ID   KCRS_MOUSE              Reviewed;         419 AA.
AC   Q6P8J7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 141.
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   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 [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Lung;
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   [2]
RP   PROTEIN SEQUENCE OF 311-326, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-356, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
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 (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 CKMT2 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   -!- 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; BC061221; AAH61221.1; -; mRNA.
DR   CCDS; CCDS26679.1; -.
DR   RefSeq; NP_940807.1; NM_198415.2.
DR   AlphaFoldDB; Q6P8J7; -.
DR   SMR; Q6P8J7; -.
DR   BioGRID; 218280; 18.
DR   IntAct; Q6P8J7; 3.
DR   MINT; Q6P8J7; -.
DR   STRING; 10090.ENSMUSP00000022122; -.
DR   CarbonylDB; Q6P8J7; -.
DR   GlyGen; Q6P8J7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6P8J7; -.
DR   PhosphoSitePlus; Q6P8J7; -.
DR   SwissPalm; Q6P8J7; -.
DR   jPOST; Q6P8J7; -.
DR   MaxQB; Q6P8J7; -.
DR   PaxDb; 10090-ENSMUSP00000022122; -.
DR   PeptideAtlas; Q6P8J7; -.
DR   ProteomicsDB; 263511; -.
DR   Antibodypedia; 12782; 457 antibodies from 34 providers.
DR   DNASU; 76722; -.
DR   Ensembl; ENSMUST00000022122.4; ENSMUSP00000022122.4; ENSMUSG00000021622.4.
DR   GeneID; 76722; -.
DR   KEGG; mmu:76722; -.
DR   UCSC; uc007rkc.1; mouse.
DR   AGR; MGI:1923972; -.
DR   CTD; 1160; -.
DR   MGI; MGI:1923972; Ckmt2.
DR   VEuPathDB; HostDB:ENSMUSG00000021622; -.
DR   eggNOG; KOG3581; Eukaryota.
DR   GeneTree; ENSGT00950000182772; -.
DR   HOGENOM; CLU_019868_4_2_1; -.
DR   InParanoid; Q6P8J7; -.
DR   OMA; YHGQEEN; -.
DR   OrthoDB; 35839at2759; -.
DR   PhylomeDB; Q6P8J7; -.
DR   TreeFam; TF314214; -.
DR   Reactome; R-MMU-71288; Creatine metabolism.
DR   BioGRID-ORCS; 76722; 4 hits in 78 CRISPR screens.
DR   PRO; PR:Q6P8J7; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q6P8J7; Protein.
DR   Bgee; ENSMUSG00000021622; Expressed in plantaris and 86 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:1901612; F:cardiolipin binding; ISO:MGI.
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:0006603; P:phosphocreatine metabolic process; TAS:MGI.
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:SF19; CREATINE KINASE S-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.
DR   Genevisible; Q6P8J7; MM.
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   CHAIN           40..419
FT                   /note="Creatine kinase S-type, mitochondrial"
FT                   /id="PRO_0000016595"
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         255
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09605"
FT   MOD_RES         356
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   419 AA;  47473 MW;  E9083E4F689903EF CRC64;
     MASAFSKLLT GRNASLLFTT LGTSALTTGY LLNRQKVSAD AREQHKLFPP SADYPDLRKH
     NNCMAECLTP TIYAKLRNKM TPSGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
     DLFDPVIKLR HNGYDPRVMK HPTDLDASKI THGQFDERYV LSSRVRTGRS IRGLSLPPAC
     SRAERREVEN VAITALEGLK GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG
     MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
     RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD
     TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGRK
//