Reviewed, UniProtKB/Swiss-Prot P04414 (KCRM_TORCA)

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
Organism	Torpedo californica (Pacific electric ray)
Taxonomic identifier	7787 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Torpedinoidei › Torpedinidae › Torpedo

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. Ref.2
Subcellular location	Cytoplasm.
Miscellaneous	This electric ray muscle-specific creatine kinase (MM isozyme) is isolated from the electric organ, which derives embryologically from skeletal muscle. It may be involved in the electrical discharge process.
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	3D-structure
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

Chain

1 – 381

381

Creatine kinase M-type

PRO_0000211981

Regions

Nucleotide binding

128 – 132

5

ATP

Nucleotide binding

320 – 325

6

ATP

Sites

Binding site

191

1

ATP By similarity

Binding site

236

1

ATP By similarity

Binding site

292

1

ATP

Binding site

335

1

ATP

Secondary structure

1

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381

Helix Strand Turn

Details...

Helix

16 – 19

4

Helix

29 – 33

5

Helix

36 – 42

7

Helix

53 – 62

10

Beta strand

67 – 69

3

Helix

81 – 84

4

Helix

86 – 96

11

Helix

112 – 114

3

Turn

123 – 125

3

Beta strand

126 – 135

10

Turn

143 – 145

3

Helix

148 – 162

15

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

223 – 244

22

Helix

246 – 266

21

Turn

275 – 277

3

Helix

284 – 286

3

Beta strand

292 – 298

7

Helix

302 – 304

3

Helix

308 – 315

8

Beta strand

317 – 321

5

Beta strand

324 – 329

6

Beta strand

333 – 338

6

Beta strand

342 – 344

3

Helix

346 – 368

23

Helix

374 – 376

3

Sequences

	Sequence		Length	Mass (Da)
	P04414-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: DF4A54FDDF3BD570	FASTA	381	42,934
	10 20 30 40 50 60 MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG FTLDDIIQTG 70 80 90 100 110 120 VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY KPTDKHKTDL NQENLKGGDD 130 140 150 160 170 180 LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE RRLVEKLCID GLATLTGEFQ GKYYPLSSMS 190 200 210 220 230 240 DAEQQQLIDD HFLFDKPISP LLLASGMARD WPDGRGIWHN NDKTFLVWVN EEDHLRVISM 250 260 270 280 290 300 QKGGNMKEVF RRFCVGLKKI EDIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP 310 320 330 340 350 360 HLCKHEKFSE VLKRTRLQKR GTGGVDTAAV GSIYDISNAD RLGFSEVEQV QMVVDGVKLM 370 380 VEMEKRLENG KSIDDLMPAQ K

References

[1]	"Creatine kinase protein sequence encoded by a cDNA made from Torpedo californica electric organ mRNA." West B.L., Babbitt P.C., Mendez B., Baxter J.D. Proc. Natl. Acad. Sci. U.S.A. 81:7007-7011(1984) [PubMed: 6594677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Electric organ.
[2]	"The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex." Lahiri S.D., Wang P.-F., Babbitt P.C., McLeish M.J., Kenyon G.L., Allen K.N. Biochemistry 41:13861-13867(2002) [PubMed: 12437342] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M36427 mRNA. Translation: AAA49278.1.

PIR

KIRYCT. A00677.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VRP	X-ray	2.10	A/B	1-381	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P04414.

Enzyme and pathway databases

BRENDA

2.7.3.2. 74507.

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

P04414.

Entry information

Entry name

KCRM_TORCA

Accession

Primary (citable) accession number: P04414

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)