ID   CALC_SHEEP              Reviewed;         143 AA.
AC   P01261;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Calcitonin;
DE   Flags: Precursor;
GN   Name=CALCA; Synonyms=CALC;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=8482543; DOI=10.1016/0378-1119(93)90379-h;
RA   Cumaraswamy A., Borges M., Tamir H., Nelkin B.D.;
RT   "Cloning of a cDNA encoding sheep calcitonin from a thyroid C-cell
RT   library.";
RL   Gene 126:269-273(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 87-118.
RA   Sauer R., Niall H.D., Potts J.T. Jr.;
RT   "Accelerated procedures for automated peptide degradation.";
RL   Fed. Proc. 29:728-728(1970).
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   EMBL; M98053; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; JN0580; TCSH.
DR   AlphaFoldDB; P01261; -.
DR   STRING; 9940.ENSOARP00000006540; -.
DR   eggNOG; ENOG502RZI5; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
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   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hormone; Phosphoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..84
FT                   /id="PRO_0000004068"
FT   PEPTIDE         87..118
FT                   /note="Calcitonin"
FT                   /id="PRO_0000004069"
FT   PROPEP          122..143
FT                   /id="PRO_0000004070"
FT   REGION          62..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01257"
FT   MOD_RES         118
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000250|UniProtKB:P01257"
FT   DISULFID        87..93
SQ   SEQUENCE   143 AA;  15659 MW;  D4CEB15C5C06B663 CRC64;
     MGFGKSSPFL AFSILVLCQA GSLQATPLRS ALETLPDPGA LSEKEGRLLL AALVKAYVQR
     KTNELEQEEE QEETEDSSLD SSRAKRCSNL STCVLSAYWK DLNNYHRYSG MGFGPETPGK
     KRDIANSLEK DLSSHFGVPT DAN