ID KCRU_MOUSE Reviewed; 418 AA. AC P30275; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 16-JUN-2009, entry version 80. DE RecName: Full=Creatine kinase, ubiquitous mitochondrial; DE EC=2.7.3.2; DE AltName: Full=U-MtCK; DE AltName: Full=Acidic-type mitochondrial creatine kinase; DE Short=Mia-CK; DE Flags: Precursor; GN Name=Ckmt1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=95322032; PubMed=7598809; DOI=10.1089/dna.1995.14.539; RA Steeghs K., Peters W., Brueckwilder M., Croes H., van Alewijk D., RA Wieringa B.; RT "Mouse ubiquitous mitochondrial creatine kinase: gene organization and RT consequences from inactivation in mouse embryonic stem cells."; RL DNA Cell Biol. 14:539-553(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 47-75; 105-130; 152-158; 173-182; 191-200; RP 250-270; 302-326 AND 355-375, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-313, AND MASS SPECTROMETRY. RC TISSUE=Brain; RX PubMed=16800626; DOI=10.1021/bi060474w; RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., RA Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., RA Squier T.C., Bigelow D.J.; RT "Endogenously nitrated proteins in mouse brain: links to RT neurodegenerative disease."; RL Biochemistry 45:8009-8022(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND MASS RP SPECTROMETRY. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between CC ATP and various phosphogens (e.g. creatine phosphate). Creatine CC kinase isoenzymes play a central role in energy transduction in CC tissues with large, fluctuating energy demands, such as skeletal CC muscle, heart, brain and spermatozoa. CC -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine. CC -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Intermembrane side. CC -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z13968; CAA78371.1; -; mRNA. DR EMBL; Z13969; CAA78372.1; -; Genomic_DNA. DR EMBL; BC025976; AAH25976.1; -; mRNA. DR IPI; IPI00128296; -. DR PIR; I48308; S24612. DR RefSeq; NP_034027.1; -. DR UniGene; Mm.252145; -. DR HSSP; P12532; 1QK1. DR SMR; P30275; 47-413. DR PhosphoSite; P30275; -. DR PRIDE; P30275; -. DR Ensembl; ENSMUSG00000000308; Mus musculus. DR GeneID; 12716; -. DR KEGG; mmu:12716; -. DR MGI; MGI:99441; Ckmt1. DR HOGENOM; P30275; -. DR HOVERGEN; P30275; -. DR OMA; P30275; SGYFDER. DR BRENDA; 2.7.3.2; 244. DR NextBio; 281988; -. DR ArrayExpress; P30275; -. DR Bgee; P30275; -. DR CleanEx; MM_CKMT1; -. DR GermOnline; ENSMUSG00000000308; Mus musculus. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; IEA:EC. DR InterPro; IPR000749; ATP-guanido_PTrfase. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat. DR Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1. DR Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1. DR PANTHER; PTHR11547; ATP-gua_Ptrans; 1. DR Pfam; PF00217; ATP-gua_Ptrans; 1. DR Pfam; PF02807; ATP-gua_PtransN; 1. DR PROSITE; PS00112; GUANIDO_KINASE; 1. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Kinase; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Nitration; KW Nucleotide-binding; Phosphoprotein; Transferase; Transit peptide. FT TRANSIT 1 39 Mitochondrion (By similarity). FT CHAIN 40 418 Creatine kinase, ubiquitous FT mitochondrial. FT /FTId=PRO_0000016591. FT NP_BIND 162 166 ATP (By similarity). FT NP_BIND 354 359 ATP (By similarity). FT REGION 40 64 Cardiolipin-binding (By similarity). FT BINDING 225 225 ATP (By similarity). FT BINDING 270 270 ATP (By similarity). FT BINDING 326 326 ATP (By similarity). FT BINDING 369 369 ATP (By similarity). FT MOD_RES 154 154 Phosphotyrosine. FT MOD_RES 313 313 Nitrated tyrosine. SQ SEQUENCE 418 AA; 47004 MW; 993CD8C290C8BFB9 CRC64; MAGPFSRLLS ARPGLRLLAL AGAGSLTAGI LLRPESVGAA AAERRRLYPP SAEYPDLRKH NNCMASHLTP AVYARLCDKT TPTGWTLDQC IQTGVDNPGH PFIKTVGMVA GDEETYEVFA ELFDPVIQER HNGYDPRTMK HTTDLDASKI RSGYFDERYV LSSRVRTGRS IRGLSLPPAC TRAERREVER VVVDALSGLK GDLAGRYYRL SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG MARDWPDARG IWHNNEKSFL IWVNEEDHTR VISMEKGGNM KRVFERFCRG LKEVEKLIQE RGWEFMWNER LGYILTCPSN LGTGLRAGVH IKLPLLSKDN RFPKILENLR LQKRGTGGVD TAATGSVFDI SNLDRLGKSE VELVQLVIDG VNYLIDCERR LERGQDIRIP PPLVHSKH //