ID KCRU_RAT Reviewed; 418 AA. AC P25809; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 24-JAN-2024, entry version 148. DE RecName: Full=Creatine kinase U-type, mitochondrial; DE EC=2.7.3.2; DE AltName: Full=Acidic-type mitochondrial creatine kinase; DE Short=Mia-CK; DE AltName: Full=Ubiquitous mitochondrial creatine kinase; DE Short=U-MtCK; DE Flags: Precursor; GN Name=Ckmt1; Synonyms=Ckmt; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Intestine; RX PubMed=1859839; DOI=10.1016/0167-4781(91)90176-m; RA Payne R.M., Haas R.C., Strauss A.W.; RT "Structural characterization and tissue-specific expression of the mRNAs RT encoding isoenzymes from two rat mitochondrial creatine kinase genes."; RL Biochim. Biophys. Acta 1089:352-361(1991). RN [2] RP PROTEIN SEQUENCE OF 40-56, AND TISSUE SPECIFICITY. RX PubMed=1939264; DOI=10.1016/s0021-9258(18)54587-7; RA Friedman D.L., Perryman M.B.; RT "Compartmentation of multiple forms of creatine kinase in the distal RT nephron of the rat kidney."; RL J. Biol. Chem. 266:22404-22410(1991). RN [3] RP PROTEIN SEQUENCE OF 152-158; 191-200; 258-270 AND 311-326, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Chen W.-Q.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-197, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane CC protein; Intermembrane side. CC -!- TISSUE SPECIFICITY: In many tissues, with highest levels in brain gut CC and kidney. In the kidney localized primarily in the outer medulla in CC the thick ascending limb and distal convoluted tubule. CC {ECO:0000269|PubMed:1939264}. 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; X59737; CAA42415.1; -; mRNA. DR PIR; S17189; S17189. DR AlphaFoldDB; P25809; -. DR SMR; P25809; -. DR IntAct; P25809; 3. DR MINT; P25809; -. DR STRING; 10116.ENSRNOP00000044253; -. DR iPTMnet; P25809; -. DR PhosphoSitePlus; P25809; -. DR SwissPalm; P25809; -. DR jPOST; P25809; -. DR PaxDb; 10116-ENSRNOP00000044253; -. DR UCSC; RGD:61976; rat. DR AGR; RGD:61976; -. DR RGD; 61976; Ckmt1. DR eggNOG; KOG3581; Eukaryota. DR InParanoid; P25809; -. DR PhylomeDB; P25809; -. DR Reactome; R-RNO-71288; Creatine metabolism. DR PRO; PR:P25809; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044289; C:mitochondrial inner-outer membrane contact site; IDA:RGD. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0043204; C:perikaryon; IDA:RGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0021549; P:cerebellum development; IEP:RGD. DR GO; GO:0048565; P:digestive tract development; IEP:RGD. DR GO; GO:0001822; P:kidney development; IEP:RGD. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD. DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD. 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:SF24; CREATINE KINASE U-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. DR World-2DPAGE; 0004:P25809; -. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Kinase; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..39 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:1939264" FT CHAIN 40..418 FT /note="Creatine kinase U-type, mitochondrial" FT /id="PRO_0000016592" 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 152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 197 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 214 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00564" FT MOD_RES 233 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30275" FT MOD_RES 356 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P07310" SQ SEQUENCE 418 AA; 47029 MW; 468339C52E4232D5 CRC64; MAGPFSRLLS ARPGLKLLAL AGAGSLAAGI LLRPESVRAA TGERRRLYPP SAEYPDLRKH NNCMASHLTP AVYARLCDKT TPTGWTLDQC IQTGVDNPGH PFIKTVGMVA GDEETYEVFA ELFDPVIQER HNGYDPRTMK HTTDLDASKI RSGYFDERYV LSSRVRTGRS IRGLSLPPAC TRAERREVER VVVDALSGLK GDLAGRYYRL SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG MARDWPDARG IWHNNEKSFL IWVNEEDHTR VISMEKGGNM KRVFERFCRG LKKVEKLIQE RGWEFMWNER LGYILTCPSN LGTGLRAGVH VKLPLLSKDS RFPKILENLR LQKRGTGGVD TPATADVFDI SNLDRLGKSE VELVQLVIDG VNYLIDCERR LEKGQDIRIP PPLVHGKH //