Reviewed, UniProtKB/Swiss-Prot P05123 (KCRM_CANFA)

Names and origin

Protein names

Recommended name:
    Creatine kinase M-type
    EC=2.7.3.2
Alternative name(s):
    Creatine kinase M chain
    M-CK

Gene names

Name:

CKM

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	381 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	Dimer of identical or non-identical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 381	380	Creatine kinase M-type		PRO_0000211974
Regions
	Nucleotide binding	128 – 132	5	ATP By similarity
	Nucleotide binding	320 – 325	6	ATP By similarity
Sites
	Binding site	191	1	ATP By similarity
	Binding site	236	1	ATP By similarity
	Binding site	292	1	ATP By similarity
	Binding site	335	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P05123-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 83F8D227D27472C2	FASTA	381	43,153
	10 20 30 40 50 60 MPFGNTHNKF KLNYKPEEEY PDLTKHNNHM AKALTPEIYK KLRDKETPSG FTLDDVIQTG 70 80 90 100 110 120 VDNPGHPFIM TVGCVAGDEE SYQVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD 130 140 150 160 170 180 LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSIE ALNSLTGEFK GKYYPLKSMT 190 200 210 220 230 240 EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM 250 260 270 280 290 300 QKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 310 320 330 340 350 360 HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV QLVVDGVKLM 370 380 VEMEKKLEKG QSIDDMIPAQ K

References

[1]	"Complete nucleotide sequence of dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species." Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B., Strauss A.W. Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985) [PubMed: 3866230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog heart proteins." Dunn M.J., Corbett J.M., Wheeler C.H. Electrophoresis 18:2795-2802(1997) [PubMed: 9504812] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-23. Tissue: Heart.
[3]	"Characterization of MB creatine kinase isoform conversion in vitro and in vivo in dogs." Billadello J.J., Fontanet H.L., Strauss A.W., Abendschein D.R. J. Clin. Invest. 83:1637-1643(1989) [PubMed: 2496146] [Abstract] Cited for: PROTEIN SEQUENCE OF 377-381. Tissue: Myocardium.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M11660 mRNA. Translation: AAA30836.1.
PIR	A24686.
3D structure databases
HSSP	HSSP built from PDB template 2CRK based on UniProtKB P00563.
SMR	P05123. Positions 2-381.
ModBase	Search...
2-D gel databases
HSC-2DPAGE	P05123.
Genome annotation databases
Ensembl	ENSCAFG00000004507. Canis familiaris. [Contig view]
Phylogenomic databases
HOVERGEN	P05123.
Enzyme and pathway databases
BRENDA	2.7.3.2. 463.
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

KCRM_CANFA

Accession

Primary (citable) accession number: P05123

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)