CNBL7_ARATH
ID CNBL7_ARATH Reviewed; 214 AA.
AC Q9SUA6; O65578;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Calcineurin B-like protein 7;
DE AltName: Full=SOS3-like calcium-binding protein 3;
GN Name=CBL7; Synonyms=SCABP3; OrderedLocusNames=At4g26560;
GN ORFNames=M3E9.10, T15N24_10;
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].
RC STRAIN=cv. Columbia;
RX PubMed=11115898; DOI=10.1104/pp.124.4.1844;
RA Kim K.-N., Cheong Y.H., Gupta R., Luan S.;
RT "Interaction specificity of Arabidopsis calcineurin B-like calcium sensors
RT and their target kinases.";
RL Plant Physiol. 124:1844-1853(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 GENE FAMILY.
RX PubMed=14730064; DOI=10.1104/pp.103.033068;
RA Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT "Calcium sensors and their interacting protein kinases: genomics of the
RT Arabidopsis and rice CBL-CIPK signaling networks.";
RL Plant Physiol. 134:43-58(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19832944; DOI=10.1111/j.1365-313x.2009.04045.x;
RA Batistic O., Waadt R., Steinhorst L., Held K., Kudla J.;
RT "CBL-mediated targeting of CIPKs facilitates the decoding of calcium
RT signals emanating from distinct cellular stores.";
RL Plant J. 61:211-222(2010).
RN [6]
RP INTERACTION WITH PP2CA.
RX PubMed=21596690; DOI=10.1093/mp/ssr031;
RA Lan W.Z., Lee S.C., Che Y.F., Jiang Y.Q., Luan S.;
RT "Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA
RT interactions.";
RL Mol. Plant 4:527-536(2011).
CC -!- FUNCTION: Acts as a calcium sensor. CBL proteins interact with CIPK
CC serine-threonine protein kinases. Binding of a CBL protein to the
CC regulatory NAF domain of a CIPK protein lead to the activation of the
CC kinase in a calcium-dependent manner.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PP2CA. {ECO:0000250,
CC ECO:0000269|PubMed:21596690}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19832944}. Nucleus
CC {ECO:0000269|PubMed:19832944}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF290434; AAG10059.1; -; mRNA.
DR EMBL; AL022223; CAA18214.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL078465; CAB43852.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79511.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85219.1; -; Genomic_DNA.
DR PIR; T05048; T05048.
DR PIR; T08922; T08922.
DR RefSeq; NP_194386.1; NM_118790.2.
DR AlphaFoldDB; Q9SUA6; -.
DR SMR; Q9SUA6; -.
DR BioGRID; 14050; 5.
DR IntAct; Q9SUA6; 1.
DR STRING; 3702.AT4G26560.1; -.
DR PaxDb; Q9SUA6; -.
DR PRIDE; Q9SUA6; -.
DR ProteomicsDB; 220288; -.
DR EnsemblPlants; AT4G26560.1; AT4G26560.1; AT4G26560.
DR GeneID; 828763; -.
DR Gramene; AT4G26560.1; AT4G26560.1; AT4G26560.
DR KEGG; ath:AT4G26560; -.
DR Araport; AT4G26560; -.
DR TAIR; locus:2133857; AT4G26560.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; Q9SUA6; -.
DR OMA; IDEEEWM; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q9SUA6; -.
DR PRO; PR:Q9SUA6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUA6; baseline and differential.
DR Genevisible; Q9SUA6; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0005513; P:detection of calcium ion; ISS:TAIR.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:TAIR.
DR GO; GO:0010446; P:response to alkaline pH; IMP:TAIR.
DR InterPro; IPR045198; CNBL1-10.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23056; PTHR23056; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..214
FT /note="Calcineurin B-like protein 7"
FT /id="PRO_0000073508"
FT DOMAIN 33..69
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 70..105
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 107..142
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 151..186
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 143
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8LAS7"
SQ SEQUENCE 214 AA; 24404 MW; 7895D04D02B291CF CRC64;
MDSTRNSASS NSTGCFTDQK KRKALYEVFK KLSGVDCQRN EGNVVEGVTC YYGEMNKEQF
HVAIFQTDKN ESLFSERVFD LFDTNHDGLL GFEEFARALS VFHPSAPIDD KIDLSFQLYD
LKQQGFIERQ GVKQLVVATL AASGMSQSDE IVESIIDKTF VQADTKHEGM IDEEEWMDLV
FRHPLLLKNM TLQYLKDITT TFPSFVLHSQ VEDT
