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Creatine kinase M-type (EC 2.7.3.2) (Creatine kinase M chain) (M-CK)

 KCRM_TETCF              Reviewed;         381 AA.
P04414;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 91.
RecName: Full=Creatine kinase M-type;
EC=2.7.3.2;
AltName: Full=Creatine kinase M chain;
AltName: Full=M-CK;
Tetronarce californica (Pacific electric ray) (Torpedo californica).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
NCBI_TaxID=7787;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Electric organ;
PubMed=6594677; DOI=10.1073/pnas.81.22.7007;
West B.L., Babbitt P.C., Mendez B., Baxter J.D.;
"Creatine kinase protein sequence encoded by a cDNA made from Torpedo
californica electric organ mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 81:7007-7011(1984).
[2]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, AND
SUBUNIT.
PubMed=12437342; DOI=10.1021/bi026655p;
Lahiri S.D., Wang P.-F., Babbitt P.C., McLeish M.J., Kenyon G.L.,
Allen K.N.;
"The 2.1 A structure of Torpedo californica creatine kinase complexed
with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue
complex.";
Biochemistry 41:13861-13867(2002).
-!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
ATP and various phosphogens (e.g. creatine phosphate). Creatine
kinase isoenzymes play a central role in energy transduction in
tissues with large, fluctuating energy demands, such as skeletal
muscle, heart, brain and spermatozoa.
-!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
{ECO:0000255|PROSITE-ProRule:PRU10029}.
-!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
the major form in skeletal muscle and myocardium, MB existing in
myocardium, and BB existing in many tissues, especially brain.
{ECO:0000269|PubMed:12437342}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: This electric ray muscle-specific creatine kinase
(MM isozyme) is isolated from the electric organ, which derives
embryologically from skeletal muscle. It may be involved in the
electrical discharge process.
-!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
ProRule:PRU00843}.
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EMBL; M36427; AAA49278.1; -; mRNA.
PIR; A00677; KIRYCT.
PDB; 1VRP; X-ray; 2.10 A; A/B=1-381.
PDBsum; 1VRP; -.
ProteinModelPortal; P04414; -.
SMR; P04414; -.
PRIDE; P04414; -.
HOVERGEN; HBG001339; -.
EvolutionaryTrace; P04414; -.
PMAP-CutDB; P04414; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
Gene3D; 1.10.135.10; -; 1.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR000749; ATP-guanido_PTrfase.
InterPro; IPR022415; ATP-guanido_PTrfase_AS.
InterPro; IPR022414; ATP-guanido_PTrfase_cat.
InterPro; IPR022413; ATP-guanido_PTrfase_N.
InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
PANTHER; PTHR11547; PTHR11547; 1.
Pfam; PF00217; ATP-gua_Ptrans; 1.
Pfam; PF02807; ATP-gua_PtransN; 1.
SUPFAM; SSF48034; SSF48034; 1.
SUPFAM; SSF55931; SSF55931; 1.
PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
Transferase.
CHAIN 1 381 Creatine kinase M-type.
/FTId=PRO_0000211981.
DOMAIN 11 98 Phosphagen kinase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00842}.
DOMAIN 125 367 Phosphagen kinase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00843}.
NP_BIND 128 132 ATP.
NP_BIND 320 325 ATP.
BINDING 191 191 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 236 236 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 292 292 ATP.
BINDING 335 335 ATP.
HELIX 16 19 {ECO:0000244|PDB:1VRP}.
HELIX 29 33 {ECO:0000244|PDB:1VRP}.
HELIX 36 42 {ECO:0000244|PDB:1VRP}.
HELIX 53 62 {ECO:0000244|PDB:1VRP}.
STRAND 67 69 {ECO:0000244|PDB:1VRP}.
HELIX 81 84 {ECO:0000244|PDB:1VRP}.
HELIX 86 96 {ECO:0000244|PDB:1VRP}.
HELIX 112 114 {ECO:0000244|PDB:1VRP}.
TURN 123 125 {ECO:0000244|PDB:1VRP}.
STRAND 126 135 {ECO:0000244|PDB:1VRP}.
TURN 143 145 {ECO:0000244|PDB:1VRP}.
HELIX 148 162 {ECO:0000244|PDB:1VRP}.
HELIX 167 169 {ECO:0000244|PDB:1VRP}.
STRAND 171 175 {ECO:0000244|PDB:1VRP}.
HELIX 176 178 {ECO:0000244|PDB:1VRP}.
HELIX 181 189 {ECO:0000244|PDB:1VRP}.
HELIX 200 203 {ECO:0000244|PDB:1VRP}.
TURN 204 214 {ECO:0000244|PDB:1VRP}.
STRAND 216 220 {ECO:0000244|PDB:1VRP}.
STRAND 223 244 {ECO:0000244|PDB:1VRP}.
HELIX 246 266 {ECO:0000244|PDB:1VRP}.
TURN 275 277 {ECO:0000244|PDB:1VRP}.
HELIX 284 286 {ECO:0000244|PDB:1VRP}.
STRAND 292 298 {ECO:0000244|PDB:1VRP}.
HELIX 302 304 {ECO:0000244|PDB:1VRP}.
HELIX 308 315 {ECO:0000244|PDB:1VRP}.
STRAND 317 321 {ECO:0000244|PDB:1VRP}.
STRAND 324 329 {ECO:0000244|PDB:1VRP}.
STRAND 333 338 {ECO:0000244|PDB:1VRP}.
STRAND 342 344 {ECO:0000244|PDB:1VRP}.
HELIX 346 368 {ECO:0000244|PDB:1VRP}.
HELIX 374 376 {ECO:0000244|PDB:1VRP}.
SEQUENCE 381 AA; 42934 MW; DF4A54FDDF3BD570 CRC64;
MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG FTLDDIIQTG
VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY KPTDKHKTDL NQENLKGGDD
LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE RRLVEKLCID GLATLTGEFQ GKYYPLSSMS
DAEQQQLIDD HFLFDKPISP LLLASGMARD WPDGRGIWHN NDKTFLVWVN EEDHLRVISM
QKGGNMKEVF RRFCVGLKKI EDIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP
HLCKHEKFSE VLKRTRLQKR GTGGVDTAAV GSIYDISNAD RLGFSEVEQV QMVVDGVKLM
VEMEKRLENG KSIDDLMPAQ K


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