KCC1G_RAT
ID KCC1G_RAT Reviewed; 476 AA.
AC Q7TNJ7; O08763; Q7TNJ6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
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; Synonyms=Camkig;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12753081; DOI=10.1046/j.1471-4159.2003.01760.x;
RA Nishimura H., Sakagami H., Uezu A., Fukunaga K., Watanabe M., Kondo H.;
RT "Cloning, characterization and expression of two alternatively splicing
RT isoforms of Ca2+/calmodulin-dependent protein kinase I gamma in the rat
RT brain.";
RL J. Neurochem. 85:1216-1227(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-309.
RC TISSUE=Brain;
RX PubMed=9074610; DOI=10.1016/s0167-4838(97)00004-6;
RA Yokokura H., Terada O., Naito Y., Hidaka H.;
RT "Isolation and comparison of rat cDNAs encoding Ca2+/calmodulin-dependent
RT protein kinase I isoforms.";
RL Biochim. Biophys. Acta 1338:8-12(1997).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a
CC proposed calcium-triggered signaling cascade. In vitro phosphorylates
CC transcription factor CREB1 (By similarity). {ECO:0000250}.
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:12753081};
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:12753081};
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TNJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TNJ7-4; Sequence=VSP_012139;
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: Prenylated on Cys-473. {ECO:0000250}.
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; AB101231; BAC80242.1; -; mRNA.
DR EMBL; AB101232; BAC80243.1; -; mRNA.
DR EMBL; D86557; BAA19880.1; -; mRNA.
DR RefSeq; NP_878262.1; NM_182842.1. [Q7TNJ7-1]
DR RefSeq; XP_006250532.1; XM_006250470.3. [Q7TNJ7-4]
DR AlphaFoldDB; Q7TNJ7; -.
DR SMR; Q7TNJ7; -.
DR STRING; 10116.ENSRNOP00000009158; -.
DR jPOST; Q7TNJ7; -.
DR PaxDb; Q7TNJ7; -.
DR Ensembl; ENSRNOT00000009158; ENSRNOP00000009158; ENSRNOG00000006470. [Q7TNJ7-1]
DR Ensembl; ENSRNOT00000044161; ENSRNOP00000041124; ENSRNOG00000006470. [Q7TNJ7-4]
DR GeneID; 171358; -.
DR KEGG; rno:171358; -.
DR CTD; 57172; -.
DR RGD; 621800; Camk1g.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000156872; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q7TNJ7; -.
DR OMA; TGVCAIM; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q7TNJ7; -.
DR TreeFam; TF314166; -.
DR BRENDA; 2.7.11.17; 5301.
DR PRO; PR:Q7TNJ7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000006470; Expressed in cerebellum and 4 other tissues.
DR Genevisible; Q7TNJ7; RN.
DR GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0012505; C:endomembrane system; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0019722; P:calcium-mediated signaling; NAS:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
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 2: Evidence at transcript level;
KW Allosteric enzyme; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cytoplasm; Golgi apparatus; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..476
FT /note="Calcium/calmodulin-dependent protein kinase type 1G"
FT /id="PRO_0000086086"
FT DOMAIN 23..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 277..317
FT /note="Autoinhibitory domain"
FT REGION 297..318
FT /note="Calmodulin-binding"
FT REGION 326..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
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 VAR_SEQ 306..476
FT /note="QAFNAAAVVHHMRKLHMNLHSPSVRQEVENRPPVSPAPEVSRPGSHDSSITE
FT APILDPSTPLPALTRLPCSHSSRPSAPGGRSLNCLVNGSLRISSSLVPMQQGPLATGPC
FT GCCSSCLNIGNKGKSSYCSEPTLFRKANKKQNFKSEVMVPVKAGGSTHCRAGQTGVCLI
FT M -> ELQVRGHGTSESRWQHPLPGWADWGVSHNVIPGARVVFQETRLALLCLSKLASA
FT LRKGSSKAGIAEAAGLRQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12753081"
FT /id="VSP_012139"
SQ SEQUENCE 476 AA; 53179 MW; 70AD679B0C36B0E3 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 PAPEVSRPGS HDSSITEAPI
LDPSTPLPAL TRLPCSHSSR PSAPGGRSLN CLVNGSLRIS SSLVPMQQGP LATGPCGCCS
SCLNIGNKGK SSYCSEPTLF RKANKKQNFK SEVMVPVKAG GSTHCRAGQT GVCLIM
