ID   KCRM_CHICK              Reviewed;         381 AA.
AC   P00565;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2008, entry version 59.
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;
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 [MRNA].
RX   MEDLINE=85014143; PubMed=6091045; DOI=10.1093/nar/12.18.6925;
RA   Kwiatkowski R.W., Schweinfest C.W., Dottin R.P.;
RT   "Molecular cloning and the complete nucleotide sequence of the
RT   creatine kinase-M cDNA from chicken.";
RL   Nucleic Acids Res. 12:6925-6934(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=85080008; PubMed=6096363;
RA   Ordahl C.P., Evans G.L., Cooper T.A., Kunz G., Perriard J.-C.;
RT   "Complete cDNA-derived amino acid sequence of chick muscle creatine
RT   kinase.";
RL   J. Biol. Chem. 259:15224-15227(1984).
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   -!- TISSUE SPECIFICITY: Predominantly found in skeletal muscle, but
CC       not in the heart.
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; M10012; AAA48689.1; -; mRNA.
DR   EMBL; X00954; CAA25465.1; -; mRNA.
DR   EMBL; X00954; CAA25466.2; -; mRNA.
DR   PIR; A00675; KICHCM.
DR   RefSeq; NP_990838.1; -.
DR   UniGene; Gga.4308; -.
DR   HSSP; P00563; 2CRK.
DR   SMR; P00565; 2-381.
DR   GeneID; 396507; -.
DR   KEGG; gga:396507; -.
DR   HOVERGEN; P00565; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN         1    381       Creatine kinase M-type.
FT                                /FTId=PRO_0000211980.
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).
SQ   SEQUENCE   381 AA;  43328 MW;  192C236BB46E2531 CRC64;
     MPFSSTHNKH KLKFSAEEEF PDLSKHNNHM AKVLTPELYK RLRDKETPSG FTLDDVIQTG
     VDNPGHPFIM TVGCVAGDEE SYEVFKDLFD PVIQDRHGGY KPTDKHRTDL NHENLKGGDD
     LDPKYVLSSR VRTGRSIKGY SLPPHCSRGE RRAVEKLSVE ALNSLEGEFK GRYYPLKAMT
     EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM
     EKGGNMKEVF RRFCVGLKKI EEIFKKAGHP FMWTEHLGYI LTCPSNLGTG LRGGVHVKLP
     KLSQHPKFEE ILHRLRLQKR GTGGVDTAAV GAVFDISNAD RLGFSEVEQV QMVVDGVKLM
     VEMEKKLEQN QPIDDMIPAQ K
//