ID KCRM_CHICK Reviewed; 381 AA. AC P00565; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 03-MAY-2023, entry version 121. DE RecName: Full=Creatine kinase M-type {ECO:0000303|PubMed:6091045, ECO:0000303|PubMed:8525081}; DE EC=2.7.3.2 {ECO:0000269|PubMed:8525081}; 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 {ECO:0000303|PubMed:8525081}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=6091045; DOI=10.1093/nar/12.18.6925; RA Kwiatkowski R.W., Schweinfest C.W., Dottin R.P.; RT "Molecular cloning and the complete nucleotide sequence of the creatine RT kinase-M cDNA from chicken."; RL Nucleic Acids Res. 12:6925-6934(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6096363; DOI=10.1016/s0021-9258(17)42538-5; RA Ordahl C.P., Evans G.L., Cooper T.A., Kunz G., Perriard J.-C.; RT "Complete cDNA-derived amino acid sequence of chick muscle creatine RT kinase."; RL J. Biol. Chem. 259:15224-15227(1984). RN [3] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=8525081; DOI=10.1016/0034-5288(95)90026-8; RA Mitchell M.A., Sandercock D.A.; RT "Creatine kinase isoenzyme profiles in the plasma of the domestic fowl RT (Gallus domesticus): effects of acute heat stress."; RL Res. Vet. Sci. 59:30-34(1995). CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP CC and various phosphogens (e.g. creatine phosphate) (PubMed:8525081). CC Creatine kinase isoenzymes play a central role in energy transduction CC in tissues with large, fluctuating energy demands, such as skeletal CC muscle, heart, brain and spermatozoa (Probable). CC {ECO:0000269|PubMed:8525081, ECO:0000305}. 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:0000255|PROSITE-ProRule:PRU10029, CC ECO:0000269|PubMed:8525081}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158; CC Evidence={ECO:0000269|PubMed:8525081}; 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 -!- TISSUE SPECIFICITY: Predominantly found in skeletal muscle, but not in CC the heart. {ECO:0000269|PubMed:6091045}. 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; M10012; AAA48689.1; -; mRNA. DR EMBL; X00954; CAA25465.1; -; mRNA. DR EMBL; X00954; CAA25466.2; -; mRNA. DR PIR; A00675; KICHCM. DR RefSeq; NP_990838.1; NM_205507.1. DR AlphaFoldDB; P00565; -. DR SMR; P00565; -. DR iPTMnet; P00565; -. DR GeneID; 107051134; -. DR VEuPathDB; HostDB:geneid_396248; -. DR InParanoid; P00565; -. DR OrthoDB; 35839at2759; -. DR PhylomeDB; P00565; -. DR PRO; PR:P00565; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; TAS:AgBase. DR GO; GO:0005615; C:extracellular space; IDA:AgBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; IDA: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; IDA: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. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..381 FT /note="Creatine kinase M-type" FT /id="PRO_0000211980" 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 99..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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" SQ SEQUENCE 381 AA; 43328 MW; 192C236BB46E2531 CRC64; MPFSSTHNKH KLKFSAEEEF PDLSKHNNHM AKVLTPELYK RLRDKETPSG FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKDLFD PVIQDRHGGY KPTDKHRTDL NHENLKGGDD LDPKYVLSSR VRTGRSIKGY SLPPHCSRGE RRAVEKLSVE ALNSLEGEFK GRYYPLKAMT EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLKKI EEIFKKAGHP FMWTEHLGYI LTCPSNLGTG LRGGVHVKLP KLSQHPKFEE ILHRLRLQKR GTGGVDTAAV GAVFDISNAD RLGFSEVEQV QMVVDGVKLM VEMEKKLEQN QPIDDMIPAQ K //