位置:首页 > 蛋白库 > CNBL8_ARATH
CNBL8_ARATH
ID   CNBL8_ARATH             Reviewed;         214 AA.
AC   Q9FUQ7; Q9SGW7;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Calcineurin B-like protein 8;
GN   Name=CBL8; OrderedLocusNames=At1g64480; ORFNames=F1N19.5;
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 [MRNA].
RA   Albrecht V., Weinl S., Blazevic D., Kudla J.;
RT   "Molecular characterization of the CBL gene family from Arabidopsis
RT   thaliana.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
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   [5]
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   [6]
RP   INTERACTION WITH CIPK23.
RX   PubMed=16814720; DOI=10.1016/j.cell.2006.06.011;
RA   Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.;
RT   "A protein kinase, interacting with two calcineurin B-like proteins,
RT   regulates K+ transporter AKT1 in Arabidopsis.";
RL   Cell 125:1347-1360(2006).
RN   [7]
RP   SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH CIPK14.
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).
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: Interacts with CIPK23. Interacts with CIPK14 at the cell
CC       membrane exclusively. {ECO:0000269|PubMed:16814720,
CC       ECO:0000269|PubMed:19832944}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19832944}. Nucleus
CC       {ECO:0000269|PubMed:19832944}. Cell membrane
CC       {ECO:0000269|PubMed:19832944}.
CC   -!- DOMAIN: The N-terminal 16 amino acids are sufficient for the cell
CC       membrane targeting of a heterologous protein.
CC       {ECO:0000269|PubMed:19832944}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF19691.1; 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; AF290433; AAG10058.1; -; mRNA.
DR   EMBL; AF411957; AAL10300.1; -; mRNA.
DR   EMBL; AC009519; AAF19691.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34245.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60358.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60359.1; -; Genomic_DNA.
DR   PIR; F96668; F96668.
DR   RefSeq; NP_001319319.1; NM_001334162.1.
DR   RefSeq; NP_001322653.1; NM_001334163.1.
DR   RefSeq; NP_176629.1; NM_105123.2.
DR   AlphaFoldDB; Q9FUQ7; -.
DR   SMR; Q9FUQ7; -.
DR   BioGRID; 27977; 3.
DR   IntAct; Q9FUQ7; 1.
DR   STRING; 3702.AT1G64480.1; -.
DR   TCDB; 8.A.82.2.1; the calmodulin calcium binding protein (calmodulin) family.
DR   PaxDb; Q9FUQ7; -.
DR   PRIDE; Q9FUQ7; -.
DR   EnsemblPlants; AT1G64480.1; AT1G64480.1; AT1G64480.
DR   EnsemblPlants; AT1G64480.2; AT1G64480.2; AT1G64480.
DR   EnsemblPlants; AT1G64480.3; AT1G64480.3; AT1G64480.
DR   GeneID; 842756; -.
DR   Gramene; AT1G64480.1; AT1G64480.1; AT1G64480.
DR   Gramene; AT1G64480.2; AT1G64480.2; AT1G64480.
DR   Gramene; AT1G64480.3; AT1G64480.3; AT1G64480.
DR   KEGG; ath:AT1G64480; -.
DR   Araport; AT1G64480; -.
DR   TAIR; locus:2019439; AT1G64480.
DR   eggNOG; KOG0034; Eukaryota.
DR   HOGENOM; CLU_061288_21_0_1; -.
DR   InParanoid; Q9FUQ7; -.
DR   OrthoDB; 1271942at2759; -.
DR   PhylomeDB; Q9FUQ7; -.
DR   PRO; PR:Q9FUQ7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FUQ7; baseline and differential.
DR   Genevisible; Q9FUQ7; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; TAS:TAIR.
DR   CDD; cd00051; EFh; 1.
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; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
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; Cell membrane; Cytoplasm; Membrane; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..214
FT                   /note="Calcineurin B-like protein 8"
FT                   /id="PRO_0000073509"
FT   DOMAIN          35..70
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          71..106
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          108..143
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          152..187
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         165
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         171
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LAS7"
SQ   SEQUENCE   214 AA;  24649 MW;  BDD1CBF7C77445DD CRC64;
     MLAFVKCFSL KRAKHPRGYE DPHVLASETP FTVNEIEALH DLFKKLSTSI INDGLIHKEE
     FLLALFRNGS MQNLFADRVF YMFDRKRNGV IEFGEFVRSL SIFHPYTPEH EKSAFMFKLF
     DLHGTGFIEP HELKKMVGAL LGETDLELSE ESIEAIVEQT MLEVDTNKDG KIDEEEWKEL
     VAKNPSILKN MTLPYLKEVT LAFPSFVLDS EVED
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024