ID   CALCR_PHYBI             Reviewed;         115 AA.
AC   P81564;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Skin calcitonin gene-related peptide;
DE            Short=S-CGRP;
DE   Flags: Precursor;
OS   Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=8393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-106, AMIDATION AT
RP   PHE-106, CHARACTERIZATION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin;
RX   PubMed=10681586; DOI=10.1074/jbc.275.8.5934;
RA   Seon A.A., Pierre T.N., Redeker V., Lacombe C., Delfour A., Nicolas P.,
RA   Amiche M.;
RT   "Isolation, structure, synthesis, and activity of a new member of the
RT   calcitonin gene-related peptide family from frog skin and molecular cloning
RT   of its precursor.";
RL   J. Biol. Chem. 275:5934-5940(2000).
CC   -!- FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels
CC       including the coronary, cerebral and systemic vasculature. Its
CC       abundance in the CNS also points toward a neurotransmitter or
CC       neuromodulator role (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Skin, intestine and brain.
CC   -!- MASS SPECTROMETRY: Mass=3806.77; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10681586};
CC   -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR   EMBL; Y18495; CAB76385.1; -; mRNA.
DR   AlphaFoldDB; P81564; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR021117; Calcitonin-like.
DR   InterPro; IPR021116; Calcitonin/adrenomedullin.
DR   InterPro; IPR018360; Calcitonin_CS.
DR   InterPro; IPR001693; Calcitonin_peptide-like.
DR   InterPro; IPR000443; IAPP.
DR   PANTHER; PTHR10505; PTHR10505; 1.
DR   Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR   PRINTS; PR00818; ISLETAMYLOID.
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; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..69
FT                   /note="Removed in mature form by a carboxypeptidase"
FT                   /evidence="ECO:0000269|PubMed:10681586"
FT                   /id="PRO_0000004080"
FT   CHAIN           70..106
FT                   /note="Skin calcitonin gene-related peptide"
FT                   /id="PRO_0000004081"
FT   PROPEP          107..115
FT                   /note="Removed in mature form by an endoprotease"
FT                   /id="PRO_0000004082"
FT   MOD_RES         106
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:10681586"
FT   DISULFID        71..76
SQ   SEQUENCE   115 AA;  12438 MW;  A53D11255CA53D31 CRC64;
     MVLLKISSLL AVLGLLVCQM YSSQAAPARR ALEPLPDRVT EAHRLLRALI RELTAEDMEA
     SSSGAAHKRS CDTSTCATQR LADFLSRSGG IGSPDFVPTD VSANSFGRRR RSLHV