ID   KCRM_TORMA              Reviewed;         381 AA.
AC   P00566;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2008, entry version 51.
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;
DE   AltName: Full=NU-2 protein;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea;
OC   Torpediniformes; Torpedinoidei; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Electric organ;
RX   MEDLINE=85063781; PubMed=6095285;
RA   Giraudat J., Devillers-Thiery A., Perriard J.-C., Changeux J.-P.;
RT   "Complete nucleotide sequence of Torpedo marmorata mRNA coding for the
RT   43,000-dalton nu 2 protein: muscle-specific creatine kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:7313-7317(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   -!- MISCELLANEOUS: This electric ray muscle-specific creatine kinase
CC       (MM isozyme) is isolated from the electric organ, which derives
CC       embryologically from skeletal muscle. It may be involved in the
CC       electrical discharge process.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; M11508; AAA49277.1; -; mRNA.
DR   PIR; A00676; KIRYCM.
DR   HSSP; P04414; 1N16.
DR   SMR; P00566; 2-381.
DR   HOVERGEN; P00566; -.
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_0000211982.
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;  42974 MW;  AE0217EB65B8772C CRC64;
     MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG FTLDDVIQTG
     VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY KPTDKHKTDL NQDNLKGGDD
     LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE RRLVEKLCIE GLATLTGEFQ GKYYPLSTMS
     DAEQQQLIDD HFLFDKPISP LLLASGMARD WPDGRGIWHN NDKSFLVWVN EEDHLRVISM
     QKGGNMKEVF RRFCVGLKKI EEIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP
     HLCKHEKFSE VLKRTRLQKR GTGGVDTEAV GSIYDISNAD RLGFSEVEQV QMVVDGVKLM
     VEMEKRLENG KSIDDLIPAQ K
//