Q10KY3 (CAMK1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcium/calmodulin-dependent serine/threonine-protein kinase 1
EC=2.7.11.17

Alternative name(s):
Calcium/calmodulin-binding serine/threonine-protein kinase
Short name=CaM-binding protein kinase
OsCBK

Gene names

Name:	CAMK1
Ordered Locus Names:	Os03g0366200, LOC_Os03g25070

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	600 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Possesses kinase activity in vitro. Ref.1 Ref.5
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by the binding of calmodulin-like protein 1 (CML1) in the presence of Ca2+. Ref.5
Tissue specificity	Highly expressed in roots in the zone of cell division. Expressed in leaf mesophyll cells and at lower levels in mature stems. Ref.1
Developmental stage	Expressed at early stages of anther development in sporogenous cells and tapetum of anthers. Expression decreases in tapetum and increases in sporogenous cells at meiosis. At mature pollen stage, expressed in stigma, and then in proembryo after fertilization. Ref.1
Post-translational modification	Autophosphorylated. Ref.1 Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Sequence caution	The sequence BAF12093.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Domain	Repeat
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: InterPro calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 600	600	Calcium/calmodulin-dependent serine/threonine-protein kinase 1		PRO_0000338447
Regions
	Domain	147 – 409	263	Protein kinase
	Nucleotide binding	153 – 161	9	ATP By similarity
	Compositional bias	17 – 21	5	Poly-Glu
Sites
	Active site	275	1	Proton acceptor By similarity
	Binding site	179	1	ATP By similarity
Experimental info
	Sequence conflict	49 – 51	3	Missing in AAK54157. Ref.1
	Sequence conflict	556	1	E → G in AAK54157. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10KY3 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: C4AF86739ED5E701	FASTA	600	66,279
	10 20 30 40 50 60 MGLCHGKSAA VLEPTVEEEE EGATRVAEAA AAPAKPASPA PSAAAAAAAP AKPGTPKQHK 70 80 90 100 110 120 FPFYLPSPLP ASSYKGSPAN SSVASTPARG GFKRPFPPPS PAKHIRALLA RRHGSVKPNE 130 140 150 160 170 180 ASIPESGEPG VALDKGFGFS RHFAAKYELG REVGRGHFGY TCAATCKKGE LKGDDVAVKV 190 200 210 220 230 240 IPKAKMTTAI AIEDVRREVR ILSSLAGHSN LVQFYDAYED EENVYIVMEL CKGGELLDRI 250 260 270 280 290 300 LARGGKYSEE DAKVVMRQIL SVASFCHLQG VVHRDLKPEN FLFSSKDENS AMKVIDFGLS 310 320 330 340 350 360 DFVKPDERLN DIVGSAYYVA PEVLHRSYGT EADMWSIGVI VYILLCGSRP FWARTESGIF 370 380 390 400 410 420 RAVLKADPSF EEAPWPTLSA EAKDFVRRLL NKDYRKRMTA AQALCHPWIR GTEEVKLPLD 430 440 450 460 470 480 MIIYRLMRAY ISSSSLRRAA LRALAKTLTT DQIYYLREQF ELIGPNKSDL ITLQNLKTAL 490 500 510 520 530 540 MKNSTNAMKD SRVVDFVNTI SNIQYRKLDF EEFSAAAISV YQMEGLETWE QHARQAYEFF 550 560 570 580 590 600 DKEGNRPIVI DELASELGLG PSVPLHVVLQ DWIRHPDGKL SFLGFMKLLH GVSSRTIPKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and biochemical characterization of a calcium/calmodulin-binding protein kinase from rice." Zhang L., Liu B.-F., Liang S., Jones R.L., Lu Y.-T. Biochem. J. 368:145-157(2002) [PubMed: 12160464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION.
[2]	"Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species." The rice chromosome 3 sequencing consortium Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S. , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S. Genome Res. 15:1284-1291(2005) [PubMed: 16109971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed: 16100779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[4]	"The rice annotation project database (RAP-DB): 2008 update." The rice annotation project (RAP) Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed: 18089549] [Abstract] Cited for: GENOME REANNOTATION. Strain: cv. Nipponbare.
[5]	"Calmodulin isoform-specific activation of a rice calmodulin-binding kinase conferred by only three amino-acids of OsCaM61." Li D.-F., Li J., Ma L., Zhang L., Lu Y.-T. FEBS Lett. 580:4325-4331(2006) [PubMed: 16842786] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, AUTOPHOSPHORYLATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF368282 mRNA. Translation: AAK54157.1. DP000009 Genomic DNA. Translation: ABF96128.1. AP008209 Genomic DNA. Translation: BAF12093.1. Sequence problems.
RefSeq	NP_001050179.1. NM_001056714.1.
UniGene	Os.38188.
3D structure databases
ProteinModelPortal	Q10KY3.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2841546.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os03g25070.1; LOC_Os03g25070.1; LOC_Os03g25070.
GeneID	4332914.
KEGG	osa:4332914.
Organism-specific databases
Gramene	Q94KC3.
Phylogenomic databases
GeneTree	EPGT00050000027885.
HOGENOM	HBG755340.
OMA	AYEDEEN.
PhylomeDB	Q10KY3.
ProtClustDB	CLSN2693946.
Family and domain databases
InterPro	IPR011992. EF-hand-like_dom. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAMK1_ORYSJ

Accession

Primary (citable) accession number: Q10KY3
Secondary accession number(s): Q0DRP5, Q94KC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	August 22, 2006
Last modified:	September 21, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program