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P04414

- KCRM_TORCA

UniProt

P04414 - KCRM_TORCA

Protein

Creatine kinase M-type

Gene
N/A
Organism
Torpedo californica (Pacific electric ray)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + creatine = ADP + phosphocreatine.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei191 – 1911ATPPROSITE-ProRule annotation
    Binding sitei236 – 2361ATPPROSITE-ProRule annotation
    Binding sitei292 – 2921ATP
    Binding sitei335 – 3351ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi128 – 1325ATP
    Nucleotide bindingi320 – 3256ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. creatine kinase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase M-type (EC:2.7.3.2)
    Alternative name(s):
    Creatine kinase M chain
    M-CK
    OrganismiTorpedo californica (Pacific electric ray)
    Taxonomic identifieri7787 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 381381Creatine kinase M-typePRO_0000211981Add
    BLAST

    Miscellaneous databases

    PMAP-CutDBP04414.

    Interactioni

    Subunit structurei

    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.1 Publication

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 194
    Helixi29 – 335
    Helixi36 – 427
    Helixi53 – 6210
    Beta strandi67 – 693
    Helixi81 – 844
    Helixi86 – 9611
    Helixi112 – 1143
    Turni123 – 1253
    Beta strandi126 – 13510
    Turni143 – 1453
    Helixi148 – 16215
    Helixi167 – 1693
    Beta strandi171 – 1755
    Helixi176 – 1783
    Helixi181 – 1899
    Helixi200 – 2034
    Turni204 – 21411
    Beta strandi216 – 2205
    Beta strandi223 – 24422
    Helixi246 – 26621
    Turni275 – 2773
    Helixi284 – 2863
    Beta strandi292 – 2987
    Helixi302 – 3043
    Helixi308 – 3158
    Beta strandi317 – 3215
    Beta strandi324 – 3296
    Beta strandi333 – 3386
    Beta strandi342 – 3443
    Helixi346 – 36823
    Helixi374 – 3763

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VRPX-ray2.10A/B1-381[»]
    ProteinModelPortaliP04414.
    SMRiP04414. Positions 8-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04414.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 9888Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini125 – 367243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase N-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG001339.

    Family and domain databases

    Gene3Di1.10.135.10. 1 hit.
    3.30.590.10. 1 hit.
    InterProiIPR022415. ATP-guanido_PTrfase_AS.
    IPR022414. ATP-guanido_PTrfase_cat.
    IPR022413. ATP-guanido_PTrfase_N.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    [Graphical view]
    PfamiPF00217. ATP-gua_Ptrans. 1 hit.
    PF02807. ATP-gua_PtransN. 1 hit.
    [Graphical view]
    SUPFAMiSSF48034. SSF48034. 1 hit.
    PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
    PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
    PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04414-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG    50
    FTLDDIIQTG VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY 100
    KPTDKHKTDL NQENLKGGDD LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE 150
    RRLVEKLCID GLATLTGEFQ GKYYPLSSMS DAEQQQLIDD HFLFDKPISP 200
    LLLASGMARD WPDGRGIWHN NDKTFLVWVN EEDHLRVISM QKGGNMKEVF 250
    RRFCVGLKKI EDIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP 300
    HLCKHEKFSE VLKRTRLQKR GTGGVDTAAV GSIYDISNAD RLGFSEVEQV 350
    QMVVDGVKLM VEMEKRLENG KSIDDLMPAQ K 381
    Length:381
    Mass (Da):42,934
    Last modified:August 13, 1987 - v1
    Checksum:iDF4A54FDDF3BD570
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36427 mRNA. Translation: AAA49278.1.
    PIRiA00677. KIRYCT.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36427 mRNA. Translation: AAA49278.1 .
    PIRi A00677. KIRYCT.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VRP X-ray 2.10 A/B 1-381 [» ]
    ProteinModelPortali P04414.
    SMRi P04414. Positions 8-381.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG001339.

    Miscellaneous databases

    EvolutionaryTracei P04414.
    PMAP-CutDB P04414.

    Family and domain databases

    Gene3Di 1.10.135.10. 1 hit.
    3.30.590.10. 1 hit.
    InterProi IPR022415. ATP-guanido_PTrfase_AS.
    IPR022414. ATP-guanido_PTrfase_cat.
    IPR022413. ATP-guanido_PTrfase_N.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    [Graphical view ]
    Pfami PF00217. ATP-gua_Ptrans. 1 hit.
    PF02807. ATP-gua_PtransN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48034. SSF48034. 1 hit.
    PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
    PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
    PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiKCRM_TORCA
    AccessioniPrimary (citable) accession number: P04414
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3