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P01263

- CALC1_ONCKE

UniProt

P01263 - CALC1_ONCKE

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 2525
Add
BLAST
Propeptidei26 – 8055
PRO_0000004077Add
BLAST
Peptidei83 – 11432Calcitonin-1
PRO_0000004078Add
BLAST
Propeptidei119 – 13618
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP01263.

Family & Domainsi

Sequence similaritiesi

Belongs to the calcitonin family.

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: June 11, 2014
This is version 89 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

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