ID   KCRU_CHICK              Reviewed;         417 AA.
AC   P70079; Q90782;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2008, entry version 53.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=White leghorn; TISSUE=Brain, and Liver;
RX   MEDLINE=96216114; 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
RT   mitochondrial creatine kinase gene as the first nonmammalian gene.";
RL   J. Biol. Chem. 271:11920-11929(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 40-68.
RC   TISSUE=Brain;
RX   MEDLINE=88162838; PubMed=2831887;
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
RT   brain and striated muscle with a conserved CK framework.";
RL   Biochem. Biophys. Res. Commun. 151:408-416(1988).
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 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and gut, weakly in
CC       testis. Also found in cell bodies of neural cells of the gray
CC       matter.
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; X96403; CAA65267.1; -; Genomic_DNA.
DR   EMBL; X96402; CAA65266.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X95526; CAA64778.1; -; Genomic_DNA.
DR   RefSeq; NP_989513.1; -.
DR   UniGene; Gga.13490; -.
DR   HSSP; P12532; 1QK1.
DR   SMR; P70079; 47-412.
DR   Ensembl; ENSGALG00000008352; Gallus gallus.
DR   GeneID; 374002; -.
DR   KEGG; gga:374002; -.
DR   HOGENOM; P70079; -.
DR   HOVERGEN; P70079; -.
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   Transferase; Transit peptide.
FT   TRANSIT       1     39       Mitochondrion.
FT   CHAIN        40    417       Creatine kinase, ubiquitous
FT                                mitochondrial.
FT                                /FTId=PRO_0000016593.
FT   NP_BIND     161    165       ATP (By similarity).
FT   NP_BIND     353    358       ATP (By similarity).
FT   BINDING     224    224       ATP (By similarity).
FT   BINDING     269    269       ATP (By similarity).
FT   BINDING     325    325       ATP (By similarity).
FT   BINDING     368    368       ATP (By similarity).
SQ   SEQUENCE   417 AA;  47104 MW;  ED9B982764153D2C CRC64;
     MASTFARALS ARRSAGLLAM VGAGSLAAGF LLARDTVSAG ERQRRRYPPS AEYPDLRKHN
     NCMASNLTPA IYARLCDKAT PNGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAE
     LFDPVIQERH NGYNPRTMKH VTDLDASKIK FGHFDERYVL SSRVRTGRSI RGLSLPPACT
     RAERREVEKV TVEALNGLTG DLSGRYYRLS EMTEKEQQQL IDDHFLFDKP VSPSLTAAGM
     ARDWPDARGI WHNNEKTFLI WINEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER
     GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT
     AATANVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL EKGQDIRIPS PVPQFRH
//