ID   KCRM_RAT                Reviewed;         381 AA.
AC   P00564; Q6P6R9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2008, entry version 68.
DE   RecName: Full=Creatine kinase M-type;
DE            EC=2.7.3.2;
DE   AltName: Full=Creatine kinase M chain;
DE   AltName: Full=M-CK;
GN   Name=Ckm; Synonyms=Ckmm;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Fischer 344;
RX   MEDLINE=85054996; PubMed=6209281;
RA   Benfield P.A., Zivin R.A., Miller L.S., Sowder R., Smythers G.W.,
RA   Henderson L., Oroszlan S., Pearson M.L.;
RT   "Isolation and sequence analysis of cDNA clones coding for rat
RT   skeletal muscle creatine kinase.";
RL   J. Biol. Chem. 259:14979-14984(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 87-381.
RA   Benfield P.A., Zivin R.A., Shearman C.W., Graf D., Henderson L.,
RA   Oroszlan S., Pearson M.L.;
RT   "The nucleotide sequence of rat muscle creatine kinase cDNA and ckm
RT   transcription during myogenesis in an RNA polymerase II mutant of L6
RT   myoblasts.";
RL   Exp. Biol. Med. 9:187-194(1984).
RN   [4]
RP   PROTEIN SEQUENCE OF 87-96; 139-148; 157-170 AND 321-341, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (DEC-2006) 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: Dimer of identical or non-identical chains. With MM being
CC       the major form in skeletal muscle and myocardium, MB existing in
CC       myocardium, and BB existing in many tissues, especially brain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; M10140; AAA40935.1; -; mRNA.
DR   EMBL; BC062058; AAH62058.1; -; mRNA.
DR   EMBL; M14864; AAA40936.1; -; mRNA.
DR   PIR; A00674; KIRTCM.
DR   RefSeq; NP_036662.1; -.
DR   UniGene; Rn.10756; -.
DR   HSSP; P00563; 2CRK.
DR   SMR; P00564; 2-381.
DR   Rat-heart-2DPAGE; P00564; -.
DR   Ensembl; ENSRNOG00000016837; Rattus norvegicus.
DR   GeneID; 24265; -.
DR   KEGG; rno:24265; -.
DR   RGD; 2358; Ckm.
DR   HOVERGEN; P00564; -.
DR   NextBio; 602819; -.
DR   ArrayExpress; P00564; -.
DR   GermOnline; ENSRNOG00000016837; Rattus norvegicus.
DR   GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    381       Creatine kinase M-type.
FT                                /FTId=PRO_0000211979.
FT   NP_BIND     128    132       ATP (By similarity).
FT   NP_BIND     320    325       ATP (By similarity).
FT   BINDING     191    191       ATP (By similarity).
FT   BINDING     236    236       ATP (By similarity).
FT   BINDING     292    292       ATP (By similarity).
FT   BINDING     335    335       ATP (By similarity).
FT   CONFLICT     16     16       P -> S (in Ref. 1; AAA40935 and 3;
FT                                AAA40936).
FT   CONFLICT     87     87       D -> N (in Ref. 2; AAA40936).
FT   CONFLICT    100    100       Y -> F (in Ref. 1; AAA40935 and 3;
FT                                AAA40936).
SQ   SEQUENCE   381 AA;  43045 MW;  B573FEB1D2A41056 CRC64;
     MPFGNTHNKF KLNYKPQEEY PDLSKHNNHM AKVLTPDLYN KLRDKETPSG FTLDDVIQTG
     VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD
     LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT
     EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM
     EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
     NLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GAVFDISNAD RLGSSEVEQV QLVVDGVKLM
     VEMEKKLEKG QSIDDMIPAQ K
//