NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
DOI=10.1006/prep.1999.1105; PubMed=10497082 [NCBI, ExPASy, EBI, Israel, Japan]
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).

Comments

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).
CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
SUBUNIT: Exists as an octamer composed of four CKMT2 homodimers (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side (By similarity).
MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ011334; CAA09597.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P11009; 1CRK. [HSSP ENTRY / PDB]

SMR

O77814; 47-413.

ModBase

O77814.

Family and domain databases

InterPro

IPR000749; ATP-gua_Ptrans.
IPR014746; Gln_synth/guanido_kin_cat.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.

PANTHER

PTHR11547; ATP-gua_Ptrans; 1.

Pfam

PF00217; ATP-gua_Ptrans; 1.
PF02807; ATP-gua_PtransN; 1.
Pfam graphical view of domain structure.

PROSITE

PS00112; GUANIDO_KINASE; 1.

BLOCKS

O77814.

Genome annotation databases

Ensembl

ENSOCUG00000011211; Oryctolagus cuniculus. [Contig view]

Phylogenomic databases

HOVERGEN

O77814; -.

Other

ProtoNet

O77814.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Transferase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion.`
`CHAIN`	`40 419`	`380`	`Creatine kinase, sarcomeric mitochondrial.`	`PRO_0000016597`
`NP_BIND`	`162 166`	`5`	`ATP (By similarity).`
`NP_BIND`	`354 359`	`6`	`ATP (By similarity).`
`REGION`	`40 64`	`25`	`Cardiolipin-binding (By similarity).`
`ACT_SITE`	`317 317`		`By similarity.`
`BINDING`	`225 225`		`ATP (By similarity).`
`BINDING`	`326 326`		`ATP (By similarity).`
`BINDING`	`369 369`		`ATP (By similarity).`

Sequence information

Length: 419 AA [This is the length of the unprocessed precursor]

Molecular weight: 47407 Da [This is the MW of the unprocessed precursor]

CRC64: C26469B25730CC6F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASTFSKLLT GRNASLLFAT LGTSALTTGY LVNRQKVCAE ARDQHKLFPP SADYPDLRKH 

        70         80         90        100        110        120 
NNCMAECLTP SIYAKLRNKV TANGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA 

       130        140        150        160        170        180 
DLFDPVIKLR HNGYDPRVMK HPTDLDASKI TQGQFDERYV LSSRVRTGRS IRGLSLPPAC 

       190        200        210        220        230        240 
SRAEAREVEN VAITALEGLK GDLAGRYYRL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG 

       250        260        270        280        290        300 
MARDWPDARG IWHNYDNTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE 

       310        320        330        340        350        360 
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD 

       370        380        390        400        410 
TRAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK

O77814 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools