ID KCRS_BOVIN Reviewed; 419 AA. AC Q3ZBP1; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 08-NOV-2023, entry version 99. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Heart ventricle; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). {ECO:0000250}. 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 CKMT2 homodimers. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Intermembrane side CC {ECO:0000250}. 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; BC103190; AAI03191.1; -; mRNA. DR RefSeq; NP_001029828.1; NM_001034656.2. DR AlphaFoldDB; Q3ZBP1; -. DR SMR; Q3ZBP1; -. DR IntAct; Q3ZBP1; 1. DR STRING; 9913.ENSBTAP00000001330; -. DR PaxDb; 9913-ENSBTAP00000001330; -. DR GeneID; 538944; -. DR KEGG; bta:538944; -. DR CTD; 1160; -. DR eggNOG; KOG3581; Eukaryota. DR InParanoid; Q3ZBP1; -. DR OrthoDB; 35839at2759; -. DR Proteomes; UP000009136; Unplaced. 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 2: Evidence at transcript level; KW ATP-binding; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; KW Transit peptide. FT TRANSIT 1..39 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 40..419 FT /note="Creatine kinase S-type, mitochondrial" FT /id="PRO_0000244733" 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 REGION 40..64 FT /note="Cardiolipin-binding" FT /evidence="ECO:0000250" 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 MOD_RES 255 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P09605" FT MOD_RES 356 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6P8J7" SQ SEQUENCE 419 AA; 47231 MW; 6C8D3F7622474D6F CRC64; MASTFSKLLT GRNASLLFAT LGTGALTTGY LLNKQNVCAA AREQHKLFPP SADYPDLRKH NNCMAECLTP AIYAKLRNKV TPSGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA DLFDPVIKLR HNGYDPRVMK HPTDLDASKI TQGQFDERYV LSSRVRTGRS IRGLSLPPAC SRAELREVEN VAITALEGLK GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK //