: (Microbial infection) Interacts with V.dahliae SCP41; the
CC interaction is direct and inhibits CBP60G.
CC {ECO:0000269|PubMed:29757140}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22466450}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4K2R6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K2R6-2; Sequence=VSP_057667;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves,
CC inflorescences and flowers, and, to a lower extent, in siliques.
CC Particularly present in guard cells. {ECO:0000269|PubMed:22466450}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, present in roots, except in tips,
CC leaves and petioles. In inflorescence and flowers, accumulates in
CC sepals, carpels (e.g. styles and floral nectars) and stamens (e.g.
CC filaments and vascular tissue of anthers), but not in petals or stigma.
CC {ECO:0000269|PubMed:22466450}.
CC -!- INDUCTION: Induced rapidly by pathogenic bacteria Pseudomonas syringae
CC pv. maculicola ES4326 and P. syringae pv. tomato DC3000, by the root-
CC colonizing endophytic plant growth-promoting fungus Piriformospora
CC indica, and by microbe-associated molecular patterns (MAMPs) such as
CC flg22 and hrcC in both local and systemic leaves in both local and
CC systemic leaves (PubMed:20921422, PubMed:19214217, PubMed:23153277,
CC PubMed:23118477). Accumulates transiently in response to 12-oxo-
CC phytodienoic acid (OPDA) (PubMed:16258017).
CC {ECO:0000269|PubMed:16258017, ECO:0000269|PubMed:19214217,
CC ECO:0000269|PubMed:20921422, ECO:0000269|PubMed:23118477,
CC ECO:0000269|PubMed:23153277}.
CC -!- DISRUPTION PHENOTYPE: Reduced basal resistance to Pseudomonas syringae
CC pv. maculicola ES4326 and P. syringae pv. tomato DC3000. Impaired
CC systemic acquired resistance (SAR) induced by P. syringae toward
CC Hyaloperonospora arabidopsidis Noco2. Plants lacking both SARD1 and
CC CBP60G fail to accumulate salicylic acid (SA) and to express PR1 and
CC SID2 upon both biotic and abiotic stresses.
CC {ECO:0000269|PubMed:19214217, ECO:0000269|PubMed:20921422,
CC ECO:0000269|PubMed:21615571, ECO:0000269|PubMed:22466450}.
CC -!- SIMILARITY: Belongs to the plant ACBP60 protein family.
CC {ECO:0000305|PubMed:20921422}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM23317.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF007270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93626.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93627.1; -; Genomic_DNA.
DR EMBL; AY095443; AAM23317.1; ALT_INIT; mRNA.
DR RefSeq; NP_001190408.1; NM_001203479.1. [F4K2R6-2]
DR RefSeq; NP_198044.2; NM_122574.4. [F4K2R6-1]
DR AlphaFoldDB; F4K2R6; -.
DR SMR; F4K2R6; -.
DR STRING; 3702.AT5G26920.1; -.
DR PaxDb; F4K2R6; -.
DR PRIDE; F4K2R6; -.
DR ProteomicsDB; 239128; -. [F4K2R6-1]
DR EnsemblPlants; AT5G26920.1; AT5G26920.1; AT5G26920. [F4K2R6-1]
DR EnsemblPlants; AT5G26920.2; AT5G26920.2; AT5G26920. [F4K2R6-2]
DR GeneID; 832750; -.
DR Gramene; AT5G26920.1; AT5G26920.1; AT5G26920. [F4K2R6-1]
DR Gramene; AT5G26920.2; AT5G26920.2; AT5G26920. [F4K2R6-2]
DR KEGG; ath:AT5G26920; -.
DR Araport; AT5G26920; -.
DR TAIR; locus:2148548; AT5G26920.
DR eggNOG; ENOG502QWE3; Eukaryota.
DR InParanoid; F4K2R6; -.
DR OrthoDB; 858757at2759; -.
DR PhylomeDB; F4K2R6; -.
DR PRO; PR:F4K2R6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K2R6; baseline and differential.
DR Genevisible; F4K2R6; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0080142; P:regulation of salicylic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010112; P:regulation of systemic acquired resistance; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IDA:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IMP:TAIR.
DR InterPro; IPR012416; CBP60.
DR PANTHER; PTHR31713; PTHR31713; 1.
DR Pfam; PF07887; Calmodulin_bind; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Activator; Alternative splicing;
KW Calmodulin-binding; DNA-binding; Hypersensitive response; Nucleus;
KW Plant defense; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..563
FT /note="Calmodulin-binding protein 60 G"
FT /id="PRO_0000433051"
FT REGION 1..76
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:19214217,
FT ECO:0000269|PubMed:20921422"
FT REGION 147..263
FT /note="DNA-binding"
FT /evidence="ECO:0000303|PubMed:20921422"
FT VAR_SEQ 276..283
FT /note="Missing (in isoform 2)"
FT /id="VSP_057667"
FT MUTAGEN 25
FT /note="F->K: Impaired calmodulin-binding."
FT /evidence="ECO:0000269|PubMed:19214217"
FT MUTAGEN 28
FT /note="V->K: Impaired calmodulin-binding and reduced
FT resistance to Pseudomonas syringae associated with loss of
FT salicylic acid (SA) accumulation."
FT /evidence="ECO:0000269|PubMed:19214217"
FT MUTAGEN 29
FT /note="V->R: Impaired calmodulin-binding and reduced
FT resistance to Pseudomonas syringae associated with loss of
FT salicylic acid (SA) accumulation."
FT /evidence="ECO:0000269|PubMed:19214217"
FT MUTAGEN 32
FT /note="V->K: Impaired calmodulin-binding."
FT /evidence="ECO:0000269|PubMed:19214217"
SQ SEQUENCE 563 AA; 63068 MW; 4FD1D2A0FE6ED630 CRC64;
MKIRNSPSFH GGSGYSVFRA RNLTFKKVVK KVMRDQSNNQ FMIQMENMIR RIVREEIQRS
LQPFLSSSCV SMERSRSETP SSRSRLKLCF INSPPSSIFT GSKIEAEDGS PLVIELVDAT
TNTLVSTGPF SSSRVELVPL NADFTEESWT VEGFNRNILT QREGKRPLLT GDLTVMLKNG
VGVITGDIAF SDNSSWTRSR KFRLGAKLTG DGAVEARSEA FGCRDQRGES YKKHHPPCPS
DEVWRLEKIA KDGVSATRLA ERKILTVKDF RRLYTVNRNE LHNIIGAGVS KKTWNTIVSH
AMDCVLDETE CYIYNANTPG VTLLFNSVYE LIRVSFNGND IQNLDQPILD QLKAEAYQNL
NRITAVNDRT FVGHPQRSLQ CPQDPGFVVT CSGSQHIDFQ GSLDPSSSSM ALCHKASSST
VHPDVLMSFD NSSTARFHID KKFLPTFGNS FKVSELDQVH GKSQTVVTKG CIENNEEDEN
AFSYHHHDDM TSSWSPGTHQ AVETMFLTVS ETEEAGMFDV HFANVNLGSP RARWCKVKAA
FKVRAAFKEV RRHTTARNPR EGL
