KCRU_PIG
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 03-AUG-2022, entry version 94.
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}.
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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; Q29577; -.
DR PeptideAtlas; Q29577; -.
DR GeneID; 100519994; -.
DR KEGG; ssc:100519994; -.
DR CTD; 548596; -.
DR eggNOG; KOG3581; Eukaryota.
DR InParanoid; Q29577; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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: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 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 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
