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   04-NOV-2008, entry version 68.
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; Synonyms=Ckmt;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Intestine;
RX   MEDLINE=91316135; 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
RT   mRNAs encoding isoenzymes from two rat mitochondrial creatine kinase
RT   genes.";
RL   Biochim. Biophys. Acta 1089:352-361(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 40-56, AND TISSUE SPECIFICITY.
RX   MEDLINE=92042182; PubMed=1939264;
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 MASS
RP   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.
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   -!- TISSUE SPECIFICITY: In many tissues, with highest levels in brain
CC       gut and kidney. In the kidney localized primarily in the outer
CC       medulla in the thick ascending limb and distal convoluted tubule.
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; X59737; CAA42415.1; -; mRNA.
DR   PIR; S17189; S17189.
DR   UniGene; Rn.155589; -.
DR   HSSP; P12532; 1QK1.
DR   SMR; P25809; 47-413.
DR   PhosphoSite; P25809; -.
DR   Ensembl; ENSRNOG00000014573; Rattus norvegicus.
DR   RGD; 61976; Ckmt1.
DR   HOVERGEN; P25809; -.
DR   ArrayExpress; P25809; -.
DR   GermOnline; ENSRNOG00000014573; Rattus norvegicus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:EC.
DR   InterPro; IPR000749; ATP-gua_Ptrans.
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; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transit peptide.
FT   TRANSIT       1     39       Mitochondrion.
FT   CHAIN        40    418       Creatine kinase, ubiquitous
FT                                mitochondrial.
FT                                /FTId=PRO_0000016592.
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 (By similarity).
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
//