ID KCRB_CANLF Reviewed; 381 AA.
AC P05124;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 27-MAR-2024, entry version 154.
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;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3755597; DOI=10.1016/0006-291x(86)90294-9;
RA Billadello J.J., Kelly D.P., Roman D.G., Strauss A.W.;
RT "The complete nucleotide sequence of canine brain B creatine kinase mRNA:
RT homology in the coding and 3' noncoding regions among species.";
RL Biochem. Biophys. Res. Commun. 138:392-398(1986).
RN [2]
RP PROTEIN SEQUENCE OF 2-30; 44-61; 87-95; 138-149; 158-171; 178-208; 224-236;
RP 247-261; 268-287; 321-357 AND 364-381.
RC TISSUE=Brain;
RX PubMed=3866230; DOI=10.1073/pnas.82.24.8394;
RA Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B., Strauss A.W.;
RT "Complete nucleotide sequence of dog heart creatine kinase mRNA:
RT conservation of amino acid sequence within and among species.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985).
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 -!- 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}.
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DR EMBL; M13453; AAA30837.1; -; mRNA.
DR PIR; A24227; B24686.
DR RefSeq; XP_003639259.1; XM_003639211.3.
DR AlphaFoldDB; P05124; -.
DR SMR; P05124; -.
DR STRING; 9615.ENSCAFP00000061954; -.
DR PaxDb; 9612-ENSCAFP00000026998; -.
DR Ensembl; ENSCAFT00000029035.5; ENSCAFP00000026998.3; ENSCAFG00000018277.5.
DR Ensembl; ENSCAFT00030002059.1; ENSCAFP00030001822.1; ENSCAFG00030001161.1.
DR Ensembl; ENSCAFT00805023772; ENSCAFP00805018695; ENSCAFG00805013042.
DR Ensembl; ENSCAFT00845033496.1; ENSCAFP00845026222.1; ENSCAFG00845018958.1.
DR GeneID; 100855552; -.
DR KEGG; cfa:100855552; -.
DR VEuPathDB; HostDB:ENSCAFG00845018958; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_4_2_1; -.
DR InParanoid; P05124; -.
DR OMA; NRGHEFM; -.
DR OrthoDB; 35839at2759; -.
DR TreeFam; TF314214; -.
DR Reactome; R-CFA-71288; Creatine metabolism.
DR Reactome; R-CFA-9696264; RND3 GTPase cycle.
DR Proteomes; UP000002254; Chromosome 8.
DR Proteomes; UP000694429; Chromosome 8.
DR Proteomes; UP000694542; Unplaced.
DR Proteomes; UP000805418; Chromosome 8.
DR Bgee; ENSCAFG00000018277; Expressed in olfactory bulb and 47 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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:0007420; P:brain development; ISS:AgBase.
DR GO; GO:0030644; P:intracellular chloride ion homeostasis; ISS:AgBase.
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.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12277"
FT CHAIN 2..381
FT /note="Creatine kinase B-type"
FT /id="PRO_0000211965"
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..123
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:0000250|UniProtKB:P12277"
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 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04447"
SQ SEQUENCE 381 AA; 42701 MW; 2C2F925C78F16364 CRC64;
MPFSNSHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG
VDNPGHPYIM TVGCVAGDEE SYDVFKELFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT
EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM
QKGGNMKEVF TRFCNGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
HLGKHEKFPE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
IEMEQRLEQG QAIDDLVPAQ K
//
