KCRS_MOUSE
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 03-AUG-2022, entry version 132.
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 iPTMnet; Q6P8J7; -.
DR PhosphoSitePlus; Q6P8J7; -.
DR SwissPalm; Q6P8J7; -.
DR jPOST; Q6P8J7; -.
DR MaxQB; Q6P8J7; -.
DR PaxDb; Q6P8J7; -.
DR PeptideAtlas; Q6P8J7; -.
DR PRIDE; Q6P8J7; -.
DR ProteomicsDB; 263511; -.
DR Antibodypedia; 12782; 427 antibodies from 34 providers.
DR DNASU; 76722; -.
DR Ensembl; ENSMUST00000022122; ENSMUSP00000022122; ENSMUSG00000021622.
DR GeneID; 76722; -.
DR KEGG; mmu:76722; -.
DR UCSC; uc007rkc.1; mouse.
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; ECLTPTI; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; Q6P8J7; -.
DR TreeFam; TF314214; -.
DR Reactome; R-MMU-71288; Creatine metabolism.
DR BioGRID-ORCS; 76722; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q6P8J7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6P8J7; protein.
DR Bgee; ENSMUSG00000021622; Expressed in plantaris and 86 other tissues.
DR Genevisible; Q6P8J7; MM.
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:0016301; F: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 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 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
