ID   CALC1_ONCKE             Reviewed;         136 AA.
AC   P01263;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Calcitonin-1;
DE   Flags: Precursor;
OS   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3691820; DOI=10.1016/0014-5793(87)80558-6;
RA   Poeschl E., Lindley I., Hofer E., Seifert J.M., Brunowsky W., Besemer J.;
RT   "The structure of procalcitonin of the salmon as deduced from its cDNA
RT   sequence.";
RL   FEBS Lett. 226:96-100(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 83-114, AND AMIDATION AT PRO-114.
RX   PubMed=5261048; DOI=10.1073/pnas.64.2.771;
RA   Niall H.D., Keutmann H.T., Copp D.H., Potts J.T. Jr.;
RT   "Amino acid sequence of salmon ultimobranchial calcitonin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 64:771-778(1969).
RN   [3]
RP   SYNTHESIS OF CALCITONIN.
RX   PubMed=5361911; DOI=10.1002/hlca.19690520702;
RA   Guttmann S., Pless J., Huguenin R.L., Sandrin E., Bossert H., Zehnder K.;
RT   "Synthesis of salmon calcitonin, a high activity hypocalcemic hormone.";
RL   Helv. Chim. Acta 52:1789-1795(1969).
RN   [4]
RP   STRUCTURE BY NMR OF CALCITONIN.
RX   PubMed=1991104; DOI=10.1021/bi00219a012;
RA   Meadows R.P., Nikonowicz E.P., Jones C.R., Bastian J.W., Gorenstein D.G.;
RT   "Two-dimensional NMR and structure determination of salmon calcitonin in
RT   methanol.";
RL   Biochemistry 30:1247-1254(1991).
RN   [5]
RP   STRUCTURE BY NMR OF CALCITONIN.
RX   PubMed=2043752; DOI=10.1002/bip.360310210;
RA   Meyer J.-P., Pelton J.T., Hoflack J., Saudek V.;
RT   "Solution structure of salmon calcitonin.";
RL   Biopolymers 31:233-241(1991).
RN   [6]
RP   STRUCTURE BY NMR OF CALCITONIN.
RX   PubMed=1931969; DOI=10.1021/bi00107a012;
RA   Motta A., Pastore A., Goud N.A., Castiglione Morelli M.A.;
RT   "Solution conformation of salmon calcitonin in sodium dodecyl sulfate
RT   micelles as determined by two-dimensional NMR and distance geometry
RT   calculations.";
RL   Biochemistry 30:10444-10450(1991).
CC   -!- FUNCTION: Causes a rapid but short-lived drop in the level of calcium
CC       and phosphate in blood by promoting the incorporation of those ions in
CC       the bones.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PHARMACEUTICAL: Available under the names Calcimar (Rhone-Poulenc
CC       Rorer), Miacalcin (Novartis) or Forcaltonin (Unigene). Used for the
CC       treatment of Paget's disease and hypercalcemia in malignancy.
CC   -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR   EMBL; Y00765; CAA68734.1; -; mRNA.
DR   PDB; 2GLG; NMR; -; A=83-114.
DR   PDB; 2GLH; NMR; -; A=83-114.
DR   PDB; 6PGQ; X-ray; 2.85 A; B=104-114.
DR   PDBsum; 2GLG; -.
DR   PDBsum; 2GLH; -.
DR   PDBsum; 6PGQ; -.
DR   AlphaFoldDB; P01263; -.
DR   BMRB; P01263; -.
DR   SMR; P01263; -.
DR   EvolutionaryTrace; P01263; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031716; F:calcitonin receptor binding; IPI:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:MGI.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IDA:UniProtKB.
DR   GO; GO:0048240; P:sperm capacitation; IDA:MGI.
DR   InterPro; IPR021118; Calcitonin.
DR   InterPro; IPR021117; Calcitonin-like.
DR   InterPro; IPR021116; Calcitonin/adrenomedullin.
DR   InterPro; IPR018360; Calcitonin_CS.
DR   InterPro; IPR001693; Calcitonin_peptide-like.
DR   PANTHER; PTHR10505; PTHR10505; 1.
DR   Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR   PRINTS; PR00270; CALCITONINA.
DR   SMART; SM00113; CALCITONIN; 1.
DR   PROSITE; PS00258; CALCITONIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Hormone; Pharmaceutical;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT   PROPEP          26..80
FT                   /id="PRO_0000004077"
FT   PEPTIDE         83..114
FT                   /note="Calcitonin-1"
FT                   /id="PRO_0000004078"
FT   PROPEP          119..136
FT                   /id="PRO_0000004079"
FT   REGION          101..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         114
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:5261048"
FT   DISULFID        83..89
FT   HELIX           86..110
FT                   /evidence="ECO:0007829|PDB:2GLG"
SQ   SEQUENCE   136 AA;  15179 MW;  BDD8867AE113B2A8 CRC64;
     MVMMKLSALL IAYFLVICQM YSSHAAPART GLESMTDQVT LTDYEARRLL NAIVKEFVQM
     TSEELEQQAN EGNSLDRPMS KRCSNLSTCV LGKLSQELHK LQTYPRTNTG SGTPGKKRSL
     PESNRYASYG DSYDGI