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P01263

- CALC1_ONCKE

UniProt

P01263 - CALC1_ONCKE

Protein

Calcitonin-1

Gene
N/A
Organism
Oncorhynchus keta (Chum salmon) (Salmo keta)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.

    GO - Molecular functioni

    1. calcitonin receptor binding Source: UniProtKB

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: MGI
    2. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
    3. sperm capacitation Source: MGI

    Keywords - Molecular functioni

    Hormone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcitonin-1
    OrganismiOncorhynchus keta (Chum salmon) (Salmo keta)
    Taxonomic identifieri8018 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeOncorhynchus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Pharmaceutical usei

    Available under the names Calcimar (Rhone-Poulenc Rorer), Miacalcin (Novartis) or Forcaltonin (Unigene). Used for the treatment of Paget's disease and hypercalcemia in malignancy.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Add
    BLAST
    Propeptidei26 – 8055PRO_0000004077Add
    BLAST
    Peptidei83 – 11432Calcitonin-1PRO_0000004078Add
    BLAST
    Propeptidei119 – 13618PRO_0000004079Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi83 ↔ 89
    Modified residuei114 – 1141Proline amide

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues, Disulfide bond

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi86 – 11025

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GLGNMR-A83-114[»]
    2GLHNMR-A83-114[»]
    ProteinModelPortaliP01263.
    SMRiP01263. Positions 83-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01263.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the calcitonin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG031362.

    Family and domain databases

    InterProiIPR021118. Calcitonin.
    IPR018360. Calcitonin_CS.
    IPR001693. Calcitonin_peptide-like.
    IPR021117. Procalcitonin-like.
    IPR021116. Procalcitonin/adrenomedullin.
    [Graphical view]
    PANTHERiPTHR10505. PTHR10505. 1 hit.
    PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
    [Graphical view]
    PRINTSiPR00270. CALCITONINA.
    SMARTiSM00113. CALCITONIN. 1 hit.
    [Graphical view]
    PROSITEiPS00258. CALCITONIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01263-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVMMKLSALL IAYFLVICQM YSSHAAPART GLESMTDQVT LTDYEARRLL    50
    NAIVKEFVQM TSEELEQQAN EGNSLDRPMS KRCSNLSTCV LGKLSQELHK 100
    LQTYPRTNTG SGTPGKKRSL PESNRYASYG DSYDGI 136
    Length:136
    Mass (Da):15,179
    Last modified:August 1, 1988 - v1
    Checksum:iBDD8867AE113B2A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00765 mRNA. Translation: CAA68734.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00765 mRNA. Translation: CAA68734.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GLG NMR - A 83-114 [» ]
    2GLH NMR - A 83-114 [» ]
    ProteinModelPortali P01263.
    SMRi P01263. Positions 83-114.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00017. Salmon Calcitonin.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG031362.

    Miscellaneous databases

    EvolutionaryTracei P01263.

    Family and domain databases

    InterProi IPR021118. Calcitonin.
    IPR018360. Calcitonin_CS.
    IPR001693. Calcitonin_peptide-like.
    IPR021117. Procalcitonin-like.
    IPR021116. Procalcitonin/adrenomedullin.
    [Graphical view ]
    PANTHERi PTHR10505. PTHR10505. 1 hit.
    Pfami PF00214. Calc_CGRP_IAPP. 1 hit.
    [Graphical view ]
    PRINTSi PR00270. CALCITONINA.
    SMARTi SM00113. CALCITONIN. 1 hit.
    [Graphical view ]
    PROSITEi PS00258. CALCITONIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The structure of procalcitonin of the salmon as deduced from its cDNA sequence."
      Poeschl E., Lindley I., Hofer E., Seifert J.M., Brunowsky W., Besemer J.
      FEBS Lett. 226:96-100(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: PROTEIN SEQUENCE OF 85-116.
    3. "Synthesis of salmon calcitonin, a high activity hypocalcemic hormone."
      Guttmann S., Pless J., Huguenin R.L., Sandrin E., Bossert H., Zehnder K.
      Helv. Chim. Acta 52:1789-1795(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: SYNTHESIS OF CALCITONIN.
    4. "Two-dimensional NMR and structure determination of salmon calcitonin in methanol."
      Meadows R.P., Nikonowicz E.P., Jones C.R., Bastian J.W., Gorenstein D.G.
      Biochemistry 30:1247-1254(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF CALCITONIN.
    5. Cited for: STRUCTURE BY NMR OF CALCITONIN.
    6. "Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations."
      Motta A., Pastore A., Goud N.A., Castiglione Morelli M.A.
      Biochemistry 30:10444-10450(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF CALCITONIN.

    Entry informationi

    Entry nameiCALC1_ONCKE
    AccessioniPrimary (citable) accession number: P01263
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Pharmaceutical

    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