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Calcium/calmodulin-dependent protein kinase type II subunit delta (CaM kinase II subunit delta) (CaMK-II subunit delta) (EC 2.7.11.17)

 KCC2D_BOVIN             Reviewed;         488 AA.
Q2HJF7;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 1.
22-NOV-2017, entry version 107.
RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit delta;
Short=CaM kinase II subunit delta;
Short=CaMK-II subunit delta;
EC=2.7.11.17;
Name=CAMK2D;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Heart ventricle;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Calcium/calmodulin-dependent protein kinase involved in
the regulation of Ca(2+) homeostatis and excitation-contraction
coupling (ECC) in heart by targeting ion channels, transporters
and accessory proteins involved in Ca(2+) influx into the myocyte,
Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+)
uptake and Na(+) and K(+) channel transport. Targets also
transcription factors and signaling molecules to regulate heart
function. In its activated form, is involved in the pathogenesis
of dilated cardiomyopathy and heart failure. Contributes to
cardiac decompensation and heart failure by regulating SR Ca(2+)
release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-
2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4,
promoting its nuclear export and binding to 14-3-3 protein, and
expression of MEF2 and genes involved in the hypertrophic program.
Is essential for left ventricular remodeling responses to
myocardial infarction. In pathological myocardial remodeling acts
downstream of the beta adrenergic receptor signaling cascade to
regulate key proteins involved in ECC. Regulates Ca(2+) influx to
myocytes by binding and phosphorylating the L-type Ca(2+) channel
subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target
and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A
and the K+ channel Kv4.3/KCND3, which contribute to
arrhythmogenesis in heart failure. Phosphorylates phospholamban
(PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing
to the enhancement of SR Ca(2+) uptake that may be important in
frequency-dependent acceleration of relaxation (FDAR) and
maintenance of contractile function during acidosis. May
participate in the modulation of skeletal muscle function in
response to exercise, by regulating SR Ca(2+) transport through
phosphorylation of PLN/PLB and triadin, a ryanodine receptor-
coupling factor (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
calmodulin results in conformational change that relieves
intrasteric autoinhibition and allows autophosphorylation of Thr-
287 which turns the kinase in a constitutively active form and
confers to the kinase a Ca(2+)-independent activity.
-!- SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A),
beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different
isoforms assemble into homo- or heteromultimeric holoenzymes
composed of 12 subunits with two hexameric rings stacked one on
top of the other. Interacts with RRAD and CACNB2 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305};
Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
{ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305};
Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
{ECO:0000305}.
-!- DOMAIN: The CAMK2 protein kinases contain a unique C-terminal
subunit association domain responsible for oligomerization.
-!- PTM: Autophosphorylation of Thr-287 following activation by
Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase
into an activated state (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC105459; AAI05460.1; -; mRNA.
RefSeq; NP_001039798.1; NM_001046333.1.
UniGene; Bt.58299; -.
ProteinModelPortal; Q2HJF7; -.
SMR; Q2HJF7; -.
STRING; 9913.ENSBTAP00000039621; -.
PaxDb; Q2HJF7; -.
PeptideAtlas; Q2HJF7; -.
PRIDE; Q2HJF7; -.
Ensembl; ENSBTAT00000039835; ENSBTAP00000039621; ENSBTAG00000014463.
GeneID; 532713; -.
KEGG; bta:532713; -.
CTD; 817; -.
eggNOG; KOG0033; Eukaryota.
eggNOG; ENOG410XNRX; LUCA.
GeneTree; ENSGT00760000118944; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG108055; -.
InParanoid; Q2HJF7; -.
KO; K04515; -.
OMA; CHVNGIV; -.
OrthoDB; EOG091G0SCS; -.
TreeFam; TF315229; -.
Proteomes; UP000009136; Chromosome 6.
Bgee; ENSBTAG00000014463; -.
ExpressionAtlas; Q2HJF7; baseline and differential.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0060341; P:regulation of cellular localization; ISS:UniProtKB.
InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR032710; NTF2-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF08332; CaMKII_AD; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF54427; SSF54427; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; Calmodulin-binding; Cell membrane;
Complete proteome; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q13557}.
CHAIN 2 488 Calcium/calmodulin-dependent protein
kinase type II subunit delta.
/FTId=PRO_0000277816.
DOMAIN 14 272 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 20 28 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 283 292 Autoinhibitory domain. {ECO:0000250}.
REGION 291 301 Calmodulin-binding. {ECO:0000250}.
COMPBIAS 331 334 Poly-Ser.
ACT_SITE 136 136 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 43 43 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q13557}.
MOD_RES 287 287 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13557}.
MOD_RES 306 306 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 307 307 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q13557}.
MOD_RES 317 317 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q6PHZ2}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:Q13557}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000250|UniProtKB:Q13557}.
MOD_RES 341 341 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13557}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PHZ2}.
MOD_RES 346 346 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PHZ2}.
MOD_RES 347 347 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13557}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000250|UniProtKB:Q13557}.
SEQUENCE 488 AA; 55293 MW; 3D4D3A8D1F778F21 CRC64;
MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL SARDHQKLER
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
LESVNHCHLN GIVHRDLKPE NLLLASKSKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY
LSPEVLRKDP YGKPVDMWAC GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT
VTPEAKDLIN KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL
KGAILTTMLA TRNFSAKSLL KKPDGVKKRK SSSSVQMMES TESSNTTIED EDVKARKQEI
IKVTEQLIEA INNGDFEAYT KICDPGLTAF EPEALGNLVE GMDFHRFYFE NALSKSNKPI
HTIILNPHVH LVGDDAACIA YIRLTQYMDG SGMPKTMQSE ETRVWHRRDG KWQNVHFHRS
GSPTVPIN


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