ID   KCRU_CHICK              Reviewed;         417 AA.
AC   P70079; Q90782;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 131.
DE   RecName: Full=Creatine kinase U-type, mitochondrial;
DE            EC=2.7.3.2;
DE   AltName: Full=Acidic-type mitochondrial creatine kinase;
DE            Short=Mia-CK;
DE   AltName: Full=Ubiquitous mitochondrial creatine kinase;
DE            Short=U-MtCK;
DE   Flags: Precursor;
GN   Name=CKMT1;
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 [GENOMIC DNA].
RC   STRAIN=White leghorn; TISSUE=Brain, and Liver;
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   PROTEIN SEQUENCE OF 40-68.
RC   TISSUE=Brain;
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).
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=creatine + ATP = N-phosphocreatine + ADP + H(+);
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Intermembrane side.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and gut, weakly in
CC       testis. Also found in cell bodies of neural cells of the gray matter.
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC       ProRule:PRU00843}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA65266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X96403; CAA65267.1; -; Genomic_DNA.
DR   EMBL; X96402; CAA65266.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X95526; CAA64778.1; -; Genomic_DNA.
DR   AlphaFoldDB; P70079; -.
DR   SMR; P70079; -.
DR   FunCoup; P70079; 59.
DR   STRING; 9031.ENSGALP00000013585; -.
DR   PaxDb; 9031-ENSGALP00000013585; -.
DR   VEuPathDB; HostDB:geneid_374002; -.
DR   eggNOG; KOG3581; Eukaryota.
DR   InParanoid; P70079; -.
DR   PhylomeDB; P70079; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR   CDD; cd00716; creatine_kinase_like; 1.
DR   FunFam; 3.30.590.10:FF:000002; Creatine kinase S-type, mitochondrial; 1.
DR   FunFam; 1.10.135.10:FF:000002; creatine kinase S-type, mitochondrial; 1.
DR   Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 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; ARGININE OR CREATINE KINASE; 1.
DR   PANTHER; PTHR11547:SF24; CREATINE KINASE U-TYPE, MITOCHONDRIAL; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF48034; Guanido kinase N-terminal domain; 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; Direct protein sequencing; Kinase; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2831887"
FT   CHAIN           40..417
FT                   /note="Creatine kinase U-type, mitochondrial"
FT                   /id="PRO_0000016593"
FT   DOMAIN          44..131
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          158..400
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         161..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         325
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         353..358
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   417 AA;  47104 MW;  ED9B982764153D2C CRC64;
     MASTFARALS ARRSAGLLAM VGAGSLAAGF LLARDTVSAG ERQRRRYPPS AEYPDLRKHN
     NCMASNLTPA IYARLCDKAT PNGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAE
     LFDPVIQERH NGYNPRTMKH VTDLDASKIK FGHFDERYVL SSRVRTGRSI RGLSLPPACT
     RAERREVEKV TVEALNGLTG DLSGRYYRLS EMTEKEQQQL IDDHFLFDKP VSPSLTAAGM
     ARDWPDARGI WHNNEKTFLI WINEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER
     GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT
     AATANVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL EKGQDIRIPS PVPQFRH
//