Reviewed, UniProtKB/Swiss-Prot P09605 (KCRS_RAT)

Names and origin

Protein names

Recommended name:
    Creatine kinase S-type, mitochondrial
    EC=2.7.3.2
Alternative name(s):
    Sarcomeric mitochondrial creatine kinase
      Short name=S-MtCK
    Basic-type mitochondrial creatine kinase
      Short name=Mib-CK

Gene names

Name:

Ckmt2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Catalytic activity	ATP + creatine = ADP + phosphocreatine.
Subunit structure	Exists as an octamer composed of four CKMT2 homodimers.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Tissue specificity	Sarcomere-specific. Found only in heart and skeletal muscles.
Miscellaneous	Mitochondrial creatine kinase binds cardiolipin.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	phosphocreatine biosynthetic process Ref.1 Traceable author statement. Source: RGD
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW sarcomere Ref.1 Traceable author statement. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Ref.1 Traceable author statement. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion Ref.2
	Chain	40 – 419	380	Creatine kinase S-type, mitochondrial		PRO_0000016598
Regions
	Nucleotide binding	162 – 166	5	ATP By similarity
	Nucleotide binding	354 – 359	6	ATP By similarity
	Region	40 – 64	25	Cardiolipin-binding
Sites
	Binding site	225	1	ATP By similarity
	Binding site	270	1	ATP By similarity
	Binding site	326	1	ATP By similarity
	Binding site	369	1	ATP By similarity
Experimental info
	Sequence conflict	45	1	H → C AA sequence Ref.2
	Sequence conflict	51	1	S → H AA sequence Ref.2
	Sequence conflict	71 – 72	2	TI → IK AA sequence Ref.2
	Sequence conflict	77 – 79	3	RNK → NCG AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P09605-1 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: 106041417F5D412F	FASTA	419	47,385
	10 20 30 40 50 60 MASAFSKLLT GRNASLLFTT LGTSALTTGY LLNRQKVSAD AREQHKLFPP SADYPDLRKH 70 80 90 100 110 120 NNCMAECLTP TIYAKLRNKM TPSGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA 130 140 150 160 170 180 DLFDPVIKLR HNGYDPRLMK HPADLDASKI THGQFDERYV LSSRVRTGRS IRGLSLPPAC 190 200 210 220 230 240 SRAERREVEN VAITALGGLK GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG 250 260 270 280 290 300 MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE 310 320 330 340 350 360 RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD 370 380 390 400 410 TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGRK

References

[1]	"Structural characterization and tissue-specific expression of the mRNAs encoding isoenzymes from two rat mitochondrial creatine kinase genes." Payne R.M., Haas R.C., Strauss A.W. Biochim. Biophys. Acta 1089:352-361(1991) [PubMed: 1859839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Heart.
[2]	"Identification and primary structure of the cardiolipin-binding domain of mitochondrial creatine kinase." Cheneval D., Carafoli E. Eur. J. Biochem. 171:1-9(1988) [PubMed: 3338460] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-79. Tissue: Heart.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X59736 mRNA. Translation: CAA42414.1.
IPI	IPI00188313.
PIR	S17188.
UniGene	Rn.202308
3D structure databases
HSSP	HSSP built from PDB template 1CRK based on UniProtKB P11009.
SMR	P09605. Positions 47-413.
ModBase	Search...
2-D gel databases
Rat-heart-2DPAGE	P09605.
Proteomic databases
PRIDE	P09605.
Organism-specific databases
RGD	61977. Ckmt2.
Phylogenomic databases
HOVERGEN	P09605.
Enzyme and pathway databases
BRENDA	2.7.3.2. 248.
Gene expression databases
Genevestigator	P09605.
Family and domain databases
InterPro	IPR000749. ATP-guanido_PTrfase. IPR014746. Gln_synth/guanido_kin_cat. [Graphical view]
Gene3D	G3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit. G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
PANTHER	PTHR11547. ATP-gua_Ptrans. 1 hit.
Pfam	PF00217. ATP-gua_Ptrans. 1 hit. PF02807. ATP-gua_PtransN. 1 hit. [Graphical view]
PROSITE	PS00112. GUANIDO_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KCRS_RAT

Accession

Primary (citable) accession number: P09605

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 1, 1992
Last modified:	October 13, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)