KCRM_CHICK
ID KCRM_CHICK Reviewed; 381 AA.
AC P00565;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Creatine kinase M-type {ECO:0000303|PubMed:6091045, ECO:0000303|PubMed:8525081};
DE EC=2.7.3.2 {ECO:0000269|PubMed:8525081};
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 {ECO:0000303|PubMed:8525081};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=6091045; DOI=10.1093/nar/12.18.6925;
RA Kwiatkowski R.W., Schweinfest C.W., Dottin R.P.;
RT "Molecular cloning and the complete nucleotide sequence of the creatine
RT kinase-M cDNA from chicken.";
RL Nucleic Acids Res. 12:6925-6934(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6096363; DOI=10.1016/s0021-9258(17)42538-5;
RA Ordahl C.P., Evans G.L., Cooper T.A., Kunz G., Perriard J.-C.;
RT "Complete cDNA-derived amino acid sequence of chick muscle creatine
RT kinase.";
RL J. Biol. Chem. 259:15224-15227(1984).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8525081; DOI=10.1016/0034-5288(95)90026-8;
RA Mitchell M.A., Sandercock D.A.;
RT "Creatine kinase isoenzyme profiles in the plasma of the domestic fowl
RT (Gallus domesticus): effects of acute heat stress.";
RL Res. Vet. Sci. 59:30-34(1995).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate) (PubMed:8525081).
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:8525081, 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:8525081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158;
CC Evidence={ECO:0000269|PubMed:8525081};
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 -!- TISSUE SPECIFICITY: Predominantly found in skeletal muscle, but not in
CC the heart. {ECO:0000269|PubMed:6091045}.
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; M10012; AAA48689.1; -; mRNA.
DR EMBL; X00954; CAA25465.1; -; mRNA.
DR EMBL; X00954; CAA25466.2; -; mRNA.
DR PIR; A00675; KICHCM.
DR RefSeq; NP_990838.1; NM_205507.1.
DR AlphaFoldDB; P00565; -.
DR SMR; P00565; -.
DR iPTMnet; P00565; -.
DR PRIDE; P00565; -.
DR GeneID; 107051134; -.
DR VEuPathDB; HostDB:geneid_396248; -.
DR InParanoid; P00565; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; P00565; -.
DR PRO; PR:P00565; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IDA: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; IDA: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; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase M-type"
FT /id="PRO_0000211980"
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 REGION 99..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 381 AA; 43328 MW; 192C236BB46E2531 CRC64;
MPFSSTHNKH KLKFSAEEEF PDLSKHNNHM AKVLTPELYK RLRDKETPSG FTLDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYEVFKDLFD PVIQDRHGGY KPTDKHRTDL NHENLKGGDD
LDPKYVLSSR VRTGRSIKGY SLPPHCSRGE RRAVEKLSVE ALNSLEGEFK GRYYPLKAMT
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM
EKGGNMKEVF RRFCVGLKKI EEIFKKAGHP FMWTEHLGYI LTCPSNLGTG LRGGVHVKLP
KLSQHPKFEE ILHRLRLQKR GTGGVDTAAV GAVFDISNAD RLGFSEVEQV QMVVDGVKLM
VEMEKKLEQN QPIDDMIPAQ K
