ID   KCRB_RAT                Reviewed;         381 AA.
AC   P07335; A0JPK7; Q499P7; Q5PPJ5; Q6IRE0; Q6P139;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Creatine kinase B-type;
DE            EC=2.7.3.2;
DE   AltName: Full=B-CK;
DE   AltName: Full=Creatine kinase B chain;
DE   AltName: Full=Creatine phosphokinase M-type;
DE            Short=CPK-B;
GN   Name=Ckb; Synonyms=Ckbb;
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].
RX   PubMed=3005113; DOI=10.1016/0378-1119(85)90321-x;
RA   Benfield P.A., Henderson L., Pearson M.L.;
RT   "Expression of a rat brain creatine kinase-beta-galactosidase fusion
RT   protein in Escherichia coli and derivation of the complete amino acid
RT   sequence of rat brain creatine kinase.";
RL   Gene 39:263-267(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2838389; DOI=10.1016/0378-1119(88)90527-6;
RA   Benfield P.A., Graf D., Korolkoff P.N., Hobson G., Pearson M.L.;
RT   "Isolation of four rat creatine kinase genes and identification of multiple
RT   potential promoter sequences within the rat brain creatine kinase promoter
RT   region.";
RL   Gene 63:227-243(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Uterus;
RX   PubMed=2284002; DOI=10.1210/mend-4-7-1000;
RA   Pentecost B.T., Mattheiss L., Dickerman H.W., Kumar S.A.;
RT   "Estrogen regulation of creatine kinase-B in the rat uterus.";
RL   Mol. Endocrinol. 4:1000-1010(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Embryonic brain, Heart, and Prostate;
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).
RN   [5]
RP   PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 138-148; 157-172; 224-236;
RP   253-265 AND 320-341, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION.
RX   PubMed=6477506; DOI=10.1042/bj2220139;
RA   Mahadevan L.C., Whatley S.A., Leung T.K.C., Lim L.;
RT   "The brain isoform of a key ATP-regulating enzyme, creatine kinase, is a
RT   phosphoprotein.";
RL   Biochem. J. 222:139-144(1984).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=1939264; DOI=10.1016/s0021-9258(18)54587-7;
RA   Friedman D.L., Perryman M.B.;
RT   "Compartmentation of multiple forms of creatine kinase in the distal
RT   nephron of the rat kidney.";
RL   J. Biol. Chem. 266:22404-22410(1991).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 AND SER-309, AND
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: Reversibly catalyzes the transfer of phosphate between ATP
CC       and various phosphogens (e.g. creatine phosphate). Creatine kinase
CC       isoenzymes play a central role in energy transduction in tissues with
CC       large, fluctuating energy demands, such as skeletal muscle, heart,
CC       brain and spermatozoa. Acts as a key regulator of adaptive
CC       thermogenesis as part of the futile creatine cycle: localizes to the
CC       mitochondria of thermogenic fat cells and acts by mediating
CC       phosphorylation of creatine to initiate a futile cycle of creatine
CC       phosphorylation and dephosphorylation. During the futile creatine
CC       cycle, creatine and N-phosphocreatine are in a futile cycle, which
CC       dissipates the high energy charge of N-phosphocreatine as heat without
CC       performing any mechanical or chemical work.
CC       {ECO:0000250|UniProtKB:Q04447}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine;
CC         Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC         Evidence={ECO:0000250|UniProtKB:Q04447, ECO:0000255|PROSITE-
CC         ProRule:PRU10029};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158;
CC         Evidence={ECO:0000250|UniProtKB:Q04447};
CC   -!- SUBUNIT: Dimer of identical or non-identical chains, which can be
CC       either B (brain type) or M (muscle type). With MM being the major form
CC       in skeletal muscle and myocardium, MB existing in myocardium, and BB
CC       existing in many tissues, especially brain. Interacts with SLC12A6 (via
CC       C-terminus); the interaction may be required for SLC12A6 potassium-
CC       chloride cotransport activity (By similarity).
CC       {ECO:0000250|UniProtKB:P12277}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q04447}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q04447}. Cell membrane
CC       {ECO:0000250|UniProtKB:P12277}. Note=Localizes to the mitochondria of
CC       thermogenic fat cells via the internal MTS-like signal (iMTS-L) region.
CC       {ECO:0000250|UniProtKB:Q04447}.
CC   -!- TISSUE SPECIFICITY: In the kidney localized primarily in the outer
CC       medulla in the thick ascending limb and distal convoluted tubule.
CC       {ECO:0000269|PubMed:1939264}.
CC   -!- DOMAIN: The internal MTS-like signal (iMTS-L) mediates targeting to
CC       mitochondria thermogenic fat cells. {ECO:0000250|UniProtKB:Q04447}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC       ProRule:PRU00843}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH87656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M14400; AAA40930.1; -; mRNA.
DR   EMBL; M18668; AAA40932.1; -; Genomic_DNA.
DR   EMBL; M57664; AAA40933.1; -; mRNA.
DR   EMBL; M57665; AAA40931.1; -; Genomic_DNA.
DR   EMBL; BC065307; AAH65307.2; -; mRNA.
DR   EMBL; BC070955; AAH70955.2; -; mRNA.
DR   EMBL; BC087656; AAH87656.1; ALT_INIT; mRNA.
DR   EMBL; BC099814; AAH99814.2; -; mRNA.
DR   EMBL; BC127477; AAI27478.2; -; mRNA.
DR   PIR; A23980; KIRTCB.
DR   RefSeq; NP_036661.3; NM_012529.3.
DR   AlphaFoldDB; P07335; -.
DR   SMR; P07335; -.
DR   BioGRID; 246448; 4.
DR   CORUM; P07335; -.
DR   IntAct; P07335; 3.
DR   MINT; P07335; -.
DR   STRING; 10116.ENSRNOP00000015122; -.
DR   ChEMBL; CHEMBL2176812; -.
DR   MoonProt; P07335; -.
DR   CarbonylDB; P07335; -.
DR   GlyGen; P07335; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P07335; -.
DR   PhosphoSitePlus; P07335; -.
DR   SwissPalm; P07335; -.
DR   jPOST; P07335; -.
DR   PaxDb; 10116-ENSRNOP00000015122; -.
DR   GeneID; 24264; -.
DR   KEGG; rno:24264; -.
DR   UCSC; RGD:2357; rat.
DR   AGR; RGD:2357; -.
DR   CTD; 1152; -.
DR   RGD; 2357; Ckb.
DR   VEuPathDB; HostDB:ENSRNOG00000010872; -.
DR   eggNOG; KOG3581; Eukaryota.
DR   HOGENOM; CLU_019868_4_2_1; -.
DR   InParanoid; P07335; -.
DR   OrthoDB; 35839at2759; -.
DR   PhylomeDB; P07335; -.
DR   TreeFam; TF314214; -.
DR   BRENDA; 2.7.3.2; 5301.
DR   Reactome; R-RNO-71288; Creatine metabolism.
DR   Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR   PRO; PR:P07335; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000010872; Expressed in cerebellum and 20 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; IEP:RGD.
DR   GO; GO:1904568; P:cellular response to wortmannin; IEP:RGD.
DR   GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR   GO; GO:0140651; P:futile creatine cycle; ISO:RGD.
DR   GO; GO:0030644; P:intracellular chloride ion homeostasis; IMP:RGD.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00716; creatine_kinase_like; 1.
DR   Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR   PANTHER; PTHR11547:SF23; CREATINE KINASE B-TYPE; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF48034; Guanido kinase N-terminal domain; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
DR   World-2DPAGE; 0004:P07335; -.
DR   Genevisible; P07335; RN.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Direct protein sequencing; Kinase;
KW   Membrane; Mitochondrion; Nitration; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..381
FT                   /note="Creatine kinase B-type"
FT                   /id="PRO_0000211970"
FT   DOMAIN          11..98
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          125..367
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   REGION          96..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..138
FT                   /note="Internal MTS-like signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q04447"
FT   COMPBIAS        96..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72
FT                   /ligand="creatine"
FT                   /ligand_id="ChEBI:CHEBI:57947"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   BINDING         128..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         232
FT                   /ligand="creatine"
FT                   /ligand_id="ChEBI:CHEBI:57947"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         285
FT                   /ligand="creatine"
FT                   /ligand_id="ChEBI:CHEBI:57947"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   BINDING         292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         320..325
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   MOD_RES         35
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         125
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q04447"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   MOD_RES         269
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q04447"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q04447"
FT   CONFLICT        18
FT                   /note="D -> A (in Ref. 3; AAA40931/AAA40933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183..184
FT                   /note="EQ -> DE (in Ref. 1; AAA40930 and 2; AAA40932)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="G -> A (in Ref. 2; AAA40932)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  42725 MW;  A8C8A09F6FF1A4D1 CRC64;
     MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG FTLDDAIQTG
     VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEDRHGGY QPSDEHKTDL NPDNLQGGDD
     LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLS GRYYALKSMT
     EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM
     QKGGNMKEVF TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
     HLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
     IEMEQRLEQG QPIDDLMPAQ K
//