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P62155

- CALM_XENLA

UniProt

P62155 - CALM_XENLA

Protein

Calmodulin

Gene

calm1

more
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi21 – 32121Add
    BLAST
    Calcium bindingi57 – 68122Add
    BLAST
    Calcium bindingi94 – 105123Add
    BLAST
    Calcium bindingi130 – 141124Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct
    3. receptor binding Source: BHF-UCL

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calmodulin
    Short name:
    CaM
    Gene namesi
    Name:calm1
    AND
    Name:calm2
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-976648. calm1.
    XB-GENE-1014645. calm2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 149148CalmodulinPRO_0000198242Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei116 – 1161N6,N6,N6-trimethyllysineBy similarity

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    PRIDEiP62155.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    cyaP401362EBI-397568,EBI-457011From a different organism.

    Protein-protein interaction databases

    IntActiP62155. 3 interactions.
    MINTiMINT-7032991.

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2014
    Beta strandi22 – 243
    Beta strandi25 – 284
    Helixi30 – 3910
    Helixi46 – 5611
    Beta strandi58 – 603
    Beta strandi61 – 655
    Helixi66 – 7611
    Beta strandi77 – 815
    Helixi84 – 9310
    Turni95 – 973
    Beta strandi98 – 1014
    Helixi103 – 11210
    Helixi119 – 12911
    Beta strandi134 – 1385
    Helixi139 – 1468

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CFCNMR-A2-149[»]
    1CFDNMR-A2-149[»]
    1CFFNMR-A2-149[»]
    1CKKNMR-A2-149[»]
    1DMONMR-A2-149[»]
    1F70NMR-A2-77[»]
    1F71NMR-A83-149[»]
    1IQ5X-ray1.80A1-149[»]
    1MUXNMR-A2-149[»]
    1NWDNMR-A2-149[»]
    1SY9NMR-A2-149[»]
    1X02NMR-A2-149[»]
    1Y0VX-ray3.60H/I/J/K/L/M6-149[»]
    2COLX-ray2.20B80-146[»]
    2K3SNMR-B83-149[»]
    2KDUNMR-A2-149[»]
    2LLONMR-A2-81[»]
    2LLQNMR-A83-149[»]
    2RRTNMR-A79-149[»]
    ProteinModelPortaliP62155.
    SMRiP62155. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62155.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 4336EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini44 – 7936EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini81 – 11636EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini117 – 14933EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the calmodulin family.Curated
    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOVERGENiHBG012180.
    KOiK02183.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 2 hits.
    [Graphical view]
    SMARTiSM00054. EFh. 4 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 4 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62155-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ    50
    DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY 100
    ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK 149
    Length:149
    Mass (Da):16,838
    Last modified:January 23, 2007 - v2
    Checksum:i6B4BC3FCDE10727B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01944 mRNA. Translation: AAA49668.1.
    K01945 mRNA. Translation: AAA49669.1.
    BC054973 mRNA. Translation: AAH54973.1.
    BC072232 mRNA. Translation: AAH72232.1.
    BC094079 mRNA. Translation: AAH94079.1.
    PIRiI51402.
    RefSeqiNP_001080864.1. NM_001087395.1.
    NP_001084025.1. NM_001090556.1.
    NP_001089059.1. NM_001095590.1.
    UniGeneiXl.54061.
    Xl.543.
    Xl.54419.

    Genome annotation databases

    GeneIDi380558.
    399259.
    606721.
    KEGGixla:380558.
    xla:399259.
    xla:606721.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01944 mRNA. Translation: AAA49668.1 .
    K01945 mRNA. Translation: AAA49669.1 .
    BC054973 mRNA. Translation: AAH54973.1 .
    BC072232 mRNA. Translation: AAH72232.1 .
    BC094079 mRNA. Translation: AAH94079.1 .
    PIRi I51402.
    RefSeqi NP_001080864.1. NM_001087395.1.
    NP_001084025.1. NM_001090556.1.
    NP_001089059.1. NM_001095590.1.
    UniGenei Xl.54061.
    Xl.543.
    Xl.54419.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CFC NMR - A 2-149 [» ]
    1CFD NMR - A 2-149 [» ]
    1CFF NMR - A 2-149 [» ]
    1CKK NMR - A 2-149 [» ]
    1DMO NMR - A 2-149 [» ]
    1F70 NMR - A 2-77 [» ]
    1F71 NMR - A 83-149 [» ]
    1IQ5 X-ray 1.80 A 1-149 [» ]
    1MUX NMR - A 2-149 [» ]
    1NWD NMR - A 2-149 [» ]
    1SY9 NMR - A 2-149 [» ]
    1X02 NMR - A 2-149 [» ]
    1Y0V X-ray 3.60 H/I/J/K/L/M 6-149 [» ]
    2COL X-ray 2.20 B 80-146 [» ]
    2K3S NMR - B 83-149 [» ]
    2KDU NMR - A 2-149 [» ]
    2LLO NMR - A 2-81 [» ]
    2LLQ NMR - A 83-149 [» ]
    2RRT NMR - A 79-149 [» ]
    ProteinModelPortali P62155.
    SMRi P62155. Positions 1-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P62155. 3 interactions.
    MINTi MINT-7032991.

    Chemistry

    BindingDBi P62155.

    Proteomic databases

    PRIDEi P62155.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 380558.
    399259.
    606721.
    KEGGi xla:380558.
    xla:399259.
    xla:606721.

    Organism-specific databases

    CTDi 801.
    805.
    Xenbasei XB-GENE-976648. calm1.
    XB-GENE-1014645. calm2.

    Phylogenomic databases

    HOVERGENi HBG012180.
    KOi K02183.

    Miscellaneous databases

    EvolutionaryTracei P62155.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 2 hits.
    [Graphical view ]
    SMARTi SM00054. EFh. 4 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 4 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of calmodulin genes from Xenopus laevis."
      Chien Y.-H., Dawid I.B.
      Mol. Cell. Biol. 4:507-513(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM1 AND CALM2).
      Tissue: Embryo and Kidney.
    3. Cited for: STRUCTURE BY NMR.
    4. "Calcium-induced conformational transition revealed by the solution structure of apo calmodulin."
      Zhang M., Tanaka T., Ikura M.
      Nat. Struct. Biol. 2:758-767(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    5. "Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition."
      Osawa M., Swindells M.B., Tanikawa J., Tanaka T., Mase T., Furuya T., Ikura M.
      J. Mol. Biol. 276:165-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    6. "NMR solution structure of a complex of calmodulin with a binding peptide of the Ca(2+) pump."
      Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M., Schulte P., Schwalbe H., Griesinger C., Krebs J., Schmid H., Vorherr T.E., Carafoli E.
      Biochemistry 38:12320-12332(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    7. "A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase."
      Osawa M., Tokumitsu H., Swindells M.B., Kurihara H., Orita M., Shibanuma T., Furuya T., Ikura M.
      Nat. Struct. Biol. 6:819-824(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    8. "Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings."
      Chou J.J., Li S., Bax A.
      J. Biomol. NMR 18:217-227(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-77 AND 83-149.
    9. "Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin."
      Yap K.L., Yuan T., Mal T.K., Vogel H.J., Ikura M.
      J. Mol. Biol. 328:193-204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    10. "Solution structure of magnesium-bound form of calmodulin C-domain E104D/E140D Mutant."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 79-149.

    Entry informationi

    Entry nameiCALM_XENLA
    AccessioniPrimary (citable) accession number: P62155
    Secondary accession number(s): P02593
    , P70667, P99014, Q61379, Q61380, Q6INP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein has four functional calcium-binding sites.

    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