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CNBL7_ORYSJ
ID   CNBL7_ORYSJ             Reviewed;         213 AA.
AC   Q3HRP0; A0A0N7KF45; Q6K876;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Calcineurin B-like protein 7;
GN   Name=CBL7; OrderedLocusNames=Os02g0291000, LOC_Os02g18880;
GN   ORFNames=OJ1086_G08.10;
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=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   [3]
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   [4]
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   [5]
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   [6]
RP   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: Cell membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC       {ECO:0000269|PubMed:18395997}.
CC   -!- INDUCTION: By salt, drought and cold stresses, and abscisic acid (ABA).
CC       {ECO:0000269|PubMed:18395997}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21753.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF08507.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ201201; ABA54182.1; -; mRNA.
DR   EMBL; AP004212; BAD21753.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008208; BAF08507.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014958; BAS78193.1; -; Genomic_DNA.
DR   RefSeq; XP_015623172.1; XM_015767686.1.
DR   RefSeq; XP_015623173.1; XM_015767687.1.
DR   AlphaFoldDB; Q3HRP0; -.
DR   SMR; Q3HRP0; -.
DR   BioGRID; 798097; 16.
DR   STRING; 4530.OS02T0291000-00; -.
DR   PaxDb; Q3HRP0; -.
DR   PRIDE; Q3HRP0; -.
DR   EnsemblPlants; Os02t0291000-00; Os02t0291000-00; Os02g0291000.
DR   GeneID; 107276277; -.
DR   Gramene; Os02t0291000-00; Os02t0291000-00; Os02g0291000.
DR   KEGG; osa:107276277; -.
DR   eggNOG; KOG0034; Eukaryota.
DR   HOGENOM; CLU_061288_21_0_1; -.
DR   InParanoid; Q3HRP0; -.
DR   OMA; NIFHPET; -.
DR   OrthoDB; 1271942at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q3HRP0; OS.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Pfam; PF13833; EF-hand_8; 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   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding; Myristate;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..213
FT                   /note="Calcineurin B-like protein 7"
FT                   /id="PRO_0000337770"
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         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         163
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
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         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
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:0000250"
SQ   SEQUENCE   213 AA;  24400 MW;  FBF1EB6D810E9CF2 CRC64;
     MGCISSKQFK RAAEHEDPAI LAKETTFSVS EVEALYELFK KISHSIFKDG LIHKEEFQLA
     LFRNSNKKNL FADRIFDLFD LKRNGVIDFG EFVRSLNIFH PETPLAEKIA FAFRLYDLRG
     TGYIEREELY EMVLAILNES DLLLSDDAVE QIVDQTFKQA DLNSDGKIDP DEWKAFASKN
     PALLKNMTLP YLKDITMAFP SFVLNSGVDD EEL
 
 
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