Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25809

- KCRU_RAT

UniProt

P25809 - KCRU_RAT

Protein

Creatine kinase U-type, mitochondrial

Gene

Ckmt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei225 – 2251ATPPROSITE-ProRule annotation
    Binding sitei270 – 2701ATPPROSITE-ProRule annotation
    Binding sitei326 – 3261ATPPROSITE-ProRule annotation
    Binding sitei369 – 3691ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi162 – 1665ATPPROSITE-ProRule annotation
    Nucleotide bindingi354 – 3596ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. phosphocreatine biosynthetic process Source: RGD

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase U-type, mitochondrial (EC:2.7.3.2)
    Alternative name(s):
    Acidic-type mitochondrial creatine kinase
    Short name:
    Mia-CK
    Ubiquitous mitochondrial creatine kinase
    Short name:
    U-MtCK
    Gene namesi
    Name:Ckmt1
    Synonyms:Ckmt
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi61976. Ckmt1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB-SubCell
    2. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939Mitochondrion1 PublicationAdd
    BLAST
    Chaini40 – 418379Creatine kinase U-type, mitochondrialPRO_0000016592Add
    BLAST

    Proteomic databases

    PaxDbiP25809.
    PRIDEiP25809.

    2D gel databases

    World-2DPAGE0004:P25809.

    PTM databases

    PhosphoSiteiP25809.

    Expressioni

    Tissue specificityi

    In many tissues, with highest levels in brain gut and kidney. In the kidney localized primarily in the outer medulla in the thick ascending limb and distal convoluted tubule.1 Publication

    Gene expression databases

    GenevestigatoriP25809.

    Interactioni

    Subunit structurei

    Exists as an octamer composed of four MTCK homodimers.

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000044253.

    Structurei

    3D structure databases

    ProteinModelPortaliP25809.
    SMRiP25809. Positions 40-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 13287Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 401243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 6425Cardiolipin-bindingBy similarityAdd
    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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG3869.
    HOGENOMiHOG000232165.
    HOVERGENiHBG001339.
    InParanoidiP25809.
    PhylomeDBiP25809.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P25809-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGPFSRLLS ARPGLKLLAL AGAGSLAAGI LLRPESVRAA TGERRRLYPP    50
    SAEYPDLRKH NNCMASHLTP AVYARLCDKT TPTGWTLDQC IQTGVDNPGH 100
    PFIKTVGMVA GDEETYEVFA ELFDPVIQER HNGYDPRTMK HTTDLDASKI 150
    RSGYFDERYV LSSRVRTGRS IRGLSLPPAC TRAERREVER VVVDALSGLK 200
    GDLAGRYYRL SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG MARDWPDARG 250
    IWHNNEKSFL IWVNEEDHTR VISMEKGGNM KRVFERFCRG LKKVEKLIQE 300
    RGWEFMWNER LGYILTCPSN LGTGLRAGVH VKLPLLSKDS RFPKILENLR 350
    LQKRGTGGVD TPATADVFDI SNLDRLGKSE VELVQLVIDG VNYLIDCERR 400
    LEKGQDIRIP PPLVHGKH 418
    Length:418
    Mass (Da):47,029
    Last modified:May 1, 1992 - v1
    Checksum:i468339C52E4232D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59737 mRNA. Translation: CAA42415.1.
    PIRiS17189.
    UniGeneiRn.155589.

    Genome annotation databases

    UCSCiRGD:61976. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59737 mRNA. Translation: CAA42415.1 .
    PIRi S17189.
    UniGenei Rn.155589.

    3D structure databases

    ProteinModelPortali P25809.
    SMRi P25809. Positions 40-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000044253.

    PTM databases

    PhosphoSitei P25809.

    2D gel databases

    World-2DPAGE 0004:P25809.

    Proteomic databases

    PaxDbi P25809.
    PRIDEi P25809.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:61976. rat.

    Organism-specific databases

    RGDi 61976. Ckmt1.

    Phylogenomic databases

    eggNOGi COG3869.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi P25809.
    PhylomeDBi P25809.

    Gene expression databases

    Genevestigatori P25809.

    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. "Structural characterization and tissue-specific expression of the mRNAs encoding isoenzymes from two rat mitochondrial creatine kinase genes."
      Payne R.M., Haas R.C., Strauss A.W.
      Biochim. Biophys. Acta 1089:352-361(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Intestine.
    2. "Compartmentation of multiple forms of creatine kinase in the distal nephron of the rat kidney."
      Friedman D.L., Perryman M.B.
      J. Biol. Chem. 266:22404-22410(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 40-56, TISSUE SPECIFICITY.
    3. Lubec G., Afjehi-Sadat L., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 152-158; 191-200; 258-270 AND 311-326, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.

    Entry informationi

    Entry nameiKCRU_RAT
    AccessioniPrimary (citable) accession number: P25809
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mitochondrial creatine kinase binds cardiolipin.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3