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CNBL1_ORYSJ
ID   CNBL1_ORYSJ             Reviewed;         213 AA.
AC   Q7XC27; B7F9Y6; Q0IVL4; Q3HRP6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Calcineurin B-like protein 1;
GN   Name=CBL1; OrderedLocusNames=Os10g0564800, LOC_Os10g41510;
GN   ORFNames=OsJ_32489 {ECO:0000312|EMBL:EEE51412.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND GENE FAMILY.
RC   STRAIN=cv. Nipponbare; TISSUE=Seedling;
RX   PubMed=18395997; DOI=10.1016/j.gene.2008.02.011;
RA   Gu Z., Ma B., Jiang Y., Chen Z., Su X., Zhang H.;
RT   "Expression analysis of the calcineurin B-like gene family in rice (Oryza
RT   sativa L.) under environmental stresses.";
RL   Gene 415:1-12(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
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   [9]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND GENE FAMILY.
RX   PubMed=15980189; DOI=10.1104/pp.105.062703;
RA   Hwang Y.-S., Bethke P.C., Cheong Y.H., Chang H.-S., Zhu T., Jones R.L.;
RT   "A gibberellin-regulated calcineurin B in rice localizes to the tonoplast
RT   and is implicated in vacuole function.";
RL   Plant Physiol. 138:1347-1358(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain membrane
CC       {ECO:0000269|PubMed:15980189}; Lipid-anchor
CC       {ECO:0000269|PubMed:15980189}. Note=Tonoplast. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, shoots, culms and scutellum.
CC       {ECO:0000269|PubMed:15980189, ECO:0000269|PubMed:18395997}.
CC   -!- INDUCTION: By salt and drought stresses, abscisic acid (ABA) and
CC       gibberellin. {ECO:0000269|PubMed:15980189,
CC       ECO:0000269|PubMed:18395997}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000305}.
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DR   EMBL; DQ201195; ABA54176.1; -; mRNA.
DR   EMBL; DP000086; AAP55048.2; -; Genomic_DNA.
DR   EMBL; AP008216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP014966; BAT12098.1; -; Genomic_DNA.
DR   EMBL; CM000147; EEE51412.1; -; Genomic_DNA.
DR   EMBL; AK243065; BAH01434.1; -; mRNA.
DR   RefSeq; XP_015614268.1; XM_015758782.1.
DR   AlphaFoldDB; Q7XC27; -.
DR   SMR; Q7XC27; -.
DR   STRING; 4530.OS10T0564800-01; -.
DR   PaxDb; Q7XC27; -.
DR   PRIDE; Q7XC27; -.
DR   EnsemblPlants; Os10t0564800-01; Os10t0564800-01; Os10g0564800.
DR   GeneID; 4349412; -.
DR   Gramene; Os10t0564800-01; Os10t0564800-01; Os10g0564800.
DR   KEGG; osa:4349412; -.
DR   eggNOG; KOG0034; Eukaryota.
DR   HOGENOM; CLU_061288_21_0_1; -.
DR   InParanoid; Q7XC27; -.
DR   OMA; PCMRDSA; -.
DR   OrthoDB; 1271942at2759; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000007752; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   Genevisible; Q7XC27; OS.
DR   GO; GO:0032578; C:aleurone grain membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
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; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   2: Evidence at transcript level;
KW   Calcium; Lipoprotein; Membrane; Metal-binding; Myristate;
KW   Reference proteome; Repeat; Vacuole.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..213
FT                   /note="Calcineurin B-like protein 1"
FT                   /id="PRO_0000337764"
FT   DOMAIN          31..66
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          67..102
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          104..139
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          148..183
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         117
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         121
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         163
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         165
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   SITE            140
FT                   /note="Involved in dimerization"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        58
FT                   /note="Q -> R (in Ref. 1; ABA54176)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   213 AA;  24497 MW;  A623943DB92D373E CRC64;
     MGCFQSTARR PRPGYEDPVG LASETAFSVS EVEALFELFK SISGSVIDDG LINKEEFQLA
     LFKNKRKENL FANRIFDLFD VKKRGVIDFG DFVRALNVFH PNIPMEEKID FSFKLYDMDN
     TGFIERKEVK QMLIALLGES EMRLSDEIIE TILDKTFSDA DTNQDGRIDR TEWENFVSRN
     PSLLKIMTLP YLKDITTTFP SFVFNSEVDD LVT
 
 
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