KCRM_TETCF
ID KCRM_TETCF Reviewed; 381 AA.
AC P04414;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 102.
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;
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electric organ;
RX PubMed=6594677; DOI=10.1073/pnas.81.22.7007;
RA West B.L., Babbitt P.C., Mendez B., Baxter J.D.;
RT "Creatine kinase protein sequence encoded by a cDNA made from Torpedo
RT californica electric organ mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7007-7011(1984).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, AND
RP SUBUNIT.
RX PubMed=12437342; DOI=10.1021/bi026655p;
RA Lahiri S.D., Wang P.-F., Babbitt P.C., McLeish M.J., Kenyon G.L.,
RA Allen K.N.;
RT "The 2.1 A structure of Torpedo californica creatine kinase complexed with
RT the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex.";
RL Biochemistry 41:13861-13867(2002).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate). Creatine kinase
CC isoenzymes play a central role in energy transduction in tissues with
CC large, fluctuating energy demands, such as skeletal muscle, heart,
CC brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine;
CC Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10029};
CC -!- SUBUNIT: Dimer of identical or non-identical chains. With MM being the
CC major form in skeletal muscle and myocardium, MB existing in
CC myocardium, and BB existing in many tissues, especially brain.
CC {ECO:0000269|PubMed:12437342}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: This electric ray muscle-specific creatine kinase (MM
CC 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.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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DR EMBL; M36427; AAA49278.1; -; mRNA.
DR PIR; A00677; KIRYCT.
DR PDB; 1VRP; X-ray; 2.10 A; A/B=1-381.
DR PDBsum; 1VRP; -.
DR AlphaFoldDB; P04414; -.
DR SMR; P04414; -.
DR EvolutionaryTrace; P04414; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase M-type"
FT /id="PRO_0000211981"
FT DOMAIN 11..98
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 125..367
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 128..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 320..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1VRP"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1VRP"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1VRP"
FT TURN 204..214
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 223..244
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 246..266
FT /evidence="ECO:0007829|PDB:1VRP"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:1VRP"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 346..368
FT /evidence="ECO:0007829|PDB:1VRP"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1VRP"
SQ 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
