P01263 (CALC1_ONCKE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Calcitonin-1
Organism	Oncorhynchus keta (Chum salmon) (Salmo keta)
Taxonomic identifier	8018 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Actinopterygii › Actinopteri › Neopterygii › Teleostei › Elopocephala › Clupeocephala › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonoidei › Salmonidae › Salmoninae › Oncorhynchus

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subcellular location	Secreted.
Pharmaceutical use	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.
Sequence similarities	Belongs to the calcitonin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Amidation Cleavage on pair of basic residues Disulfide bond
Technical term	3D-structure Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological_process	activation of adenylate cyclase activity Inferred from direct assay PubMed 12704735. Source: MGI elevation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Inferred from direct assay PubMed 8078488. Source: UniProtKB sperm capacitation Inferred from direct assay PubMed 12704735. Source: MGI
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Propeptide

26 – 80

55

PRO_0000004077

Peptide

83 – 114

32

Calcitonin-1

PRO_0000004078

Propeptide

119 – 136

18

PRO_0000004079

Amino acid modifications

Modified residue

114

1

Proline amide

Disulfide bond

83 ↔ 89

Secondary structure

1

.

.

.

136

Helix Strand Turn

Details...

Helix

86 – 110

25

Sequences

	Sequence		Length	Mass (Da)
	P01263 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: BDD8867AE113B2A8	FASTA	136	15,179
	10 20 30 40 50 60 MVMMKLSALL IAYFLVICQM YSSHAAPART GLESMTDQVT LTDYEARRLL NAIVKEFVQM 70 80 90 100 110 120 TSEELEQQAN EGNSLDRPMS KRCSNLSTCV LGKLSQELHK LQTYPRTNTG SGTPGKKRSL 130 PESNRYASYG DSYDGI

References

[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]	"Amino acid sequence of salmon ultimobranchial calcitonin." Niall H.D., Keutmann H.T., Copp D.H., Potts J.T. Jr. Proc. Natl. Acad. Sci. U.S.A. 64:771-778(1969) [PubMed] [Europe PMC] [Abstract] 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]	"Solution structure of salmon calcitonin." Meyer J.-P., Pelton J.T., Hoflack J., Saudek V. Biopolymers 31:233-241(1991) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00765 mRNA. Translation: CAA68734.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GLG	NMR	-	A	83-114	[»]
2GLH	NMR	-	A	83-114	[»]

ProteinModelPortal

P01263.

SMR

P01263. Positions 83-114.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG031362.

Family and domain databases

InterPro

IPR018360. Calcitonin_CS.
IPR001693. Calcitonin_peptide-like.
IPR021117. Procalcitonin-like.
IPR021116. Procalcitonin/adrenomedullin.
IPR021118. Procalcitonin_A-typ.
[Graphical view]

PANTHER

PTHR10505. PTHR10505. 1 hit.
PTHR10505:SF3. PTHR10505:SF3. 1 hit.

Pfam

PF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]

PRINTS

PR00270. CALCITONINA.

SMART

SM00113. CALCITONIN. 1 hit.
[Graphical view]

PROSITE

PS00258. CALCITONIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00017. Salmon Calcitonin.

EvolutionaryTrace

P01263.

Entry information

Entry name

CALC1_ONCKE

Accession

Primary (citable) accession number: P01263

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program