KCC1B_RAT
ID KCC1B_RAT Reviewed; 343 AA.
AC O70150; O08767;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1B;
DE EC=2.7.11.17;
DE AltName: Full=CaM kinase I beta;
DE Short=CaM kinase IB;
DE Short=CaM-KI beta;
DE Short=CaMKI-beta;
DE AltName: Full=Pregnancy up-regulated non-ubiquitously-expressed CaM kinase homolog;
GN Name=Pnck;
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] (ISOFORM 2).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9405489; DOI=10.1074/jbc.272.51.32704;
RA Naito Y., Watanabe Y., Yokokura H., Sugita R., Nishio M., Hidaka H.;
RT "Isoform-specific activation and structure diversity of calmodulin kinase
RT I.";
RL J. Biol. Chem. 272:32704-32708(1997).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a
CC proposed calcium-triggered signaling cascade. In vitro, isoform 1 and
CC isoform 2 phosphorylate CREB1, SYN1/synapsin I. Phosphorylates and
CC activates CAMK1. {ECO:0000269|PubMed:9405489}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Must be
CC phosphorylated to be maximally active. Activated by CAMKK1.
CC {ECO:0000269|PubMed:9405489}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CamKIbeta2;
CC IsoId=O70150-1; Sequence=Displayed;
CC Name=2; Synonyms=CamKIbeta1;
CC IsoId=O70150-2; Sequence=VSP_012636;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in liver, heart, lung,
CC kidney, spleen and testis. Isoform 2 is predominantly expressed in
CC cerebrum and cerebellum. {ECO:0000269|PubMed:9405489}.
CC -!- PTM: Isoform 1 and isoform 2 are phosphorylated by CAMKK1.
CC {ECO:0000305}.
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; D86556; BAA19879.1; -; mRNA.
DR EMBL; AB004267; BAA28263.1; -; mRNA.
DR RefSeq; NP_058971.1; NM_017275.1. [O70150-1]
DR RefSeq; XP_006229635.1; XM_006229573.3. [O70150-1]
DR RefSeq; XP_006229636.1; XM_006229574.3. [O70150-1]
DR RefSeq; XP_006229637.1; XM_006229575.3. [O70150-1]
DR RefSeq; XP_008771850.1; XM_008773628.2. [O70150-1]
DR RefSeq; XP_017457441.1; XM_017601952.1. [O70150-2]
DR AlphaFoldDB; O70150; -.
DR SMR; O70150; -.
DR BioGRID; 248282; 2.
DR STRING; 10116.ENSRNOP00000024227; -.
DR iPTMnet; O70150; -.
DR PhosphoSitePlus; O70150; -.
DR PaxDb; O70150; -.
DR PRIDE; O70150; -.
DR Ensembl; ENSRNOT00000090795; ENSRNOP00000074179; ENSRNOG00000058317. [O70150-1]
DR Ensembl; ENSRNOT00000095467; ENSRNOP00000094811; ENSRNOG00000058317. [O70150-2]
DR GeneID; 29660; -.
DR KEGG; rno:29660; -.
DR UCSC; RGD:69249; rat. [O70150-1]
DR CTD; 139728; -.
DR RGD; 69249; Pnck.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000162187; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; O70150; -.
DR OMA; EFVWARQ; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; O70150; -.
DR TreeFam; TF314166; -.
DR PRO; PR:O70150; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000058317; Expressed in frontal cortex and 5 other tissues.
DR Genevisible; O70150; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd14169; STKc_CaMKI_beta; 1.
DR InterPro; IPR042696; CaMKI_beta_STKc.
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 Alternative splicing; ATP-binding; Calcium; Calmodulin-binding; Cytoplasm;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..343
FT /note="Calcium/calmodulin-dependent protein kinase type 1B"
FT /id="PRO_0000086081"
FT DOMAIN 15..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 290..311
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 314..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYK9"
FT VAR_SEQ 319..343
FT /note="GEEASRQGMTRHSHPGLGTSQSPKW -> ALLISFPDPCPPDWPLLESPRPW
FT V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9074610"
FT /id="VSP_012636"
SQ SEQUENCE 343 AA; 38439 MW; 994D451D809A9D80 CRC64;
MLLLKKQTED ISSVYEIREK LGSGAFSEVM LAQERGSAHL VALKCIPKKA LRGKEALVEN
EIAVLRRISH PNIVALEDVH ESPSHLYLAM ELVTGGELFD RIMERGSYTE KDASHLVGQV
LGAVSYLHSL GIVHRDLKPE NLLYATPFED SKIMVSDFGL SKIQAGNMLG TACGTPGYVA
PELLEQKPYG KAVDVWALGV ISYILLCGYP PFYDESDPEL FSQILRASYE FDSPFWDDIS
ESAKDFIRHL LERDPQKRFT CQQALQHLWI SGDAALDRDI LGSVSEQIQK NFARTHWKRA
FNATSFLRHI RKLGQSPEGE EASRQGMTRH SHPGLGTSQS PKW
