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P04414 (KCRM_TORCA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase M-type

EC=2.7.3.2
Alternative name(s):
Creatine kinase M chain
M-CK
OrganismTorpedo californica (Pacific electric ray)
Taxonomic identifier7787 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

creatine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Creatine kinase M-type
PRO_0000211981

Regions

Domain11 – 9888Phosphagen kinase N-terminal
Domain125 – 367243Phosphagen kinase C-terminal
Nucleotide binding128 – 1325ATP
Nucleotide binding320 – 3256ATP

Sites

Binding site1911ATP By similarity
Binding site2361ATP By similarity
Binding site2921ATP
Binding site3351ATP

Secondary structure

.............................................................. 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04414 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: DF4A54FDDF3BD570

FASTA38142,934
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36427 mRNA. Translation: AAA49278.1.
PIRKIRYCT. A00677.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VRPX-ray2.10A/B1-381[»]
ProteinModelPortalP04414.
SMRP04414. Positions 8-381.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001339.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. SSF48034. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04414.
PMAP-CutDBP04414.

Entry information

Entry nameKCRM_TORCA
AccessionPrimary (citable) accession number: P04414
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 16, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references