(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 130.
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};
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   SMR; Q9SUA6; -.
DR   BioGrid; 14050; 5.
DR   IntAct; Q9SUA6; 1.
DR   STRING; 3702.AT4G26560.1; -.
DR   PaxDb; Q9SUA6; -.
DR   PRIDE; Q9SUA6; -.
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   eggNOG; COG5126; LUCA.
DR   HOGENOM; HOG000233019; -.
DR   InParanoid; Q9SUA6; -.
DR   KO; K06268; -.
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:0005513; P:detection of calcium ion; ISS:TAIR.
DR   GO; GO:0032780; P:negative regulation of ATPase activity; IDA:TAIR.
DR   GO; GO:0010446; P:response to alkaline pH; IMP:TAIR.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
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;
DR   PRODOM; Q9SUA6.
DR   SWISS-2DPAGE; Q9SUA6.
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:0000255|PROSITE-ProRule:PRU00448"
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   CA_BIND         46..59
FT                   /note="1; atypical"
FT   CA_BIND         83..94
FT                   /note="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CA_BIND         120..131
FT                   /note="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CA_BIND         164..175
FT                   /note="4"
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
//

If you have problems or comments...

PBIL Back to PBIL home page