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

 KCC2G_RAT               Reviewed;         527 AA.
P11730; Q64003; Q64004;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
30-AUG-2017, entry version 153.
RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit gamma;
Short=CaM kinase II subunit gamma;
Short=CaMK-II subunit gamma;
EC=2.7.11.17;
Name=Camk2g;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Brain;
PubMed=2846534;
Tobimatsu T., Kameshita I., Fujisawa H.;
"Molecular cloning of the cDNA encoding the third polypeptide (gamma)
of brain calmodulin-dependent protein kinase II.";
J. Biol. Chem. 263:16082-16086(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C).
TISSUE=Aortic smooth muscle;
PubMed=8172610; DOI=10.1042/bj2990489;
Zhou Z.L., Ikebe M.;
"New isoforms of Ca2+/calmodulin-dependent protein kinase II in smooth
muscle.";
Biochem. J. 299:489-495(1994).
[3]
INDUCTION BY COCAINE.
PubMed=16891908; DOI=10.1097/01.fjc.0000211796.45281.46;
Henning R.J., Cuevas J.;
"Cocaine activates calcium/calmodulin kinase II and causes
cardiomyocyte hypertrophy.";
J. Cardiovasc. Pharmacol. 48:802-813(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-321; SER-325;
SER-329; SER-355 AND SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Calcium/calmodulin-dependent protein kinase that
functions autonomously after Ca(2+)/calmodulin-binding and
autophosphorylation, and is involved in sarcoplasmic reticulum
Ca(2+) transport in skeletal muscle and may function in dendritic
spine and synapse formation and neuronal plasticity. In slow-
twitch muscles, is involved in regulation of sarcoplasmic
reticulum (SR) Ca(2+) transport and in fast-twitch muscle
participates in the control of Ca(2+) release from the SR through
phosphorylation of the ryanodine receptor-coupling factor triadin.
In neurons, may participate in the promotion of dendritic spine
and synapse formation and maintenance of synaptic plasticity which
enables long-term potentiation (LTP) and hippocampus-dependent
learning (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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=A;
IsoId=P11730-1; Sequence=Displayed;
Name=B;
IsoId=P11730-2; Sequence=VSP_004781, VSP_004782;
Name=C;
IsoId=P11730-3; Sequence=VSP_004781, VSP_004783;
-!- INDUCTION: By cocaine in cardiomyocytes.
{ECO:0000269|PubMed:16891908}.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J04063; AAA41857.1; -; mRNA.
EMBL; S71570; AAB30670.1; -; mRNA.
EMBL; S71571; AAB30671.1; -; mRNA.
PIR; A31908; A31908.
PIR; S43845; S43845.
RefSeq; NP_598289.1; NM_133605.1. [P11730-1]
RefSeq; XP_008768721.1; XM_008770499.2. [P11730-3]
UniGene; Rn.10961; -.
ProteinModelPortal; P11730; -.
SMR; P11730; -.
BioGrid; 251145; 3.
IntAct; P11730; 1.
STRING; 10116.ENSRNOP00000062321; -.
ChEMBL; CHEMBL2111382; -.
iPTMnet; P11730; -.
PhosphoSitePlus; P11730; -.
PaxDb; P11730; -.
PRIDE; P11730; -.
Ensembl; ENSRNOT00000066163; ENSRNOP00000062321; ENSRNOG00000009783. [P11730-1]
GeneID; 171140; -.
KEGG; rno:171140; -.
UCSC; RGD:621802; rat. [P11730-1]
CTD; 818; -.
RGD; 621802; Camk2g.
eggNOG; KOG0033; Eukaryota.
eggNOG; ENOG410XNRX; LUCA.
GeneTree; ENSGT00760000118944; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG108055; -.
InParanoid; P11730; -.
KO; K04515; -.
OMA; DASHCIN; -.
PhylomeDB; P11730; -.
BRENDA; 2.7.11.17; 5301.
Reactome; R-RNO-3371571; HSF1-dependent transactivation.
Reactome; R-RNO-399719; Trafficking of AMPA receptors.
Reactome; R-RNO-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-RNO-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-RNO-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-RNO-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
Reactome; R-RNO-5578775; Ion homeostasis.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-877300; Interferon gamma signaling.
Reactome; R-RNO-936837; Ion transport by P-type ATPases.
PRO; PR:P11730; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000009783; -.
ExpressionAtlas; P11730; baseline and differential.
Genevisible; P11730; RN.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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; IDA:RGD.
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:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; TAS:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032710; NTF2-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24347; PTHR24347; 1.
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.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calmodulin-binding;
Complete proteome; Developmental protein; Differentiation; Kinase;
Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein;
Reference proteome; Sarcoplasmic reticulum;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 527 Calcium/calmodulin-dependent protein
kinase type II subunit gamma.
/FTId=PRO_0000086103.
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}.
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 287 287 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13555}.
MOD_RES 306 306 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 307 307 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 316 336 Missing (in isoform B and isoform C).
{ECO:0000303|PubMed:8172610}.
/FTId=VSP_004781.
VAR_SEQ 351 361 KKRKSSSSVHL -> PEQQQKQSRKPSPRARDPLQTA (in
isoform B). {ECO:0000303|PubMed:8172610}.
/FTId=VSP_004782.
VAR_SEQ 352 362 Missing (in isoform C).
{ECO:0000303|PubMed:8172610}.
/FTId=VSP_004783.
CONFLICT 2 2 A -> E (in Ref. 2; AAB30670/AAB30671).
{ECO:0000305}.
SEQUENCE 527 AA; 59038 MW; 58DBF1B72F64FA31 CRC64;
MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL SARDHQKLER
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIHQI
LESVNHIHQH DIVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY
LSPEVLRKDP YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL
KGAILTTMLV SRNFSVGRQS SAPASPAASA AGLAGQAAKS LLNKKSDGGV KKRKSSSSVH
LMEPQTTVVH NATDGIKGST ESCNTTTEDE DLKVRKQEII KITEQLIEAI NNGDFEAYTK
ICDPGLTSFE PEALGNLVEG MDFHKFYFEN LLSKNSKPIH TTILNPHVHV IGEDAACIAY
IRLTQYIDGQ GRPRTSQSEE TRVWHRRDGK WLNVHYHCSG APAAPLQ


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