KCRU_MOUSE
ID KCRU_MOUSE Reviewed; 418 AA.
AC P30275;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 174.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=7598809; DOI=10.1089/dna.1995.14.539;
RA Steeghs K., Peters W., Brueckwilder M., Croes H., van Alewijk D.,
RA Wieringa B.;
RT "Mouse ubiquitous mitochondrial creatine kinase: gene organization and
RT consequences from inactivation in mouse embryonic stem cells.";
RL DNA Cell Biol. 14:539-553(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 47-75; 105-130; 152-158; 173-182; 191-200; 250-270;
RP 302-326 AND 355-375, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233 AND SER-366, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- INTERACTION:
CC P30275; P41969: Elk1; NbExp=2; IntAct=EBI-773103, EBI-15576110;
CC P30275; Q5S007: LRRK2; Xeno; NbExp=2; IntAct=EBI-773103, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side.
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; Z13968; CAA78371.1; -; mRNA.
DR EMBL; Z13969; CAA78372.1; -; Genomic_DNA.
DR EMBL; BC025976; AAH25976.1; -; mRNA.
DR CCDS; CCDS16640.1; -.
DR PIR; I48308; S24612.
DR RefSeq; NP_034027.1; NM_009897.2.
DR RefSeq; XP_006498718.1; XM_006498655.1.
DR RefSeq; XP_006498719.1; XM_006498656.2.
DR AlphaFoldDB; P30275; -.
DR SMR; P30275; -.
DR BioGRID; 198727; 3.
DR DIP; DIP-32284N; -.
DR IntAct; P30275; 6.
DR MINT; P30275; -.
DR STRING; 10090.ENSMUSP00000000317; -.
DR iPTMnet; P30275; -.
DR PhosphoSitePlus; P30275; -.
DR SwissPalm; P30275; -.
DR jPOST; P30275; -.
DR PaxDb; P30275; -.
DR PeptideAtlas; P30275; -.
DR PRIDE; P30275; -.
DR ProteomicsDB; 269284; -.
DR DNASU; 12716; -.
DR Ensembl; ENSMUST00000000317; ENSMUSP00000000317; ENSMUSG00000000308.
DR Ensembl; ENSMUST00000078222; ENSMUSP00000077349; ENSMUSG00000000308.
DR GeneID; 12716; -.
DR KEGG; mmu:12716; -.
DR UCSC; uc008lyt.1; mouse.
DR CTD; 12716; -.
DR MGI; MGI:99441; Ckmt1.
DR VEuPathDB; HostDB:ENSMUSG00000000308; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_4_2_1; -.
DR InParanoid; P30275; -.
DR OMA; NCMASAM; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; P30275; -.
DR TreeFam; TF314214; -.
DR BRENDA; 2.7.3.2; 3474.
DR Reactome; R-MMU-71288; Creatine metabolism.
DR BioGRID-ORCS; 12716; 2 hits in 73 CRISPR screens.
DR PRO; PR:P30275; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P30275; protein.
DR Bgee; ENSMUSG00000000308; Expressed in left colon and 187 other tissues.
DR ExpressionAtlas; P30275; baseline and differential.
DR Genevisible; P30275; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044289; C:mitochondrial inner-outer membrane contact site; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:ParkinsonsUK-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL.
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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 40..418
FT /note="Creatine kinase U-type, mitochondrial"
FT /id="PRO_0000016591"
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 REGION 40..64
FT /note="Cardiolipin-binding"
FT /evidence="ECO:0000250"
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 MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25809"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25809"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 418 AA; 47004 MW; 993CD8C290C8BFB9 CRC64;
MAGPFSRLLS ARPGLRLLAL AGAGSLTAGI LLRPESVGAA AAERRRLYPP SAEYPDLRKH
NNCMASHLTP AVYARLCDKT TPTGWTLDQC IQTGVDNPGH PFIKTVGMVA GDEETYEVFA
ELFDPVIQER HNGYDPRTMK HTTDLDASKI RSGYFDERYV LSSRVRTGRS IRGLSLPPAC
TRAERREVER VVVDALSGLK GDLAGRYYRL SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG
MARDWPDARG IWHNNEKSFL IWVNEEDHTR VISMEKGGNM KRVFERFCRG LKEVEKLIQE
RGWEFMWNER LGYILTCPSN LGTGLRAGVH IKLPLLSKDN RFPKILENLR LQKRGTGGVD
TAATGSVFDI SNLDRLGKSE VELVQLVIDG VNYLIDCERR LERGQDIRIP PPLVHSKH
