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UniProtKB/Swiss-Prot entry P04414


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KCRM_TORCA
Primary accession number P04414
Secondary accession numbers None
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 59)
Name and origin of the protein
Protein name Creatine kinase M-type
Synonyms EC 2.7.3.2
Creatine kinase M chain
M-CK
Gene name None
From
Torpedo californica (Pacific electric ray) [TaxID: 7787] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea; Torpediniformes; Torpedinoidei; Torpedinidae; Torpedo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Electric organ;
PubMed=6594677 [NCBI, ExPASy, EBI, Israel, Japan]
West B.L., Babbitt P.C., Mendez B., Baxter J.D.;
"Creatine kinase protein sequence encoded by a cDNA made from Torpedo californica electric organ mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 81:7007-7011(1984).
[2]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, AND SUBUNIT.
DOI=10.1021/bi026655p; PubMed=12437342 [NCBI, ExPASy, EBI, Israel, Japan]
Lahiri S.D., Wang P.-F., Babbitt P.C., McLeish M.J., Kenyon G.L., Allen K.N.;
"The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex.";
Biochemistry 41:13861-13867(2002).
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: 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.
  • SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M36427; AAA49278.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00677; KIRYCT.
3D structure databases
PDB
1VRP; X-ray; 2.10 A; A/B=1-381.[ExPASy / RCSB / EBI]
PDBsum 1VRP; -.
ModBase P04414.
Family and domain databases
InterPro IPR000749; ATP-gua_Ptrans.
IPR014746; Gln_synth/guanido_kin_cat.
Graphical view of domain structure.
Gene3D G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
PANTHER PTHR11547; ATP-gua_Ptrans; 1.
Pfam PF00217; ATP-gua_Ptrans; 1.
PF02807; ATP-gua_PtransN; 1.
Pfam graphical view of domain structure.
PROSITE PS00112; GUANIDO_KINASE; 1.
BLOCKS P04414.
Phylogenomic databases
HOVERGEN P04414; -.
Other
ProtoNet P04414.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   381  381     Creatine kinase M-type. PRO_0000211981
NP_BIND   128   132  5     ATP. 
NP_BIND   320   325  6     ATP. 
ACT_SITE   283   283         
BINDING   191   191        ATP (By similarity). 
BINDING   292   292        ATP. 
BINDING   335   335        ATP. 
HELIX   16    19  4      
HELIX   29    33  5      
HELIX   36    42  7      
HELIX   53    62  10      
STRAND   67    69  3      
HELIX   81    84  4      
HELIX   86    96  11      
HELIX   112   114  3      
TURN   123   125  3      
STRAND   126   135  10      
TURN   143   145  3      
HELIX   148   162  15      
HELIX   167   169  3      
STRAND   171   175  5      
HELIX   176   178  3      
HELIX   181   189  9      
HELIX   200   203  4      
TURN   204   214  11      
STRAND   216   220  5      
STRAND   223   244  22      
HELIX   246   266  21      
TURN   275   277  3      
HELIX   284   286  3      
STRAND   292   298  7      
HELIX   302   304  3      
HELIX   308   315  8      
STRAND   317   321  5      
STRAND   324   329  6      
STRAND   333   338  6      
STRAND   342   344  3      
HELIX   346   368  23      
HELIX   374   376  3      
Sequence information
Length: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 42934 Da [This is the MW of the unprocessed precursor] CRC64: DF4A54FDDF3BD570 [This is a checksum on the sequence]
        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 

P04414 in FASTA format

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