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