KCRM_CANLF
ID KCRM_CANLF Reviewed; 381 AA.
AC P05123;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Creatine kinase M-type;
DE EC=2.7.3.2 {ECO:0000250|UniProtKB:P00563};
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=3866230; DOI=10.1073/pnas.82.24.8394;
RA Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B., Strauss A.W.;
RT "Complete nucleotide sequence of dog heart creatine kinase mRNA:
RT conservation of amino acid sequence within and among species.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-23.
RC TISSUE=Heart;
RX PubMed=9504812; DOI=10.1002/elps.1150181514;
RA Dunn M.J., Corbett J.M., Wheeler C.H.;
RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT heart proteins.";
RL Electrophoresis 18:2795-2802(1997).
RN [3]
RP PROTEIN SEQUENCE OF 377-381.
RC TISSUE=Myocardium;
RX PubMed=2496146; DOI=10.1172/jci114062;
RA Billadello J.J., Fontanet H.L., Strauss A.W., Abendschein D.R.;
RT "Characterization of MB creatine kinase isoform conversion in vitro and in
RT vivo in dogs.";
RL J. Clin. Invest. 83:1637-1643(1989).
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. {ECO:0000250|UniProtKB:P00563}.
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:0000250|UniProtKB:P00563, ECO:0000255|PROSITE-
CC ProRule:PRU10029};
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
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; M11660; AAA30836.1; -; mRNA.
DR PIR; A24686; A24686.
DR RefSeq; NP_001300705.1; NM_001313776.1.
DR AlphaFoldDB; P05123; -.
DR SMR; P05123; -.
DR STRING; 9615.ENSCAFP00000041666; -.
DR UCD-2DPAGE; P05123; -.
DR PaxDb; P05123; -.
DR PRIDE; P05123; -.
DR Ensembl; ENSCAFT00030004913; ENSCAFP00030004365; ENSCAFG00030002587.
DR Ensembl; ENSCAFT00845010014; ENSCAFP00845007817; ENSCAFG00845005622.
DR GeneID; 476435; -.
DR KEGG; cfa:476435; -.
DR CTD; 1158; -.
DR VEuPathDB; HostDB:ENSCAFG00845005622; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR InParanoid; P05123; -.
DR OrthoDB; 825025at2759; -.
DR Reactome; R-CFA-71288; Creatine metabolism.
DR Proteomes; UP000002254; Chromosome 1.
DR Bgee; ENSCAFG00000004507; Expressed in smooth muscle tissue and 47 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
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 ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9504812"
FT CHAIN 2..381
FT /note="Creatine kinase M-type"
FT /id="PRO_0000211974"
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:0000255|PROSITE-ProRule:PRU00843"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 320..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
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"
SQ SEQUENCE 381 AA; 43153 MW; 83F8D227D27472C2 CRC64;
MPFGNTHNKF KLNYKPEEEY PDLTKHNNHM AKALTPEIYK KLRDKETPSG FTLDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYQVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD
LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSIE ALNSLTGEFK GKYYPLKSMT
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM
QKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV QLVVDGVKLM
VEMEKKLEKG QSIDDMIPAQ K
