ID KCRM_RABIT Reviewed; 381 AA. AC P00563; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 08-NOV-2023, entry version 145. DE RecName: Full=Creatine kinase M-type; DE EC=2.7.3.2 {ECO:0000269|PubMed:5499971}; 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 Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3857581; DOI=10.1073/pnas.82.8.2310; RA Pickering L., Pang H., Biemann K., Munro H., Schimmel P.; RT "Two tissue-specific isozymes of creatine kinase have closely matched amino RT acid sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6094551; DOI=10.1016/s0021-9258(17)42593-2; RA Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L., RA Belagaje R., Biemann K., Page D., Kuby S., Schimmel P.; RT "Rabbit muscle creatine phosphokinase. cDNA cloning, primary structure and RT detection of human homologues."; RL J. Biol. Chem. 259:14317-14320(1984). RN [3] RP CATALYTIC ACTIVITY, AND INHIBITION BY CHEMICAL MODIFICATION. RX PubMed=5499971; DOI=10.1042/bj1200589; RA Atherton R.S., Laws J.F., Miles B.J., Thomson A.R.; RT "Brain adenosine 5'-triphosphate-creatine phosphotransferase."; RL Biochem. J. 120:589-600(1970). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS). RC TISSUE=Muscle; RX PubMed=9849893; DOI=10.1016/s0014-5793(98)01355-6; RA Rao J.K., Bujacz G., Wlodawer A.; RT "Crystal structure of rabbit muscle creatine kinase."; RL FEBS Lett. 439:133-137(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP. RX PubMed=17327675; DOI=10.1107/s0907444906056204; RA Ohren J.F., Kundracik M.L., Borders C.L. Jr., Edmiston P., Viola R.E.; RT "Structural asymmetry and intersubunit communication in muscle creatine RT kinase."; RL Acta Crystallogr. D 63:381-389(2007). CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP CC and various phosphogens (e.g. creatine phosphate) (PubMed:5499971). 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:5499971, 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:5499971}; 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 -!- INTERACTION: CC P00563; P11974: PKM; NbExp=2; IntAct=EBI-2750756, EBI-7133357; CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE- CC ProRule:PRU00843}. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/CRK/"; 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; K02831; AAA31205.1; -; mRNA. DR PIR; A00673; KIRBCM. DR RefSeq; NP_001075708.1; NM_001082239.1. DR PDB; 1U6R; X-ray; 1.65 A; A/B=2-381. DR PDB; 2CRK; X-ray; 2.35 A; A=1-381. DR PDBsum; 1U6R; -. DR PDBsum; 2CRK; -. DR AlphaFoldDB; P00563; -. DR SMR; P00563; -. DR IntAct; P00563; 1. DR MINT; P00563; -. DR STRING; 9986.ENSOCUP00000020805; -. DR BindingDB; P00563; -. DR ChEMBL; CHEMBL1075201; -. DR PaxDb; 9986-ENSOCUP00000020805; -. DR GeneID; 100009056; -. DR CTD; 1158; -. DR eggNOG; KOG3581; Eukaryota. DR InParanoid; P00563; -. DR OrthoDB; 35839at2759; -. DR BRENDA; 2.7.3.2; 1749. DR SABIO-RK; P00563; -. DR EvolutionaryTrace; P00563; -. DR PRO; PR:P00563; -. DR Proteomes; UP000001811; Unplaced. 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; IEA:InterPro. 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. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1..381 FT /note="Creatine kinase M-type" FT /id="PRO_0000211978" 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:0000305|PubMed:17327675" FT BINDING 191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:17327675" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:17327675" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:17327675" FT BINDING 320..325 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:17327675" 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" FT HELIX 6..11 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 29..33 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 36..42 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 53..62 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:2CRK" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 86..96 FT /evidence="ECO:0007829|PDB:1U6R" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:1U6R" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 126..135 FT /evidence="ECO:0007829|PDB:1U6R" FT TURN 143..145 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 148..163 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:1U6R" FT TURN 204..214 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 225..244 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 246..267 FT /evidence="ECO:0007829|PDB:1U6R" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 308..315 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 317..320 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 333..338 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:1U6R" FT HELIX 346..369 FT /evidence="ECO:0007829|PDB:1U6R" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:1U6R" SQ SEQUENCE 381 AA; 43112 MW; 821447F395FE71CC CRC64; MPFGNTHNKY KLNYKSEEEY PDLSKHNNHM AKVLTPDLYK KLRDKETPSG FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF KPTDKHKTDL NHENLKGGDD LDPHYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K //