Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-39947-00614
Entry Name
UniProt Accession
Theoretical PI
5.93
Molecular Weight
59505.84
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calcium-dependent protein kinase isoform 2
Protein Synonyms/Alias
CDPK 2; 2.7.11.1;
Gene Name
CPK2
Gene Synonyms/Alias
Os07g0515100; LOC_Os07g33110; P0048D08.112;
Created Date
01-OCT-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGSCCSRAT
[1]
N-Myristoylation
Organism
Oryza sativa subsp. japonica (Rice)
NCBI Taxa ID
39947
Reference
[1] Martín ML, Busconi L. Membrane localization of a rice calcium-dependentprotein kinase (CDPK) is mediated by myristoylation and palmitoylation. Plant J. 2000 Nov;24(4):429-35. Review.[PMID:11115124]
Functional Description
May play a role in signal transduction pathways that involve calcium as a second messenger.
Sequence Annotation
Domain: 85 343 Protein kinase.
Domain: 385 420 EF-hand 1.
Domain: 421 456 EF-hand 2.
Domain: 457 492 EF-hand 3.
Domain: 493 527 EF-hand 4.
Nucleotide-binding: 91 99 ATP.
Region: 348 378 Autoinhibitory domain.
Active site: 209 209 Proton acceptor.
Binding site: 114 114 ATP.
Protein Length
533 AA.
Protein Sequence
(Canonical)
MGSCCSRATS PDSGRGGANG YGYSHQTKPA QTTPSYNHPQ PPPPAEVRYT PSAMNPPVVP  60
PVVAPPKPTP DTILGKPYDD VRSVYSLGKE LGRGQFGVTY LCTEIASGKQ YACKSISKRK  120
LVSKADKEDI RREIQIMQHL SGQQNIVEFR GAYEDKSNVH VVMELCAGGE LFDRIIAKGH  180
YSERAAATIC RAVVNVVNIC HFMGVMHRDL KPENFLLATK EENAMLKATD FGLSVFIEEG  240
KMYRDIVGSA YYVAPEVLRR NYGKEIDVWS AGVILYILLS GVPPFWAETE KGIFDAILQG  300
EIDFESQPWP SISESAKDLV RKMLTQDPKK RITSAQVLQH PWLRDGEASD KPIDSAVLSR  360
MKQFRAMNKL KKMALKVIAS NLNEEEIKGL KQMFTNMDTD NSGTITYEEL KAGLAKLGSK  420
LSEAEVKQLM EAADVDGNGS IDYVEFITAT MHRHKLERDE HLFKAFQYFD KDNSGFITRD  480
ELESALIEHE MGDTSTIKDI ISEVDTDNDG RINYEEFCAM MRGGGMQQPM RLK         533
FASTA
(Canonical)
>LipidDB-39947-00614|P53683
MGSCCSRATSPDSGRGGANGYGYSHQTKPAQTTPSYNHPQPPPPAEVRYTPSAMNPPVVP
PVVAPPKPTPDTILGKPYDDVRSVYSLGKELGRGQFGVTYLCTEIASGKQYACKSISKRK
LVSKADKEDIRREIQIMQHLSGQQNIVEFRGAYEDKSNVHVVMELCAGGELFDRIIAKGH
YSERAAATICRAVVNVVNICHFMGVMHRDLKPENFLLATKEENAMLKATDFGLSVFIEEG
KMYRDIVGSAYYVAPEVLRRNYGKEIDVWSAGVILYILLSGVPPFWAETEKGIFDAILQG
EIDFESQPWPSISESAKDLVRKMLTQDPKKRITSAQVLQHPWLRDGEASDKPIDSAVLSR
MKQFRAMNKLKKMALKVIASNLNEEEIKGLKQMFTNMDTDNSGTITYEELKAGLAKLGSK
LSEAEVKQLMEAADVDGNGSIDYVEFITATMHRHKLERDEHLFKAFQYFDKDNSGFITRD
ELESALIEHEMGDTSTIKDIISEVDTDNDGRINYEEFCAMMRGGGMQQPMRLK
Gene Ontology
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW
Interpro
InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR018247; EF_Hand_1_Ca_BS
InterPro; IPR002048; EF_hand_dom
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR002290; Ser/Thr_dual-sp_kinase
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF13499; EF-hand_7;
Pfam; PF00069; Pkinase;
SMART
SMART; SM00054; EFh;
SMART; SM00220; S_TKc;
PROSITE
PROSITE; PS00018; EF_HAND_1;
PROSITE; PS50222; EF_HAND_2;
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS