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Creatine kinase S-type, mitochondrial (EC 2.7.3.2) (Basic-type mitochondrial creatine kinase) (Mib-CK) (RSMTCK) (Sarcomeric mitochondrial creatine kinase) (S-MtCK)

 KCRS_RABIT              Reviewed;         419 AA.
O77814;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 90.
RecName: Full=Creatine kinase S-type, mitochondrial;
EC=2.7.3.2;
AltName: Full=Basic-type mitochondrial creatine kinase;
Short=Mib-CK;
AltName: Full=RSMTCK;
AltName: Full=Sarcomeric mitochondrial creatine kinase;
Short=S-MtCK;
Flags: Precursor;
Name=CKMT2;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=10497082; DOI=10.1006/prep.1999.1105;
Marcillat O., Perraut C., Granjon T., Vial C., Vacheron M.J.;
"Cloning, Escherichia coli expression, and phase-transition
chromatography-based purification of recombinant rabbit heart
mitochondrial creatine kinase.";
Protein Expr. Purif. 17:163-168(1999).
-!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
ATP and various phosphogens (e.g. creatine phosphate). Creatine
kinase isoenzymes play a central role in energy transduction in
tissues with large, fluctuating energy demands, such as skeletal
muscle, heart, brain and spermatozoa (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
{ECO:0000255|PROSITE-ProRule:PRU10029}.
-!- SUBUNIT: Exists as an octamer composed of four CKMT2 homodimers.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Intermembrane side
{ECO:0000250}.
-!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
-!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
ProRule:PRU00843}.
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EMBL; AJ011334; CAA09597.1; -; mRNA.
RefSeq; NP_001156542.1; NM_001163070.1.
UniGene; Ocu.3234; -.
ProteinModelPortal; O77814; -.
SMR; O77814; -.
STRING; 9986.ENSOCUP00000009646; -.
PRIDE; O77814; -.
GeneID; 100302412; -.
KEGG; ocu:100302412; -.
CTD; 1160; -.
eggNOG; KOG3581; Eukaryota.
eggNOG; COG3869; LUCA.
HOGENOM; HOG000232165; -.
HOVERGEN; HBG001339; -.
InParanoid; O77814; -.
KO; K00933; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
Gene3D; 1.10.135.10; -; 1.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR000749; ATP-guanido_PTrfase.
InterPro; IPR022415; ATP-guanido_PTrfase_AS.
InterPro; IPR022414; ATP-guanido_PTrfase_cat.
InterPro; IPR022413; ATP-guanido_PTrfase_N.
InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
PANTHER; PTHR11547; PTHR11547; 1.
Pfam; PF00217; ATP-gua_Ptrans; 1.
Pfam; PF02807; ATP-gua_PtransN; 1.
SUPFAM; SSF48034; SSF48034; 1.
SUPFAM; SSF55931; SSF55931; 1.
PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Kinase; Membrane; Mitochondrion;
Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase; Transit peptide.
TRANSIT 1 39 Mitochondrion.
CHAIN 40 419 Creatine kinase S-type, mitochondrial.
/FTId=PRO_0000016597.
DOMAIN 46 132 Phosphagen kinase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00842}.
DOMAIN 159 401 Phosphagen kinase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00843}.
NP_BIND 162 166 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
NP_BIND 354 359 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
REGION 40 64 Cardiolipin-binding. {ECO:0000250}.
BINDING 225 225 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 270 270 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 326 326 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 369 369 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
MOD_RES 255 255 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09605}.
MOD_RES 356 356 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6P8J7}.
SEQUENCE 419 AA; 47407 MW; C26469B25730CC6F CRC64;
MASTFSKLLT GRNASLLFAT LGTSALTTGY LVNRQKVCAE ARDQHKLFPP SADYPDLRKH
NNCMAECLTP SIYAKLRNKV TANGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
DLFDPVIKLR HNGYDPRVMK HPTDLDASKI TQGQFDERYV LSSRVRTGRS IRGLSLPPAC
SRAEAREVEN VAITALEGLK GDLAGRYYRL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG
MARDWPDARG IWHNYDNTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD
TRAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK


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