Reviewed, UniProtKB/Swiss-Prot Q43531 (CCAMK_LILLO)

Names and origin

Protein names

Recommended name:
    Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase
      Short name=LlCCaMK
    EC=2.7.11.17

Gene names

Name:

CCAMK

Organism

Lilium longiflorum (Trumpet lily)

Taxonomic identifier

4690 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Liliales › Liliaceae › Lilium

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase that may be involved in microsporogenesis. Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by calcium/calmodulin binding after calcium-induced autophosphorylation. Autophosphorylation is associated with a time-dependent loss of kinase activity sensitive to reaction pH and ATP concentration. In vitro inactivation leads to the formation of network-like structures. Ref.2 Ref.4
Subcellular location	Membrane; Single-pass membrane protein Potential.
Developmental stage	Expressed during anther development. Ref.1
Post-translational modification	Autophosphorylation stimulated by calcium and inhibited by calcium/calmodulin. Occurs probably by an intermolecular mechanism.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Contains 3 EF-hand domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Coiled coil Repeat Transmembrane
Ligand	ATP-binding Calcium Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 520	520	Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase		PRO_0000085698
Regions
	Transmembrane	227 – 243	17	Potential
	Domain	13 – 302	290	Protein kinase
	Domain	396 – 431	36	EF-hand 1
	Domain	432 – 467	36	EF-hand 2
	Domain	474 – 509	36	EF-hand 3
	Nucleotide binding	19 – 27	9	ATP By similarity
	Calcium binding	409 – 420	12	1 Potential
	Calcium binding	445 – 456	12	2 Potential
	Calcium binding	487 – 498	12	3 Potential
	Region	325 – 338	14	Calmodulin-binding
	Coiled coil	346 – 368	23	Potential
Sites
	Active site	167	1	Proton acceptor By similarity
	Binding site	44	1	ATP By similarity
Amino acid modifications
	Modified residue	267	1	Phosphothreonine
Experimental info
	Mutagenesis	267	1	T → A: Loss of calcium/calmodulin-stimulated kinase activity. Ref.3
	Mutagenesis	417	1	D → A: No effect. Ref.2
	Mutagenesis	453	1	S → A: Decreased calcium binding. Ref.2
	Mutagenesis	495	1	T → A: No calcium binding. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q43531-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6D583FD61C1453C4	FASTA	520	57,887
	10 20 30 40 50 60 MSRHESRKLS DDYEVVDVLG KGGFSVVRRG ISKSRGKNND VAIKTLRRYG YTLPGAQRSQ 70 80 90 100 110 120 PGQRGLSPLG MPTLKQVSVS DALLTNEILV MRRIVEDVSP HPNVIHLHDV YEDANGVHLV 130 140 150 160 170 180 LELCSGGELF DRIVAQDRYS ESEAAEVVQQ IASGLAALHK STIIHRDLKP ENCLFLNQEK 190 200 210 220 230 240 RSTLKIMDFG LSSVEDFTDP IVALFGSIDY VSPEALSQRQ VSSASDMWSL GVILYILLSG 250 260 270 280 290 300 CPPFHAPSNR EKQQRILAGD FSFEEHTWKT ITSSAKDLIS SLLSVDPYKR PTANDLLKHP 310 320 330 340 350 360 WVIGDSAKQE LIEPEVVSRL RSFNARRKLR AAAIASVLSS KVLLRTKKLK NLLGSHDMKS 370 380 390 400 410 420 EELENLRAHF KRICANGDNA TLPEFEEVLK AMKMNSLIPL APRVFDLFDN NRDGTIDMRE 430 440 450 460 470 480 ILCGLSNLRN SQGDDALQLC FQMYDADRSG CISKEELASM LRALPEDCVP ADITEPGKLD 490 500 510 520 EIFDQMDANS DGVVTFDEFK AAMQRDSSLQ DVVLSSLRTI

References

[1]	"Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain." Patil S., Takezawa D., Poovaiah B.W. Proc. Natl. Acad. Sci. U.S.A. 92:4897-4901(1995) [PubMed: 7761420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Strain: cv. Nellie white. Tissue: Anther.
[2]	"Dual regulation of a chimeric plant serine/threonine kinase by calcium and calcium/calmodulin." Takezawa D., Ramachandiran S., Paranjape V., Poovaiah B.W. J. Biol. Chem. 271:8126-8132(1996) [PubMed: 8626500] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF ASP-417; SER-453 AND THR-495, ENZYME REGULATION.
[3]	"Calcium-stimulated autophosphorylation site of plant chimeric calcium/calmodulin-dependent protein kinase." Sathyanarayanan P.V., Siems W.F., Jones J.P., Poovaiah B.W. J. Biol. Chem. 276:32940-32947(2001) [PubMed: 11399751] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS OF THR-267.
[4]	"Autophosphorylation-dependent inactivation of plant chimeric calcium/calmodulin-dependent protein kinase." Sathyanarayanan P.V., Poovaiah B.W. Eur. J. Biochem. 269:2457-2463(2002) [PubMed: 12027883] [Abstract] Cited for: ENZYME REGULATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U24188 mRNA. Translation: AAC49008.1.
3D structure databases
SMR	Q43531. Positions 5-332, 256-503, 358-517.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.11.17. 1959.
Family and domain databases
InterPro	IPR020642. Ca-dep_prot_kinase. IPR020636. Ca/CaM-dep_prot_kinase-like. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001125. Recoverin. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PANTHER	PTHR22982:SF13. Ca-dep_prot_kinase. 1 hit. PTHR22982. Ca/CaM-dep_prot_kinase-like. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00450. RECOVERIN.
SMART	SM00054. EFh. 3 hits. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 3 hits. PS50222. EF_HAND_2. 4 hits. 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

CCAMK_LILLO

Accession

Primary (citable) accession number: Q43531

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)