ID KCRM_CANLF Reviewed; 381 AA. AC P05123; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 153. DE RecName: Full=Creatine kinase M-type; DE EC=2.7.3.2 {ECO:0000250|UniProtKB:P00563}; DE AltName: Full=Creatine kinase M chain; DE AltName: Full=Creatine phosphokinase M-type; DE Short=CPK-M; DE AltName: Full=M-CK; GN Name=CKM; 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=Heart; 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). RN [2] RP PROTEIN SEQUENCE OF 2-23. RC TISSUE=Heart; RX PubMed=9504812; DOI=10.1002/elps.1150181514; RA Dunn M.J., Corbett J.M., Wheeler C.H.; RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog RT heart proteins."; RL Electrophoresis 18:2795-2802(1997). RN [3] RP PROTEIN SEQUENCE OF 377-381. RC TISSUE=Myocardium; RX PubMed=2496146; DOI=10.1172/jci114062; RA Billadello J.J., Fontanet H.L., Strauss A.W., Abendschein D.R.; RT "Characterization of MB creatine kinase isoform conversion in vitro and in RT vivo in dogs."; RL J. Clin. Invest. 83:1637-1643(1989). 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. {ECO:0000250|UniProtKB:P00563}. 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:P00563, ECO:0000255|PROSITE- CC ProRule:PRU10029}; 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. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE- CC ProRule:PRU00843}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11660; AAA30836.1; -; mRNA. DR PIR; A24686; A24686. DR RefSeq; NP_001300705.1; NM_001313776.1. DR AlphaFoldDB; P05123; -. DR SMR; P05123; -. DR STRING; 9615.ENSCAFP00000041666; -. DR SwissPalm; P05123; -. DR PaxDb; 9612-ENSCAFP00000006727; -. DR Ensembl; ENSCAFT00000007262.5; ENSCAFP00000006727.4; ENSCAFG00000004507.5. DR Ensembl; ENSCAFT00030004913.1; ENSCAFP00030004365.1; ENSCAFG00030002587.1. DR Ensembl; ENSCAFT00805004084; ENSCAFP00805003110; ENSCAFG00805002217. DR Ensembl; ENSCAFT00845010014.1; ENSCAFP00845007817.1; ENSCAFG00845005622.1. DR GeneID; 476435; -. DR KEGG; cfa:476435; -. DR CTD; 1158; -. DR VEuPathDB; HostDB:ENSCAFG00845005622; -. DR VGNC; VGNC:39291; CKM. DR eggNOG; KOG3581; Eukaryota. DR GeneTree; ENSGT00950000182772; -. DR InParanoid; P05123; -. DR OrthoDB; 35839at2759; -. DR Reactome; R-CFA-71288; Creatine metabolism. DR Proteomes; UP000002254; Chromosome 1. DR Proteomes; UP000694429; Chromosome 1. DR Proteomes; UP000694542; Unplaced. DR Proteomes; UP000805418; Chromosome 1. DR Bgee; ENSCAFG00000004507; Expressed in smooth muscle tissue and 47 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; ISS:AgBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; ISS:AgBase. DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009408; P:response to heat; ISS:AgBase. 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:SF63; CREATINE KINASE M-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 UCD-2DPAGE; P05123; -. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9504812" FT CHAIN 2..381 FT /note="Creatine kinase M-type" FT /id="PRO_0000211974" 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 BINDING 128..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 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" 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 335 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07310" FT MOD_RES 166 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00564" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00564" FT MOD_RES 180 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00564" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07310" FT MOD_RES 313 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00564" FT MOD_RES 322 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P07310" FT MOD_RES 372 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07310" SQ SEQUENCE 381 AA; 43153 MW; 83F8D227D27472C2 CRC64; MPFGNTHNKF KLNYKPEEEY PDLTKHNNHM AKALTPEIYK KLRDKETPSG FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYQVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSIE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K //