KCRM_PIG
ID KCRM_PIG Reviewed; 381 AA.
AC Q5XLD3; Q45EW9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Xu D.Q., Xiong Y.Z., Ling X.F., Lang J.;
RT "Molecular cloning and characterization of porcine CKM.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ling X.F., Xiong Y.Z., Xu D.Q.;
RT "Cloning and sequence analysis of genomic structure and the proximal
RT promoter region of porcine CKM gene.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; AY754869; AAV28621.1; -; mRNA.
DR EMBL; DQ153192; AAZ66747.1; -; Genomic_DNA.
DR RefSeq; NP_001123421.1; NM_001129949.1.
DR AlphaFoldDB; Q5XLD3; -.
DR SMR; Q5XLD3; -.
DR STRING; 9823.ENSSSCP00000021419; -.
DR PeptideAtlas; Q5XLD3; -.
DR PRIDE; Q5XLD3; -.
DR Ensembl; ENSSSCT00005034041; ENSSSCP00005020770; ENSSSCG00005021466.
DR Ensembl; ENSSSCT00015008842; ENSSSCP00015003563; ENSSSCG00015006617.
DR Ensembl; ENSSSCT00025061951; ENSSSCP00025026305; ENSSSCG00025045630.
DR Ensembl; ENSSSCT00030083879; ENSSSCP00030038539; ENSSSCG00030060031.
DR Ensembl; ENSSSCT00030084010; ENSSSCP00030038619; ENSSSCG00030060031.
DR Ensembl; ENSSSCT00035093171; ENSSSCP00035039116; ENSSSCG00035068926.
DR Ensembl; ENSSSCT00040083461; ENSSSCP00040036371; ENSSSCG00040061159.
DR Ensembl; ENSSSCT00045063279; ENSSSCP00045044615; ENSSSCG00045036676.
DR Ensembl; ENSSSCT00055022694; ENSSSCP00055017951; ENSSSCG00055011557.
DR Ensembl; ENSSSCT00060036770; ENSSSCP00060015654; ENSSSCG00060027142.
DR Ensembl; ENSSSCT00065002071; ENSSSCP00065000672; ENSSSCG00065001659.
DR Ensembl; ENSSSCT00070056778; ENSSSCP00070048238; ENSSSCG00070028309.
DR GeneID; 397264; -.
DR KEGG; ssc:397264; -.
DR CTD; 1158; -.
DR eggNOG; KOG3581; Eukaryota.
DR InParanoid; Q5XLD3; -.
DR OrthoDB; 825025at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase M-type"
FT /id="PRO_0000211977"
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; 43059 MW; DF768FBFAF4E636D CRC64;
MPFGNTHNKY KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG FTLDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYVVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD
LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM
VEMEKKLEKG QSIDDMIPAQ K
