ID KCRU_PIG Reviewed; 416 AA. AC Q29577; B2ZF48; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 08-NOV-2023, entry version 99. 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 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 [LARGE SCALE MRNA]. RA Liu G.Y.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-409. RC TISSUE=Small intestine; RX PubMed=8672129; DOI=10.1007/s003359900153; RA Winteroe A.K., Fredholm M., Davies W.; RT "Evaluation and characterization of a porcine small intestine cDNA library: RT analysis of 839 clones."; RL Mamm. Genome 7:509-517(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 (By similarity). {ECO:0000250}. 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:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Intermembrane side CC {ECO:0000250}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU650786; ACD02423.1; -; mRNA. DR EMBL; F14801; CAA23265.1; -; mRNA. DR RefSeq; NP_001302567.1; NM_001315638.1. DR AlphaFoldDB; Q29577; -. DR SMR; Q29577; -. DR STRING; 9823.ENSSSCP00000005068; -. DR PaxDb; 9823-ENSSSCP00000005068; -. DR PeptideAtlas; Q29577; -. DR GeneID; 100519994; -. DR KEGG; ssc:100519994; -. DR CTD; 548596; -. DR eggNOG; KOG3581; Eukaryota. DR InParanoid; Q29577; -. DR OrthoDB; 35839at2759; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine 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 CDD; cd00716; creatine_kinase_like; 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 2: Evidence at transcript level; KW ATP-binding; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; KW Transit peptide. FT TRANSIT 1..39 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 40..416 FT /note="Creatine kinase U-type, mitochondrial" FT /id="PRO_0000211983" 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 REGION 40..63 FT /note="Cardiolipin-binding" FT /evidence="ECO:0000250" 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" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25809" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25809" FT MOD_RES 213 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00564" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30275" FT MOD_RES 355 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P07310" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30275" FT CONFLICT 365..366 FT /note="SI -> ES (in Ref. 2; CAA23265)" FT /evidence="ECO:0000305" FT CONFLICT 396..398 FT /note="CER -> LANG (in Ref. 2; CAA23265)" FT /evidence="ECO:0000305" SQ SEQUENCE 416 AA; 46950 MW; 113919BF6571CF08 CRC64; MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPIRAA SERRRQYPPS AEYPDLRKHN NCMASHLTPA VYARLCDKTT PTGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAE LFDPVIQERH NGYDPRTMKH TTDLDASKIR SGFFDERYVL SSRVRTGRSI RGLSLPPACT RAERREVERV VVDALSGLKG DLAGRYYRLS EMTEAEQQQL IDDHFLFDKP VSPLLTAAGM ARDWPDARGI WHNNEKSFLI WVNEEDHTRV ISMEKGGNMK KVFERFCRGL KEVERLIQER GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT AATGSIFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL ERGQDIRIPP PLPNKH //