KCRS_CHICK
ID KCRS_CHICK Reviewed; 419 AA.
AC P11009;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Creatine kinase S-type, mitochondrial;
DE EC=2.7.3.2;
DE AltName: Full=Basic-type mitochondrial creatine kinase;
DE Short=Mib-CK;
DE AltName: Full=Sarcomeric mitochondrial creatine kinase;
DE Short=S-MtCK;
DE Flags: Precursor;
GN Name=CKMT2;
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] OF 1-39.
RC STRAIN=White leghorn;
RX PubMed=8662608; DOI=10.1074/jbc.271.20.11920;
RA Muehlebach S.M., Wirz T., Braendle U., Perriard J.-C.;
RT "Evolution of the creative kinases. The chicken acidic type mitochondrial
RT creatine kinase gene as the first nonmammalian gene.";
RL J. Biol. Chem. 271:11920-11929(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-419, AND PROTEIN SEQUENCE OF 40-69.
RC TISSUE=Heart, and Skeletal muscle;
RX PubMed=2831887; DOI=10.1016/0006-291x(88)90608-0;
RA Hossle J.P., Schlegel J., Wegmann G., Wyss M., Boehlen P.,
RA Eppenberger H.M., Wallimann T., Perriard J.-C.;
RT "Distinct tissue specific mitochondrial creatine kinases from chicken brain
RT and striated muscle with a conserved CK framework.";
RL Biochem. Biophys. Res. Commun. 151:408-416(1988).
RN [3]
RP PROTEIN SEQUENCE OF 40-48.
RX PubMed=8305443; DOI=10.1021/bi00170a014;
RA Kaldis P., Furter R., Wallimann T.;
RT "The N-terminal heptapeptide of mitochondrial creatine kinase is important
RT for octamerization.";
RL Biochemistry 33:952-959(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=8692275; DOI=10.1038/381341a0;
RA Fritz-Wolf K., Schnyder T., Wallimann T., Kabsch W.;
RT "Structure of mitochondrial creatine kinase.";
RL Nature 381:341-345(1996).
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.
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 -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC {ECO:0000269|PubMed:8692275}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side.
CC -!- TISSUE SPECIFICITY: Expressed in the leg muscle and heart.
CC -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
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; M18866; AAA48688.1; -; mRNA.
DR PIR; A27708; A27708.
DR RefSeq; NP_001161216.1; NM_001167744.1.
DR PDB; 1CRK; X-ray; 3.00 A; A/B/C/D=40-419.
DR PDBsum; 1CRK; -.
DR AlphaFoldDB; P11009; -.
DR SMR; P11009; -.
DR STRING; 9031.ENSGALP00000032149; -.
DR PaxDb; P11009; -.
DR PRIDE; P11009; -.
DR GeneID; 396508; -.
DR KEGG; gga:396508; -.
DR CTD; 1160; -.
DR VEuPathDB; HostDB:geneid_396508; -.
DR eggNOG; KOG3581; Eukaryota.
DR InParanoid; P11009; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; P11009; -.
DR BRENDA; 2.7.3.2; 1306.
DR SABIO-RK; P11009; -.
DR EvolutionaryTrace; P11009; -.
DR PRO; PR:P11009; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 1.
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; Direct protein sequencing; Kinase; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2831887,
FT ECO:0000269|PubMed:8305443"
FT CHAIN 40..419
FT /note="Creatine kinase S-type, mitochondrial"
FT /id="PRO_0000016599"
FT DOMAIN 46..132
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 159..401
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 162..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 354..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT CONFLICT 20..23
FT /note="AAGS -> CSRQ (in Ref. 2; AAA48688)"
FT /evidence="ECO:0000305"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 243..248
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 259..278
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 280..300
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1CRK"
FT TURN 359..363
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:1CRK"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:1CRK"
FT HELIX 380..402
FT /evidence="ECO:0007829|PDB:1CRK"
SQ SEQUENCE 419 AA; 47084 MW; 9ACC60D709B9283F CRC64;
MAGTFGRLLA GRVTAALFAA AGSGVLTTGY LLNQQNVKAT VHEKRKLFPP SADYPDLRKH
NNCMAECLTP AIYAKLRDKL TPNGYSLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
EIFDPVIKAR HNGYDPRTMK HHTDLDASKI THGQFDERYV LSSRVRTGRS IRGLSLPPAC
SRAERREVEN VVVTALAGLK GDLSGKYYSL TNMSERDQQQ LIDDHFLFDK PVSPLLTCAG
MARDWPDARG IWHNNDKTFL VWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIKE
RGWEFMWNER LGYVLTCPSN LGTGLRAGVH VKLPRLSKDP RFPKILENLR LQKRGTGGVD
TAAVADVYDI SNLDRMGRSE VELVQIVIDG VNYLVDCEKK LEKGQDIKVP PPLPQFGRK
