KCRB_RAT
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 03-AUG-2022, entry version 173.
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.
CC {ECO:0000250|UniProtKB:P12277}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q04447}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q04447}. 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; 2.
DR MINT; P07335; -.
DR STRING; 10116.ENSRNOP00000015122; -.
DR ChEMBL; CHEMBL2176812; -.
DR MoonProt; P07335; -.
DR CarbonylDB; P07335; -.
DR iPTMnet; P07335; -.
DR PhosphoSitePlus; P07335; -.
DR World-2DPAGE; 0004:P07335; -.
DR jPOST; P07335; -.
DR PaxDb; P07335; -.
DR PRIDE; P07335; -.
DR GeneID; 24264; -.
DR KEGG; rno:24264; -.
DR UCSC; RGD:2357; rat.
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 OMA; ECINDAI; -.
DR OrthoDB; 825025at2759; -.
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 tissues.
DR Genevisible; P07335; RN.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0140651; P:futile creatine cycle; ISO:RGD.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 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; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Mitochondrion;
KW Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW 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
