KCRM_BOVIN
ID KCRM_BOVIN Reviewed; 381 AA.
AC Q9XSC6; Q5E9Y4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MET-377.
RC TISSUE=Heart;
RA Towler E.M.;
RT "Bovine creatine kinase M.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 11-359, AND SUBUNIT.
RX PubMed=11173463; DOI=10.1107/s0907444900015614;
RA Tisi D., Bax B., Loew A.;
RT "The three-dimensional structure of cytosolic bovine retinal creatine
RT kinase.";
RL Acta Crystallogr. D 57:187-193(2001).
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 {ECO:0000250}.
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; AF120106; AAD30974.1; -; mRNA.
DR EMBL; BT020785; AAX08802.1; -; mRNA.
DR EMBL; BT021173; AAX31355.1; -; mRNA.
DR EMBL; BC102907; AAI02908.1; -; mRNA.
DR RefSeq; NP_777198.2; NM_174773.4.
DR PDB; 1G0W; X-ray; 2.30 A; A=7-359.
DR PDBsum; 1G0W; -.
DR AlphaFoldDB; Q9XSC6; -.
DR SMR; Q9XSC6; -.
DR STRING; 9913.ENSBTAP00000018492; -.
DR Allergome; 11907; Bos d CK.
DR PaxDb; Q9XSC6; -.
DR PeptideAtlas; Q9XSC6; -.
DR PRIDE; Q9XSC6; -.
DR Ensembl; ENSBTAT00000018492; ENSBTAP00000018492; ENSBTAG00000013921.
DR GeneID; 286822; -.
DR KEGG; bta:286822; -.
DR CTD; 1158; -.
DR VEuPathDB; HostDB:ENSBTAG00000013921; -.
DR VGNC; VGNC:27385; CKM.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_4_2_1; -.
DR InParanoid; Q9XSC6; -.
DR OMA; IIMQERV; -.
DR OrthoDB; 825025at2759; -.
DR TreeFam; TF314214; -.
DR EvolutionaryTrace; Q9XSC6; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000013921; Expressed in laryngeal cartilage and 82 other tissues.
DR ExpressionAtlas; Q9XSC6; baseline and differential.
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; ISS:AgBase.
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; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase M-type"
FT /id="PRO_0000211973"
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"
FT VARIANT 377
FT /note="I -> M"
FT /evidence="ECO:0000269|Ref.1"
FT CONFLICT 376
FT /note="M -> L (in Ref. 1; AAD30974)"
FT /evidence="ECO:0000305"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1G0W"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1G0W"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1G0W"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1G0W"
FT TURN 204..214
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 225..244
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 246..266
FT /evidence="ECO:0007829|PDB:1G0W"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1G0W"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:1G0W"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1G0W"
FT HELIX 346..369
FT /evidence="ECO:0007829|PDB:1G0W"
SQ SEQUENCE 381 AA; 42989 MW; C97EBBFB00BCF2FC CRC64;
MPFGNTHNKH KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG FTLDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF KPTDKHKTDL NHENLKGGDD
LDPNYVLSSR VRTGRSIKGY ALPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM
VEMEKKLEKG QSIDDMIPAQ K
