Reviewed, UniProtKB/Swiss-Prot P00563 (KCRM_RABIT)

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

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure
Gene Ontology (GO)
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

Chain

1 – 381

381

Creatine kinase M-type

PRO_0000211978

Regions

Nucleotide binding

128 – 132

5

ATP

Nucleotide binding

320 – 325

6

ATP

Sites

Binding site

191

1

ATP

Binding site

236

1

ATP

Binding site

292

1

ATP

Secondary structure

1

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381

Helix Strand Turn

Details...

Helix

6 – 11

6

Helix

16 – 19

4

Helix

29 – 33

5

Helix

36 – 42

7

Helix

53 – 62

10

Helix

81 – 84

4

Helix

86 – 96

11

Turn

97 – 99

3

Helix

112 – 114

3

Turn

123 – 125

3

Beta strand

126 – 135

10

Turn

143 – 145

3

Helix

148 – 163

16

Helix

167 – 169

3

Beta strand

171 – 175

5

Helix

176 – 178

3

Helix

181 – 189

9

Helix

200 – 203

4

Turn

204 – 214

11

Beta strand

216 – 220

5

Beta strand

225 – 244

20

Helix

246 – 267

22

Turn

275 – 277

3

Helix

284 – 286

3

Beta strand

292 – 298

7

Helix

300 – 303

4

Helix

308 – 315

8

Beta strand

317 – 320

4

Beta strand

322 – 324

3

Beta strand

333 – 338

6

Beta strand

342 – 344

3

Helix

346 – 369

24

Beta strand

374 – 376

3

Sequences

	Sequence		Length	Mass (Da)
	P00563-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 821447F395FE71CC	FASTA	381	43,112
	10 20 30 40 50 60 MPFGNTHNKY KLNYKSEEEY PDLSKHNNHM AKVLTPDLYK KLRDKETPSG FTLDDVIQTG 70 80 90 100 110 120 VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF KPTDKHKTDL NHENLKGGDD 130 140 150 160 170 180 LDPHYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT 190 200 210 220 230 240 EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM 250 260 270 280 290 300 EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 310 320 330 340 350 360 HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV QLVVDGVKLM 370 380 VEMEKKLEKG QSIDDMIPAQ K

References

[1]	"Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences." Pickering L., Pang H., Biemann K., Munro H., Schimmel P. Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985) [PubMed: 3857581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Rabbit muscle creatine phosphokinase. cDNA cloning, primary structure and detection of human homologues." Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L., Belagaje R., Biemann K., Page D., Kuby S., Schimmel P. J. Biol. Chem. 259:14317-14320(1984) [PubMed: 6094551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Brain adenosine 5'-triphosphate-creatine phosphotransferase." Atherton R.S., Laws J.F., Miles B.J., Thomson A.R. Biochem. J. 120:589-600(1970) [PubMed: 5499971] [Abstract] Cited for: ACTIVE SITE.
[4]	"Crystal structure of rabbit muscle creatine kinase." Rao J.K., Bujacz G., Wlodawer A. FEBS Lett. 439:133-137(1998) [PubMed: 9849893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS). Tissue: Muscle.
[5]	"Structural asymmetry and intersubunit communication in muscle creatine kinase." Ohren J.F., Kundracik M.L., Borders C.L. Jr., Edmiston P., Viola R.E. Acta Crystallogr. D 63:381-389(2007) [PubMed: 17327675] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

K02831 mRNA. Translation: AAA31205.1.

PIR

KIRBCM. A00673.

RefSeq

NP_001075708.1.

UniGene

Ocu.6249

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U6R	X-ray	1.65	A/B	2-381	[»]
2CRK	X-ray	2.35	A	1-381	[»]

ModBase

Search...

Genome annotation databases

GeneID

100009056.

Phylogenomic databases

HOVERGEN

P00563.

Enzyme and pathway databases

BRENDA

2.7.3.2. 255.

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...

Other Resources

PMAP-CutDB

P00563.

Entry information

Entry name

KCRM_RABIT

Accession

Primary (citable) accession number: P00563

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)