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Protein

Calcitonin-1

Gene
N/A
Organism
Oncorhynchus keta (Chum salmon) (Salmo keta)
Status
Reviewed-Annotation score: Annotation score: 4 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 – 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 – 11025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MVMMKLSALL IAYFLVICQM YSSHAAPART GLESMTDQVT LTDYEARRLL
60 70 80 90 100
NAIVKEFVQM TSEELEQQAN EGNSLDRPMS KRCSNLSTCV LGKLSQELHK
110 120 130
LQTYPRTNTG SGTPGKKRSL PESNRYASYG DSYDGI
Length:136
Mass (Da):15,179
Last modified:August 1, 1988 - v1
Checksum:iBDD8867AE113B2A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00765 mRNA. Translation: CAA68734.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00765 mRNA. Translation: CAA68734.1.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG031362.

Miscellaneous databases

EvolutionaryTraceiP01263.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 93 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.