ID   CALC_ANGJA              Reviewed;          32 AA.
AC   P01262;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Calcitonin;
OS   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT PRO-32.
RA   Noda T., Narita K.;
RT   "Amino acid sequence of eel calcitonin.";
RL   J. Biochem. 79:353-359(1976).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=10387083; DOI=10.1021/bi983018j;
RA   Hashimoto Y., Toma K., Nishikido J., Yamamoto K., Haneda K., Inazu T.,
RA   Valentine K.G., Opella S.J.;
RT   "Effects of glycosylation on the structure and dynamics of eel calcitonin
RT   in micelles and lipid bilayers determined by nuclear magnetic resonance
RT   spectroscopy.";
RL   Biochemistry 38:8377-8384(1999).
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   -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR   PIR; A01529; TCEE.
DR   PDB; 1BKU; NMR; -; A=1-32.
DR   PDB; 1BYV; NMR; -; A=1-32.
DR   PDB; 1BZB; NMR; -; A=1-32.
DR   PDBsum; 1BKU; -.
DR   PDBsum; 1BYV; -.
DR   PDBsum; 1BZB; -.
DR   AlphaFoldDB; P01262; -.
DR   BMRB; P01262; -.
DR   SMR; P01262; -.
DR   EvolutionaryTrace; P01262; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond;
KW   Hormone; Secreted.
FT   PEPTIDE         1..32
FT                   /note="Calcitonin"
FT                   /id="PRO_0000044669"
FT   MOD_RES         32
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|Ref.1"
FT   DISULFID        1..7
FT   HELIX           5..19
FT                   /evidence="ECO:0007829|PDB:1BKU"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:1BKU"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:1BYV"
SQ   SEQUENCE   32 AA;  3418 MW;  AFC93549F8048922 CRC64;
     CSNLSTCVLG KLSQELHKLQ TYPRTDVGAG TP