ID   CALC_CANLF              Reviewed;         130 AA.
AC   P41547; Q9MYV2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Calcitonin;
DE   Flags: Precursor;
GN   Name=CALCA; Synonyms=CALC, CCALCI;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10967131; DOI=10.1007/s003350010157;
RA   Wende S., Krempler A., Breen M., Brunnberg L., Brenig B.;
RT   "Molecular analysis and chromosomal assignment of the canine CALC-I/alpha-
RT   CGRP gene.";
RL   Mamm. Genome 11:736-740(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-50, AND NUCLEOTIDE SEQUENCE [MRNA] OF 64-130.
RC   TISSUE=Thyroid;
RX   PubMed=1758974; DOI=10.1016/0167-0115(91)90082-r;
RA   Mol J.A., Kwant M.M., Arnold I.C.J., Hazewinkel H.A.W.;
RT   "Elucidation of the sequence of canine (pro)-calcitonin. A molecular
RT   biological and protein chemical approach.";
RL   Regul. Pept. 35:189-195(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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Calcitonin;
CC         IsoId=P41547-1; Sequence=Displayed;
CC       Name=Calcitonin-gene related peptide I;
CC         IsoId=Q9MYV1-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Synthesized by C-cells of the thyroid gland.
CC   -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR   EMBL; AJ271090; CAB97486.1; -; Genomic_DNA.
DR   EMBL; X56994; CAA40311.1; ALT_SEQ; mRNA.
DR   PIR; A60063; A60063.
DR   RefSeq; NP_001003266.1; NM_001003266.2. [P41547-1]
DR   AlphaFoldDB; P41547; -.
DR   SMR; P41547; -.
DR   STRING; 9612.ENSCAFP00000012567; -.
DR   PaxDb; P41547; -.
DR   Ensembl; ENSCAFT00030047165; ENSCAFP00030041235; ENSCAFG00030025508. [P41547-1]
DR   Ensembl; ENSCAFT00040038196; ENSCAFP00040033301; ENSCAFG00040020572. [P41547-1]
DR   Ensembl; ENSCAFT00845041491; ENSCAFP00845032532; ENSCAFG00845023464. [P41547-1]
DR   GeneID; 403946; -.
DR   CTD; 796; -.
DR   VEuPathDB; HostDB:ENSCAFG00845023464; -.
DR   eggNOG; ENOG502RZI5; Eukaryota.
DR   GeneTree; ENSGT00940000167380; -.
DR   HOGENOM; CLU_122444_0_0_1; -.
DR   InParanoid; P41547; -.
DR   OrthoDB; 1454612at2759; -.
DR   TreeFam; TF333069; -.
DR   Proteomes; UP000002254; Chromosome 21.
DR   Bgee; ENSCAFG00000008562; Expressed in spinal cord and 17 other tissues.
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   Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Hormone; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:1758974"
FT   PROPEP          26..82
FT                   /id="PRO_0000004038"
FT   PEPTIDE         85..116
FT                   /note="Calcitonin"
FT                   /id="PRO_0000004039"
FT   PROPEP          121..130
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004040"
FT   REGION          62..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01257"
FT   MOD_RES         116
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        85..91
FT                   /evidence="ECO:0000250"
FT   CONFLICT        45
FT                   /note="E -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="L -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="L -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   130 AA;  14051 MW;  632F07397D9CFDA7 CRC64;
     MGLWKSSPFL AFSILVLCQA GGLQAAPFRS ALEGLPDPTA LSEKEGRLLL AALVKAYVQR
     KNELEQEQEQ ETEGSSLDSS RAKRCSNLST CVLGTYSKDL NNFHTFSGIG FGAETPGKKR
     DIASGLERGR