Reviewed, UniProtKB/Swiss-Prot P00566 (KCRM_TORMA)

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     NU-2 protein
Organism	Torpedo marmorata (Marbled electric ray)
Taxonomic identifier	7788 [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 transcript 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.
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
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_0000211982
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)
	P00566-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: AE0217EB65B8772C	FASTA	381	42,974
	10 20 30 40 50 60 MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG FTLDDVIQTG 70 80 90 100 110 120 VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY KPTDKHKTDL NQDNLKGGDD 130 140 150 160 170 180 LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE RRLVEKLCIE GLATLTGEFQ GKYYPLSTMS 190 200 210 220 230 240 DAEQQQLIDD HFLFDKPISP LLLASGMARD WPDGRGIWHN NDKSFLVWVN EEDHLRVISM 250 260 270 280 290 300 QKGGNMKEVF RRFCVGLKKI EEIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP 310 320 330 340 350 360 HLCKHEKFSE VLKRTRLQKR GTGGVDTEAV GSIYDISNAD RLGFSEVEQV QMVVDGVKLM 370 380 VEMEKRLENG KSIDDLIPAQ K

References

[1]

"Complete nucleotide sequence of Torpedo marmorata mRNA coding for the 43,000-dalton nu 2 protein: muscle-specific creatine kinase." Giraudat J., Devillers-Thiery A., Perriard J.-C., Changeux J.-P. Proc. Natl. Acad. Sci. U.S.A. 81:7313-7317(1984) [PubMed: 6095285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Electric organ.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M11508 mRNA. Translation: AAA49277.1.
PIR	KIRYCM. A00676.
3D structure databases
HSSP	HSSP built from PDB template 1N16 based on UniProtKB P04414.
SMR	P00566. Positions 2-381.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00566.
Enzyme and pathway databases
BRENDA	2.7.3.2. 39087.
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_TORMA

Accession

Primary (citable) accession number: P00566

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)