ID   KCRS_RABIT              Reviewed;         419 AA.
AC   O77814;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Creatine kinase, sarcomeric mitochondrial;
DE            EC=2.7.3.2;
DE   AltName: Full=S-MtCK;
DE   AltName: Full=Basic-type mitochondrial creatine kinase;
DE   AltName: Full=Mib-CK;
DE   AltName: Full=RSMTCK;
DE   Flags: Precursor;
GN   Name=CKMT2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   MEDLINE=99428403; PubMed=10497082; DOI=10.1006/prep.1999.1105;
RA   Marcillat O., Perraut C., Granjon T., Vial C., Vacheron M.J.;
RT   "Cloning, Escherichia coli expression, and phase-transition
RT   chromatography-based purification of recombinant rabbit heart
RT   mitochondrial creatine kinase.";
RL   Protein Expr. Purif. 17:163-168(1999).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Exists as an octamer composed of four CKMT2 homodimers
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side (By similarity).
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; AJ011334; CAA09597.1; -; mRNA.
DR   HSSP; P11009; 1CRK.
DR   SMR; O77814; 47-413.
DR   Ensembl; ENSOCUG00000011211; Oryctolagus cuniculus.
DR   HOVERGEN; O77814; -.
DR   BRENDA; 2.7.3.2; 255.
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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     39       Mitochondrion.
FT   CHAIN        40    419       Creatine kinase, sarcomeric
FT                                mitochondrial.
FT                                /FTId=PRO_0000016597.
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).
SQ   SEQUENCE   419 AA;  47407 MW;  C26469B25730CC6F CRC64;
     MASTFSKLLT GRNASLLFAT LGTSALTTGY LVNRQKVCAE ARDQHKLFPP SADYPDLRKH
     NNCMAECLTP SIYAKLRNKV TANGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
     DLFDPVIKLR HNGYDPRVMK HPTDLDASKI TQGQFDERYV LSSRVRTGRS IRGLSLPPAC
     SRAEAREVEN VAITALEGLK GDLAGRYYRL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG
     MARDWPDARG IWHNYDNTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
     RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD
     TRAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK
//