ID   KCRM_PIG                Reviewed;         381 AA.
AC   Q5XLD3; Q45EW9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   26-MAY-2009, entry version 27.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Xu D.Q., Xiong Y.Z., Ling X.F., Lang J.;
RT   "Molecular cloning and characterization of porcine CKM.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ling X.F., Xiong Y.Z., Xu D.Q.;
RT   "Cloning and sequence analysis of genomic structure and the proximal
RT   promoter region of porcine CKM gene.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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: 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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; AY754869; AAV28621.1; -; mRNA.
DR   EMBL; DQ153192; AAZ66747.1; -; Genomic_DNA.
DR   RefSeq; NP_001123421.1; -.
DR   UniGene; Ssc.415; -.
DR   SMR; Q5XLD3; 2-381.
DR   GeneID; 397264; -.
DR   KEGG; ssc:397264; -.
DR   HOVERGEN; Q5XLD3; -.
DR   BRENDA; 2.7.3.2; 249.
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; Nucleotide-binding; Transferase.
FT   CHAIN         1    381       Creatine kinase M-type.
FT                                /FTId=PRO_0000211977.
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;  43059 MW;  DF768FBFAF4E636D CRC64;
     MPFGNTHNKY KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG FTLDDVIQTG
     VDNPGHPFIM TVGCVAGDEE SYVVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD
     LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT
     EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM
     EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
     HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM
     VEMEKKLEKG QSIDDMIPAQ K
//