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P62152

- CALM_DROME

UniProt

P62152 - CALM_DROME

Protein

Calmodulin

Gene

Cam

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei116 – 1161Not N6-methylated

    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: FlyBase
    2. calmodulin binding Source: FlyBase
    3. myosin heavy chain binding Source: FlyBase
    4. myosin V binding Source: FlyBase
    5. myosin VI head/neck binding Source: FlyBase
    6. protein binding Source: FlyBase

    GO - Biological processi

    1. actin filament-based movement Source: FlyBase
    2. adaptation of rhodopsin mediated signaling Source: FlyBase
    3. centriole replication Source: FlyBase
    4. deactivation of rhodopsin mediated signaling Source: FlyBase
    5. kinetochore organization Source: FlyBase
    6. lateral inhibition Source: FlyBase
    7. metarhodopsin inactivation Source: FlyBase
    8. mitotic spindle organization Source: FlyBase
    9. muscle cell cellular homeostasis Source: FlyBase
    10. photoreceptor cell axon guidance Source: FlyBase
    11. positive regulation of NFAT protein import into nucleus Source: FlyBase
    12. protein phosphorylation Source: FlyBase
    13. regulation of light-activated channel activity Source: FlyBase
    14. regulation of response to DNA damage stimulus Source: FlyBase
    15. rhabdomere development Source: FlyBase
    16. rhodopsin mediated signaling pathway Source: FlyBase
    17. sensory perception of sound Source: FlyBase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_180317. CREB phosphorylation through the activation of CaMKII.
    REACT_180765. Synthesis of IP3 and IP4 in the cytosol.
    REACT_180852. Translocation of GLUT4 to the plasma membrane.
    REACT_181514. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_184321. Ca2+ pathway.
    REACT_203584. FCERI mediated Ca+2 mobilization.
    REACT_209150. Calmodulin induced events.
    REACT_211028. Smooth Muscle Contraction.
    REACT_213958. DARPP-32 events.
    REACT_224224. Glycogen breakdown (glycogenolysis).
    REACT_226300. CaM pathway.
    REACT_227109. Inactivation, recovery and regulation of the phototransduction cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calmodulin
    Short name:
    CaM
    Gene namesi
    Name:Cam
    ORF Names:CG8472
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0000253. Cam.

    Subcellular locationi

    GO - Cellular componenti

    1. centriole Source: FlyBase
    2. cytoplasm Source: FlyBase
    3. microtubule associated complex Source: FlyBase
    4. midbody Source: FlyBase
    5. myosin V complex Source: FlyBase
    6. myosin VI complex Source: FlyBase
    7. rhabdomere Source: FlyBase
    8. spindle Source: FlyBase
    9. spindle pole Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 149148CalmodulinPRO_0000198278Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei95 – 951N6,N6,N6-trimethyllysine1 Publication

    Post-translational modificationi

    Trimethylation of Lys-116 observed in other calmodulins is absent here, but does occur at Lys-95 specifically in the compound eye.

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    PaxDbiP62152.
    PRIDEiP62152.

    Expressioni

    Gene expression databases

    BgeeiP62152.

    Interactioni

    Protein-protein interaction databases

    BioGridi62106. 28 interactions.
    DIPiDIP-42091N.
    IntActiP62152. 6 interactions.
    MINTiMINT-279657.

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2014
    Beta strandi25 – 284
    Helixi30 – 3910
    Helixi46 – 5611
    Beta strandi61 – 655
    Helixi66 – 7914
    Helixi82 – 9312
    Turni94 – 963
    Beta strandi98 – 1014
    Helixi103 – 11210
    Helixi119 – 12911
    Beta strandi133 – 1386
    Helixi139 – 1479

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MXEX-ray1.70A/B2-149[»]
    2BBMNMR-A2-149[»]
    2BBNNMR-A2-149[»]
    2BKHX-ray2.40B2-148[»]
    2VASX-ray2.40B1-149[»]
    2X51X-ray2.20B1-149[»]
    3GN4X-ray2.70B/D/F/H1-149[»]
    3L9IX-ray2.20C1-149[»]
    4ANJX-ray2.60B1-149[»]
    4CLNX-ray2.20A2-149[»]
    4DBPX-ray2.20C1-149[»]
    4DBQX-ray2.60B1-149[»]
    DisProtiDP00344.
    ProteinModelPortaliP62152.
    SMRiP62152. Positions 5-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62152.

    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

    eggNOGiCOG5126.
    GeneTreeiENSGT00690000101867.
    InParanoidiP62152.
    KOiK02183.
    OMAiSKECILE.
    OrthoDBiEOG7F7WBV.
    PhylomeDBiP62152.

    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.

    P62152-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ    50
    DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGF 100
    ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVTMMTSK 149
    Length:149
    Mass (Da):16,811
    Last modified:January 23, 2007 - v2
    Checksum:i6B44A8917FC7027B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00133 mRNA. Translation: CAA68327.1.
    X05948 Genomic DNA. Translation: CAA29380.1.
    X05949 Genomic DNA. Translation: CAA29381.1.
    X05950 Genomic DNA. Translation: CAB51566.1.
    X05951 Genomic DNA. Translation: CAA29383.1.
    AE013599 Genomic DNA. Translation: AAF58542.1.
    AE013599 Genomic DNA. Translation: AAF58543.1.
    AY118890 mRNA. Translation: AAM50750.1.
    BT003282 mRNA. Translation: AAO25039.1.
    PIRiS01173. MCFF.
    RefSeqiNP_001246276.1. NM_001259347.2.
    NP_001246277.1. NM_001259348.2.
    NP_523710.1. NM_078986.3.
    NP_725120.1. NM_165870.1.
    UniGeneiDm.577.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088001; FBpp0087109; FBgn0000253.
    FBtr0088002; FBpp0087110; FBgn0000253.
    FBtr0304963; FBpp0293502; FBgn0000253.
    FBtr0304964; FBpp0293503; FBgn0000253.
    GeneIDi36329.
    KEGGidme:Dmel_CG8472.
    UCSCiCG8472-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00133 mRNA. Translation: CAA68327.1 .
    X05948 Genomic DNA. Translation: CAA29380.1 .
    X05949 Genomic DNA. Translation: CAA29381.1 .
    X05950 Genomic DNA. Translation: CAB51566.1 .
    X05951 Genomic DNA. Translation: CAA29383.1 .
    AE013599 Genomic DNA. Translation: AAF58542.1 .
    AE013599 Genomic DNA. Translation: AAF58543.1 .
    AY118890 mRNA. Translation: AAM50750.1 .
    BT003282 mRNA. Translation: AAO25039.1 .
    PIRi S01173. MCFF.
    RefSeqi NP_001246276.1. NM_001259347.2.
    NP_001246277.1. NM_001259348.2.
    NP_523710.1. NM_078986.3.
    NP_725120.1. NM_165870.1.
    UniGenei Dm.577.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MXE X-ray 1.70 A/B 2-149 [» ]
    2BBM NMR - A 2-149 [» ]
    2BBN NMR - A 2-149 [» ]
    2BKH X-ray 2.40 B 2-148 [» ]
    2VAS X-ray 2.40 B 1-149 [» ]
    2X51 X-ray 2.20 B 1-149 [» ]
    3GN4 X-ray 2.70 B/D/F/H 1-149 [» ]
    3L9I X-ray 2.20 C 1-149 [» ]
    4ANJ X-ray 2.60 B 1-149 [» ]
    4CLN X-ray 2.20 A 2-149 [» ]
    4DBP X-ray 2.20 C 1-149 [» ]
    4DBQ X-ray 2.60 B 1-149 [» ]
    DisProti DP00344.
    ProteinModelPortali P62152.
    SMRi P62152. Positions 5-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62106. 28 interactions.
    DIPi DIP-42091N.
    IntActi P62152. 6 interactions.
    MINTi MINT-279657.

    Proteomic databases

    PaxDbi P62152.
    PRIDEi P62152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088001 ; FBpp0087109 ; FBgn0000253 .
    FBtr0088002 ; FBpp0087110 ; FBgn0000253 .
    FBtr0304963 ; FBpp0293502 ; FBgn0000253 .
    FBtr0304964 ; FBpp0293503 ; FBgn0000253 .
    GeneIDi 36329.
    KEGGi dme:Dmel_CG8472.
    UCSCi CG8472-RA. d. melanogaster.

    Organism-specific databases

    CTDi 36329.
    FlyBasei FBgn0000253. Cam.

    Phylogenomic databases

    eggNOGi COG5126.
    GeneTreei ENSGT00690000101867.
    InParanoidi P62152.
    KOi K02183.
    OMAi SKECILE.
    OrthoDBi EOG7F7WBV.
    PhylomeDBi P62152.

    Enzyme and pathway databases

    Reactomei REACT_180317. CREB phosphorylation through the activation of CaMKII.
    REACT_180765. Synthesis of IP3 and IP4 in the cytosol.
    REACT_180852. Translocation of GLUT4 to the plasma membrane.
    REACT_181514. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_184321. Ca2+ pathway.
    REACT_203584. FCERI mediated Ca+2 mobilization.
    REACT_209150. Calmodulin induced events.
    REACT_211028. Smooth Muscle Contraction.
    REACT_213958. DARPP-32 events.
    REACT_224224. Glycogen breakdown (glycogenolysis).
    REACT_226300. CaM pathway.
    REACT_227109. Inactivation, recovery and regulation of the phototransduction cascade.

    Miscellaneous databases

    ChiTaRSi Cam. drosophila.
    EvolutionaryTracei P62152.
    GenomeRNAii 36329.
    NextBioi 797939.

    Gene expression databases

    Bgeei P62152.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Canton-S and Oregon-R.
      Tissue: Embryo.
    2. "Structure and sequence of the Drosophila melanogaster calmodulin gene."
      Smith V.L., Doyle K.E., Maune J.F., Munjaal R.P., Beckingham K.
      J. Mol. Biol. 196:471-485(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Drosophila melanogaster contains a single calmodulin gene. Further structure and expression studies."
      Doyle K.E., Kovalick G.E., Lee E., Beckingham K.
      J. Mol. Biol. 213:599-605(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    8. "The calmodulin gene of Drosophila melanogaster."
      Beckingham K., Doyle K.E., Maune J.F.
      Methods Enzymol. 139:230-247(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-141.
    9. "Characterisation of calmodulin from Drosophila heads."
      Gorlach M., Dieter P., Seydewitz H.H., Kaiser C., Witt I., Marme D.
      Biochim. Biophys. Acta 832:228-232(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: AMINO-ACID COMPOSITION.
    10. "Novel eye-specific calmodulin methylation characterized by protein mapping in Drosophila melanogaster."
      Takemori N., Komori N., Thompson J.N. Jr., Yamamoto M.T., Matsumoto H.
      Proteomics 7:2651-2658(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-95.
      Tissue: Eye.
    11. "Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy."
      Ikura M., Spera S., Barbato G., Kay L.E., Krinks M., Bax A.
      Biochemistry 30:9216-9228(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    12. "Solution structure of a calmodulin-target peptide complex by multidimensional NMR."
      Ikura M., Clore G.M., Gronenborn A.M., Zhu G., Klee C.B., Bax A.
      Science 256:632-638(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 7-147 IN INTERACTION WITH MYLK2.
    13. "Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution."
      Taylor D.A., Sack J.S., Maune J.F., Beckingham K., Quiocho F.A.
      J. Biol. Chem. 266:21375-21380(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    14. "Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism."
      Clapperton J.A., Martin S.R., Smerdon S.J., Gamblin S.J., Bayley P.M.
      Biochemistry 41:14669-14679(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

    Entry informationi

    Entry nameiCALM_DROME
    AccessioniPrimary (citable) accession number: P62152
    Secondary accession number(s): P07181, Q9V3T4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    This protein has four functional calcium-binding sites.
    Two alternative gene models exist that generate identical translations.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3