ID KCRS_CHICK Reviewed; 419 AA. AC P11009; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 08-NOV-2023, entry version 159. DE RecName: Full=Creatine kinase S-type, mitochondrial; DE EC=2.7.3.2; DE AltName: Full=Basic-type mitochondrial creatine kinase; DE Short=Mib-CK; DE AltName: Full=Sarcomeric mitochondrial creatine kinase; DE Short=S-MtCK; DE Flags: Precursor; GN Name=CKMT2; 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] OF 1-39. RC STRAIN=White leghorn; RX PubMed=8662608; DOI=10.1074/jbc.271.20.11920; RA Muehlebach S.M., Wirz T., Braendle U., Perriard J.-C.; RT "Evolution of the creative kinases. The chicken acidic type mitochondrial RT creatine kinase gene as the first nonmammalian gene."; RL J. Biol. Chem. 271:11920-11929(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-419, AND PROTEIN SEQUENCE OF 40-69. RC TISSUE=Heart, and Skeletal muscle; RX PubMed=2831887; DOI=10.1016/0006-291x(88)90608-0; RA Hossle J.P., Schlegel J., Wegmann G., Wyss M., Boehlen P., RA Eppenberger H.M., Wallimann T., Perriard J.-C.; RT "Distinct tissue specific mitochondrial creatine kinases from chicken brain RT and striated muscle with a conserved CK framework."; RL Biochem. Biophys. Res. Commun. 151:408-416(1988). RN [3] RP PROTEIN SEQUENCE OF 40-48. RX PubMed=8305443; DOI=10.1021/bi00170a014; RA Kaldis P., Furter R., Wallimann T.; RT "The N-terminal heptapeptide of mitochondrial creatine kinase is important RT for octamerization."; RL Biochemistry 33:952-959(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT. RX PubMed=8692275; DOI=10.1038/381341a0; RA Fritz-Wolf K., Schnyder T., Wallimann T., Kabsch W.; RT "Structure of mitochondrial creatine kinase."; RL Nature 381:341-345(1996). 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. 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 -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers. CC {ECO:0000269|PubMed:8692275}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane CC protein; Intermembrane side. CC -!- TISSUE SPECIFICITY: Expressed in the leg muscle and heart. CC -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin. 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; M18866; AAA48688.1; -; mRNA. DR PIR; A27708; A27708. DR RefSeq; NP_001161216.1; NM_001167744.1. DR PDB; 1CRK; X-ray; 3.00 A; A/B/C/D=40-419. DR PDBsum; 1CRK; -. DR AlphaFoldDB; P11009; -. DR SMR; P11009; -. DR STRING; 9031.ENSGALP00000032149; -. DR PaxDb; 9031-ENSGALP00000032149; -. DR GeneID; 396508; -. DR KEGG; gga:396508; -. DR CTD; 1160; -. DR VEuPathDB; HostDB:geneid_396508; -. DR eggNOG; KOG3581; Eukaryota. DR InParanoid; P11009; -. DR OrthoDB; 35839at2759; -. DR PhylomeDB; P11009; -. DR BRENDA; 2.7.3.2; 1306. DR SABIO-RK; P11009; -. DR EvolutionaryTrace; P11009; -. DR PRO; PR:P11009; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central. 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:SF19; CREATINE KINASE S-TYPE, MITOCHONDRIAL; 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; Direct protein sequencing; Kinase; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..39 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:2831887, FT ECO:0000269|PubMed:8305443" FT CHAIN 40..419 FT /note="Creatine kinase S-type, mitochondrial" FT /id="PRO_0000016599" FT DOMAIN 46..132 FT /note="Phosphagen kinase N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842" FT DOMAIN 159..401 FT /note="Phosphagen kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 162..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 225 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 270 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 326 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 354..359 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 369 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT CONFLICT 20..23 FT /note="AAGS -> CSRQ (in Ref. 2; AAA48688)" FT /evidence="ECO:0000305" FT HELIX 50..53 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 63..67 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 70..76 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 87..96 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 115..118 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 120..130 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 160..169 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 182..197 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 205..212 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 215..223 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 234..237 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 238..240 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 243..248 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 250..254 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 259..278 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 280..300 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 326..332 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 334..338 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 342..349 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:1CRK" FT TURN 359..363 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 367..372 FT /evidence="ECO:0007829|PDB:1CRK" FT STRAND 375..378 FT /evidence="ECO:0007829|PDB:1CRK" FT HELIX 380..402 FT /evidence="ECO:0007829|PDB:1CRK" SQ SEQUENCE 419 AA; 47084 MW; 9ACC60D709B9283F CRC64; MAGTFGRLLA GRVTAALFAA AGSGVLTTGY LLNQQNVKAT VHEKRKLFPP SADYPDLRKH NNCMAECLTP AIYAKLRDKL TPNGYSLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA EIFDPVIKAR HNGYDPRTMK HHTDLDASKI THGQFDERYV LSSRVRTGRS IRGLSLPPAC SRAERREVEN VVVTALAGLK GDLSGKYYSL TNMSERDQQQ LIDDHFLFDK PVSPLLTCAG MARDWPDARG IWHNNDKTFL VWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIKE RGWEFMWNER LGYVLTCPSN LGTGLRAGVH VKLPRLSKDP RFPKILENLR LQKRGTGGVD TAAVADVYDI SNLDRMGRSE VELVQIVIDG VNYLVDCEKK LEKGQDIKVP PPLPQFGRK //