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CDPKD_ORYSJ
ID   CDPKD_ORYSJ             Reviewed;         551 AA.
AC   Q9FXQ3; Q0JAQ3; Q7X828;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Calcium-dependent protein kinase 13 {ECO:0000305};
DE            Short=OsCDPK13 {ECO:0000305};
DE            Short=OsCPK13 {ECO:0000303|PubMed:15695435};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=Calcium-dependent protein kinase OsCDPK7 {ECO:0000303|PubMed:10929125};
GN   Name=CPK13 {ECO:0000303|PubMed:15695435};
GN   OrderedLocusNames=Os04g0584600 {ECO:0000312|EMBL:BAS90683.1},
GN   LOC_Os04g49510 {ECO:0000305};
GN   ORFNames=OSJNBa0013K16.2 {ECO:0000312|EMBL:CAE03753.2};
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] (ISOFORM 1), FUNCTION, AND INDUCTION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=10929125; DOI=10.1046/j.1365-313x.2000.00787.x;
RA   Saijo Y., Hata S., Kyozuka J., Shimamoto K., Izui K.;
RT   "Over-expression of a single Ca2+-dependent protein kinase confers both
RT   cold and salt/drought tolerance on rice plants.";
RL   Plant J. 23:319-327(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
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 MRNA] (ISOFORM 1).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=11726707; DOI=10.1093/pcp/pce158;
RA   Saijo Y., Kinoshita N., Ishiyama K., Hata S., Kyozuka J., Hayakawa T.,
RA   Nakamura T., Shimamoto K., Yamaya T., Izui K.;
RT   "A Ca(2+)-dependent protein kinase that endows rice plants with cold- and
RT   salt-stress tolerance functions in vascular bundles.";
RL   Plant Cell Physiol. 42:1228-1233(2001).
RN   [8]
RP   INDUCTION BY N-ACETYLCHITOOLIGOSACCHARIDE ELICITOR.
RX   PubMed=12956525; DOI=10.1023/a:1024890601888;
RA   Akimoto-Tomiyama C., Sakata K., Yazaki J., Nakamura K., Fujii F.,
RA   Shimbo K., Yamamoto K., Sasaki T., Kishimoto N., Kikuchi S., Shibuya N.,
RA   Minami E.;
RT   "Rice gene expression in response to N-acetylchitooligosaccharide elicitor:
RT   comprehensive analysis by DNA microarray with randomly selected ESTs.";
RL   Plant Mol. Biol. 52:537-551(2003).
RN   [9]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15695435; DOI=10.1093/pcp/pci035;
RA   Asano T., Tanaka N., Yang G., Hayashi N., Komatsu S.;
RT   "Genome-wide identification of the rice calcium-dependent protein kinase
RT   and its closely related kinase gene families: comprehensive analysis of the
RT   CDPKs gene family in rice.";
RL   Plant Cell Physiol. 46:356-366(2005).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=21136139; DOI=10.1007/s11103-010-9717-1;
RA   Asano T., Hakata M., Nakamura H., Aoki N., Komatsu S., Ichikawa H.,
RA   Hirochika H., Ohsugi R.;
RT   "Functional characterisation of OsCPK21, a calcium-dependent protein kinase
RT   that confers salt tolerance in rice.";
RL   Plant Mol. Biol. 75:179-191(2011).
RN   [11]
RP   INDUCTION BY UV-C.
RX   PubMed=24035516; DOI=10.1016/j.phytochem.2013.08.012;
RA   Park H.L., Lee S.W., Jung K.H., Hahn T.R., Cho M.H.;
RT   "Transcriptomic analysis of UV-treated rice leaves reveals UV-induced
RT   phytoalexin biosynthetic pathways and their regulatory networks in rice.";
RL   Phytochemistry 96:57-71(2013).
CC   -!- FUNCTION: May play a role in signal transduction pathways that involve
CC       calcium as a second messenger (By similarity). May function in signal
CC       transduction pathways that positively regulate responses to cold, salt
CC       and drought stresses (PubMed:10929125). {ECO:0000250|UniProtKB:Q06850,
CC       ECO:0000269|PubMed:10929125}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000305};
CC   -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play
CC       an important role in the regulation of the kinase activity.
CC       {ECO:0000250|UniProtKB:Q06850}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FXQ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FXQ3-2; Sequence=VSP_058555;
CC   -!- TISSUE SPECIFICITY: Expressed in vascular tissues of crowns and roots,
CC       vascular bundles and central cylinder (PubMed:11726707). Expressed in
CC       roots, leaf blades, spikelets and developing seeds (PubMed:21136139).
CC       {ECO:0000269|PubMed:11726707, ECO:0000269|PubMed:21136139}.
CC   -!- INDUCTION: By cold and salt stresses (PubMed:10929125). Induced by N-
CC       acetylchitooligosaccharide elicitor (PubMed:12956525). Induced by UV-C
CC       (PubMed:24035516). {ECO:0000269|PubMed:10929125,
CC       ECO:0000269|PubMed:12956525, ECO:0000269|PubMed:24035516}.
CC   -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily:
CC       a kinase domain, an autoinhibitory (junction) domain and a calmodulin-
CC       like domain. The autoinhibitory domain (352-382) inactivates kinase
CC       activity under calcium-free conditions. {ECO:0000250|UniProtKB:Q06850}.
CC   -!- MISCELLANEOUS: Plants over-expressing CPK13 display enhanced tolerance
CC       to cold, drought and salt stresses. {ECO:0000269|PubMed:10929125}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDPK subfamily. {ECO:0000305}.
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DR   EMBL; AB042550; BAB16888.1; -; mRNA.
DR   EMBL; AL662957; CAE03753.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF15584.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS90683.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS90684.1; -; Genomic_DNA.
DR   EMBL; AK061881; BAG88162.1; -; mRNA.
DR   RefSeq; XP_015635476.1; XM_015779990.1. [Q9FXQ3-1]
DR   AlphaFoldDB; Q9FXQ3; -.
DR   SMR; Q9FXQ3; -.
DR   STRING; 4530.OS04T0584600-02; -.
DR   PaxDb; Q9FXQ3; -.
DR   PRIDE; Q9FXQ3; -.
DR   EnsemblPlants; Os04t0584600-01; Os04t0584600-01; Os04g0584600. [Q9FXQ3-2]
DR   EnsemblPlants; Os04t0584600-02; Os04t0584600-02; Os04g0584600. [Q9FXQ3-1]
DR   GeneID; 4336783; -.
DR   Gramene; Os04t0584600-01; Os04t0584600-01; Os04g0584600. [Q9FXQ3-2]
DR   Gramene; Os04t0584600-02; Os04t0584600-02; Os04g0584600. [Q9FXQ3-1]
DR   KEGG; osa:4336783; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   HOGENOM; CLU_000288_37_3_1; -.
DR   InParanoid; Q9FXQ3; -.
DR   OMA; WPLISNS; -.
DR   OrthoDB; 330091at2759; -.
DR   PlantReactome; R-ADU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-AHA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-AIP-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ALY-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ATA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ATH-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-BDI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-BNA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-BOL-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-BRA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-BVU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CAN-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CAR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CCA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CCL-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CCN-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CCP-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CLA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-COL-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CRU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CSA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CSC-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CSI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-CSK-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-DCA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ECU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-EGR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ETE-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-FVE-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-GMA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-GRA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-HLP-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-HVU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ITR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-JCU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-LAN-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-LPE-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-MAC-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-MES-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-MGU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-MTR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-NAT-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-NNU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OAU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OBA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OBR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OGL-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OGR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OGU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OLO-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OME-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OMI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ONI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OOF-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OPU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ORU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR   PlantReactome; R-OSA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-OSI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PAB-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PAV-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PDA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PED-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PHA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PHH-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PPE-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PTA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PTI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PVE-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-PVU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-SBI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-SHI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-SIT-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-SLY-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-STU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-TAE-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-TCA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-TDI-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-TPR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-TTU-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-TUR-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-VAN-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-VRA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-VVN-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ZJA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ZMA-9607185; Generation of superoxide radicals.
DR   PlantReactome; R-ZMY-9607185; Generation of superoxide radicals.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   ExpressionAtlas; Q9FXQ3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR   GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR   GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00054; EFh; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Calcium; Kinase; Lipoprotein; Membrane;
KW   Metal-binding; Myristate; Nucleotide-binding; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..551
FT                   /note="Calcium-dependent protein kinase 13"
FT                   /id="PRO_0000437557"
FT   DOMAIN          88..346
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          389..424
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          425..460
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          461..496
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          497..530
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          15..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..382
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q06850"
FT   COMPBIAS        15..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        212
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         94..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         402
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         404
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         406
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         413
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         438
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         440
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         442
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         444
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         449
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         474
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         476
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         478
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         480
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         485
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         508
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         510
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         512
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         514
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         519
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         51..85
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058555"
SQ   SEQUENCE   551 AA;  60966 MW;  E479A089EF287A7B CRC64;
     MGNACGGSLR SKYLSFKQTA SQRHDTDDNN NAAAADSPKK PSRPPAAAKT DDHPVSASAP
     AAAMRRGQAP ADLGSVLGHP TPNLRDLYAM GRKLGQGQFG TTYLCTELST GVDYACKSIS
     KRKLITKEDI EDVRREIQIM HHLSGHKNVV AIKGAYEDQL YVHIVMELCA GGELFDRIIQ
     RGHYSERKAA ELTRIIVGVV EACHSLGVMH RDLKPENFLL ANKDDDLSLK AIDFGLSVFF
     KPGQTFTDVV GSPYYVAPEV LLKHYGPEAD VWTAGVILYI LLSGVPPFWA ETQQGIFDAV
     LKGFIDFDSD PWPVISESAK DLITKMLNPR PKERLTAHEV LCHPWIRDHG VAPDRPLDPA
     VLSRIKQFSA MNKLKKMALR VIAESLSEEE IAGLKEMFQT MDADNSGAIT YDELKEGLRK
     YGSTLKDTEI RDLMDAADID NSGTIDYIEF IAATLHLNKL EREEHLVAAF SYFDKDGSGY
     ITVDELQQAC KEHNMPDAFL DDVINEADQD NDGRIDYGEF VAMMTKGNMG VGRRTMRNSL
     NISMRDAPGA L
 
 
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