CAB25_ARATH
ID CAB25_ARATH Reviewed; 238 AA.
AC O80683;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Calmodulin-binding protein 25 {ECO:0000303|PubMed:15086802};
DE Short=AtCAMBP25 {ECO:0000303|PubMed:15086802};
DE AltName: Full=VQ motif-containing protein 15 {ECO:0000303|PubMed:22535423};
DE Short=AtVQ15 {ECO:0000303|PubMed:22535423};
GN Name=CAMBP25 {ECO:0000303|PubMed:15086802};
GN Synonyms=VQ15 {ECO:0000303|PubMed:22535423};
GN OrderedLocusNames=At2g41010 {ECO:0000312|Araport:AT2G41010};
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 [MRNA], FUNCTION, INTERACTION WITH CALMODULIN,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15086802; DOI=10.1111/j.1365-313x.2004.02062.x;
RA Perruc E., Charpenteau M., Ramirez B.C., Jauneau A., Galaud J.P.,
RA Ranjeva R., Ranty B.;
RT "A novel calmodulin-binding protein functions as a negative regulator of
RT osmotic stress tolerance in Arabidopsis thaliana seedlings.";
RL Plant J. 38:410-420(2004).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH WRKY25 AND WRKY51, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22535423; DOI=10.1104/pp.112.196816;
RA Cheng Y., Zhou Y., Yang Y., Chi Y.J., Zhou J., Chen J.Y., Wang F., Fan B.,
RA Shi K., Zhou Y.H., Yu J.Q., Chen Z.;
RT "Structural and functional analysis of VQ motif-containing proteins in
RT Arabidopsis as interacting proteins of WRKY transcription factors.";
RL Plant Physiol. 159:810-825(2012).
CC -!- FUNCTION: Calmodulin-binding protein that functions as a negative
CC regulator of osmotic stress tolerance. {ECO:0000269|PubMed:15086802}.
CC -!- SUBUNIT: Interacts with calmodulin (CaM) (PubMed:15086802). Interacts
CC with WRKY25 and WRKY51 (PubMed:22535423). {ECO:0000269|PubMed:15086802,
CC ECO:0000269|PubMed:22535423}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15086802}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and siliques.
CC {ECO:0000269|PubMed:15086802}.
CC -!- INDUCTION: By cold, salt stress and dehydration.
CC {ECO:0000269|PubMed:15086802}.
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DR EMBL; AY531115; AAS20952.1; -; mRNA.
DR EMBL; AC004261; AAD12010.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09915.1; -; Genomic_DNA.
DR EMBL; AK117111; BAC41790.1; -; mRNA.
DR EMBL; AF325087; AAK17155.1; -; mRNA.
DR EMBL; BT024619; ABD43017.1; -; mRNA.
DR PIR; T02118; T02118.
DR RefSeq; NP_181634.1; NM_129666.5.
DR AlphaFoldDB; O80683; -.
DR STRING; 3702.AT2G41010.1; -.
DR PaxDb; O80683; -.
DR PRIDE; O80683; -.
DR ProteomicsDB; 223858; -.
DR EnsemblPlants; AT2G41010.1; AT2G41010.1; AT2G41010.
DR GeneID; 818701; -.
DR Gramene; AT2G41010.1; AT2G41010.1; AT2G41010.
DR KEGG; ath:AT2G41010; -.
DR Araport; AT2G41010; -.
DR TAIR; locus:2063265; AT2G41010.
DR eggNOG; ENOG502SYS5; Eukaryota.
DR HOGENOM; CLU_080279_0_0_1; -.
DR InParanoid; O80683; -.
DR OMA; FDPIVKP; -.
DR OrthoDB; 1351092at2759; -.
DR PhylomeDB; O80683; -.
DR PRO; PR:O80683; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80683; baseline and differential.
DR Genevisible; O80683; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0010337; P:regulation of salicylic acid metabolic process; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR InterPro; IPR039830; CAMBP25.
DR InterPro; IPR008889; VQ.
DR InterPro; IPR039609; VQ_15/22.
DR PANTHER; PTHR33179; PTHR33179; 1.
DR PANTHER; PTHR33179:SF41; PTHR33179:SF41; 1.
DR Pfam; PF05678; VQ; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..238
FT /note="Calmodulin-binding protein 25"
FT /id="PRO_0000432306"
FT REGION 68..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 92..108
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:15086802"
FT MOTIF 125..134
FT /note="VQ"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 25377 MW; 02945E258F8392D4 CRC64;
MVTSEGLASV DSWLYRQGFN VDSWLLSDTF SHDNDLLARA LHTTVTAPHT LTPSSAFFDS
SAVSHPSSTN TLSSTVSGAS DPEIIGGGAK RKRNCLLTDG KAAKRRARAS KKSQTTFITA
DPSNFRQMVQ QVTGAKYIDD SSSFGIFDPI VKPEPLRFVN KLPCGPSDRS TAVPMLDTSA
FLSNHHQENL AVGNAFSGNS SSVGLPSGKP SATADPGGSA VEFDNYPTFP TLESWKVM
