KCRM_RABIT
ID KCRM_RABIT Reviewed; 381 AA.
AC P00563;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Creatine kinase M-type;
DE EC=2.7.3.2 {ECO:0000269|PubMed:5499971};
DE AltName: Full=Creatine kinase M chain;
DE AltName: Full=Creatine phosphokinase M-type;
DE Short=CPK-M;
DE AltName: Full=M-CK;
GN Name=CKM;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3857581; DOI=10.1073/pnas.82.8.2310;
RA Pickering L., Pang H., Biemann K., Munro H., Schimmel P.;
RT "Two tissue-specific isozymes of creatine kinase have closely matched amino
RT acid sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6094551; DOI=10.1016/s0021-9258(17)42593-2;
RA Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L.,
RA Belagaje R., Biemann K., Page D., Kuby S., Schimmel P.;
RT "Rabbit muscle creatine phosphokinase. cDNA cloning, primary structure and
RT detection of human homologues.";
RL J. Biol. Chem. 259:14317-14320(1984).
RN [3]
RP CATALYTIC ACTIVITY, AND INHIBITION BY CHEMICAL MODIFICATION.
RX PubMed=5499971; DOI=10.1042/bj1200589;
RA Atherton R.S., Laws J.F., Miles B.J., Thomson A.R.;
RT "Brain adenosine 5'-triphosphate-creatine phosphotransferase.";
RL Biochem. J. 120:589-600(1970).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RC TISSUE=Muscle;
RX PubMed=9849893; DOI=10.1016/s0014-5793(98)01355-6;
RA Rao J.K., Bujacz G., Wlodawer A.;
RT "Crystal structure of rabbit muscle creatine kinase.";
RL FEBS Lett. 439:133-137(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.
RX PubMed=17327675; DOI=10.1107/s0907444906056204;
RA Ohren J.F., Kundracik M.L., Borders C.L. Jr., Edmiston P., Viola R.E.;
RT "Structural asymmetry and intersubunit communication in muscle creatine
RT kinase.";
RL Acta Crystallogr. D 63:381-389(2007).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate) (PubMed:5499971).
CC Creatine kinase isoenzymes play a central role in energy transduction
CC in tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa (Probable).
CC {ECO:0000269|PubMed:5499971, ECO:0000305}.
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 ECO:0000269|PubMed:5499971};
CC -!- SUBUNIT: Dimer of identical or non-identical chains, which can be
CC either B (brain type) or M (muscle type). With MM being the major form
CC in skeletal muscle and myocardium, MB existing in myocardium, and BB
CC existing in many tissues, especially brain.
CC {ECO:0000250|UniProtKB:P12277}.
CC -!- INTERACTION:
CC P00563; P11974: PKM; NbExp=2; IntAct=EBI-2750756, EBI-7133357;
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/CRK/";
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DR EMBL; K02831; AAA31205.1; -; mRNA.
DR PIR; A00673; KIRBCM.
DR RefSeq; NP_001075708.1; NM_001082239.1.
DR PDB; 1U6R; X-ray; 1.65 A; A/B=2-381.
DR PDB; 2CRK; X-ray; 2.35 A; A=1-381.
DR PDBsum; 1U6R; -.
DR PDBsum; 2CRK; -.
DR AlphaFoldDB; P00563; -.
DR SMR; P00563; -.
DR IntAct; P00563; 1.
DR MINT; P00563; -.
DR STRING; 9986.ENSOCUP00000020805; -.
DR BindingDB; P00563; -.
DR ChEMBL; CHEMBL1075201; -.
DR PRIDE; P00563; -.
DR GeneID; 100009056; -.
DR KEGG; ocu:100009056; -.
DR CTD; 1158; -.
DR eggNOG; KOG3581; Eukaryota.
DR InParanoid; P00563; -.
DR OrthoDB; 825025at2759; -.
DR BRENDA; 2.7.3.2; 1749.
DR SABIO-RK; P00563; -.
DR EvolutionaryTrace; P00563; -.
DR PRO; PR:P00563; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; ISS:AgBase.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; ISS:AgBase.
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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase M-type"
FT /id="PRO_0000211978"
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 /evidence="ECO:0000305|PubMed:17327675"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17327675"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17327675"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17327675"
FT BINDING 320..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17327675"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2CRK"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1U6R"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1U6R"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1U6R"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1U6R"
FT TURN 204..214
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 225..244
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 246..267
FT /evidence="ECO:0007829|PDB:1U6R"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1U6R"
FT HELIX 346..369
FT /evidence="ECO:0007829|PDB:1U6R"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1U6R"
SQ SEQUENCE 381 AA; 43112 MW; 821447F395FE71CC CRC64;
MPFGNTHNKY KLNYKSEEEY PDLSKHNNHM AKVLTPDLYK KLRDKETPSG FTLDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF KPTDKHKTDL NHENLKGGDD
LDPHYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV QLVVDGVKLM
VEMEKKLEKG QSIDDMIPAQ K
