KCC1G_MOUSE
ID KCC1G_MOUSE Reviewed; 477 AA.
AC Q91VB2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1G;
DE EC=2.7.11.17;
DE AltName: Full=CaM kinase I gamma;
DE Short=CaM kinase IG;
DE Short=CaM-KI gamma;
DE Short=CaMKI gamma;
DE Short=CaMKIG;
DE AltName: Full=CaMK-like CREB kinase III;
DE Short=CLICK III;
GN Name=Camk1g;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP ACTIVITY REGULATION, MUTAGENESIS OF CYS-474, PHOSPHORYLATION BY CAMKK1,
RP PHOSPHORYLATION OF CREB1, ISOPRENYLATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12637513; DOI=10.1074/jbc.m300578200;
RA Takemoto-Kimura S., Terai H., Takamoto M., Ohmae S., Kikumura S., Segi E.,
RA Arakawa Y., Furuyashiki T., Narumiya S., Bito H.;
RT "Molecular cloning and characterization of CLICK-III/CaMKIgamma, a novel
RT membrane-anchored neuronal Ca2+/calmodulin-dependent protein kinase
RT (CaMK).";
RL J. Biol. Chem. 278:18597-18605(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RA Bjork B.C., Watanabe Y., Murray J.C., Schutte B.C.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a
CC proposed calcium-triggered signaling cascade. In vitro phosphorylates
CC transcription factor CREB1.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17;
CC Evidence={ECO:0000269|PubMed:12637513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.17; Evidence={ECO:0000269|PubMed:12637513};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC calmodulin is thought to result in a conformational change and leads to
CC activation through phosphorylation by CAMKK1.
CC {ECO:0000269|PubMed:12637513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12637513}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:12637513}; Peripheral membrane
CC protein {ECO:0000269|PubMed:12637513}. Cell membrane
CC {ECO:0000269|PubMed:12637513}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12637513}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, in neuronal cell bodies
CC of the central nucleus of amygdala and ventromedial hypothalamic
CC nucleus. Also detected in heart, testis, and kidney.
CC {ECO:0000269|PubMed:12637513}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 11 dpc in parallel with the
CC onset of development of the central nervous system.
CC {ECO:0000269|PubMed:12637513}.
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and interacts in the inactive folded state with the catalytic
CC domain as a pseudosubstrate. {ECO:0000250}.
CC -!- PTM: May be prenylated on Cys-474. {ECO:0000269|PubMed:12637513}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AY212936; AAP29965.1; -; mRNA.
DR EMBL; AF428262; AAL28101.1; -; mRNA.
DR EMBL; BC021840; AAH21840.1; -; mRNA.
DR CCDS; CCDS15638.1; -.
DR RefSeq; NP_659066.1; NM_144817.2.
DR AlphaFoldDB; Q91VB2; -.
DR SMR; Q91VB2; -.
DR STRING; 10090.ENSMUSP00000016323; -.
DR iPTMnet; Q91VB2; -.
DR PhosphoSitePlus; Q91VB2; -.
DR SwissPalm; Q91VB2; -.
DR MaxQB; Q91VB2; -.
DR PaxDb; Q91VB2; -.
DR PRIDE; Q91VB2; -.
DR ProteomicsDB; 263486; -.
DR Antibodypedia; 20698; 305 antibodies from 30 providers.
DR DNASU; 215303; -.
DR Ensembl; ENSMUST00000016323; ENSMUSP00000016323; ENSMUSG00000016179.
DR GeneID; 215303; -.
DR KEGG; mmu:215303; -.
DR UCSC; uc007eel.1; mouse.
DR CTD; 57172; -.
DR MGI; MGI:2388073; Camk1g.
DR VEuPathDB; HostDB:ENSMUSG00000016179; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000156872; -.
DR InParanoid; Q91VB2; -.
DR OMA; TGVCAIM; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q91VB2; -.
DR TreeFam; TF314166; -.
DR BRENDA; 2.7.11.17; 3474.
DR BioGRID-ORCS; 215303; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q91VB2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91VB2; protein.
DR Bgee; ENSMUSG00000016179; Expressed in ventromedial nucleus of hypothalamus and 147 other tissues.
DR ExpressionAtlas; Q91VB2; baseline and differential.
DR Genevisible; Q91VB2; MM.
DR GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Calmodulin-binding; Cell membrane;
KW Cytoplasm; Golgi apparatus; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..477
FT /note="Calcium/calmodulin-dependent protein kinase type 1G"
FT /id="PRO_0000086085"
FT DOMAIN 23..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 277..317
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 297..318
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 326..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 474
FT /note="C->S: Loss of association to membranes."
FT /evidence="ECO:0000269|PubMed:12637513"
SQ SEQUENCE 477 AA; 53296 MW; 3A61FBDC49A7BB56 CRC64;
MGRKEEEDCS SWKKQTTNIR KTFIFMEVLG SGAFSEVFLV KQRVTGKLFA LKCIKKSPAF
RDSSLENEIA VLKRIKHENI VTLEDIYEST THYYLVMQLV SGGELFDRIL ERGVYTEKDA
SLVIQQVLSA VKYLHENGIV HRDLKPENLL YLTPEENSKI MITDFGLSKM EQNGVMSTAC
GTPGYVAPEV LAQKPYSKAV DCWSIGVITY ILLCGYPPFY EETESKLFEK IKEGYYEFES
PFWDDISESA KDFICHLLEK DPNERYTCEK ALRHPWIDGN TALHRDIYPS VSLQIQKNFA
KSKWRQAFNA AAVVHHMRKL HMNLHSPSVR QEVENRPPVS PAPEVSRPDS HDSSITEAPI
LDPSTPLPAL TRLPCSHSSR PSAPSGGRSL NCLVNGSLRI SSSLVPMQQG PLATGPCGCC
SSCLNIGNKG KSSYCSEPTL FRKANKKQNF KSEVMVPVKA GGSTHCRGGQ TGVCLVM
