ID   BOMB_BOMVA              Reviewed;         107 AA.
AC   P84213; P01296;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Bombesin;
DE   Flags: Precursor;
OS   Bombina variegata (Yellow-bellied toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Skin;
RX   PubMed=2335218; DOI=10.1016/0014-5793(90)80227-a;
RA   Richter K., Egger R., Kreil G.;
RT   "Molecular cloning of a cDNA encoding the bombesin precursor in skin of
RT   Bombina variegata.";
RL   FEBS Lett. 262:353-355(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 42-55, SUBCELLULAR LOCATION, PYROGLUTAMATE FORMATION AT
RP   GLN-42, AMIDATION AT MET-55, AND TISSUE SPECIFICITY.
RC   TISSUE=Skin secretion;
RX   PubMed=4537042; DOI=10.1016/0003-9861(72)90162-2;
RA   Anastasi A., Erspamer V., Bucci M.;
RT   "Isolation and amino acid sequences of alytesin and bombesin, two analogous
RT   active tetradecapeptides from the skin of European discoglossid frogs.";
RL   Arch. Biochem. Biophys. 148:443-446(1972).
RN   [3]
RP   PROTEIN SEQUENCE OF 42-55, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=15134346; DOI=10.1515/bc.2004.027;
RA   Marenah L., Flatt P.R., Orr D.F., McClean S., Shaw C., Abdel-Wahab Y.H.;
RT   "Skin secretion of the toad Bombina variegata contains multiple insulin-
RT   releasing peptides including bombesin and entirely novel insulinotropic
RT   structures.";
RL   Biol. Chem. 385:315-321(2004).
CC   -!- FUNCTION: Stimulates smooth muscle contraction. Role in induction of
CC       hypothermia, stimulation of DNA replication and release of many
CC       gastrointestinal hormones. Possesses insulin-releasing activity.
CC       {ECO:0000269|PubMed:15134346}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15134346,
CC       ECO:0000269|PubMed:2335218, ECO:0000269|PubMed:4537042}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:15134346, ECO:0000269|PubMed:2335218,
CC       ECO:0000269|PubMed:4537042}.
CC   -!- MASS SPECTROMETRY: Mass=1619.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15134346};
CC   -!- SIMILARITY: Belongs to the bombesin/neuromedin-B/ranatensin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X52447; CAA36686.1; -; mRNA.
DR   PIR; S09095; BSTDY.
DR   AlphaFoldDB; P84213; -.
DR   SMR; P84213; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; TAS:UniProtKB.
DR   GO; GO:0006952; P:defense response; TAS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; NAS:UniProtKB.
DR   GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
DR   InterPro; IPR000874; Bombesin.
DR   Pfam; PF02044; Bombesin; 1.
DR   PROSITE; PS00257; BOMBESIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..41
FT                   /id="PRO_0000003008"
FT   PEPTIDE         42..55
FT                   /note="Bombesin"
FT                   /id="PRO_0000003009"
FT   PROPEP          56..107
FT                   /id="PRO_0000003010"
FT   MOD_RES         42
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:4537042"
FT   MOD_RES         55
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000269|PubMed:4537042"
SQ   SEQUENCE   107 AA;  12341 MW;  9692B50600FAF618 CRC64;
     MSAIPLNRIL PLGFLLIFSF ISLSSCMEFV EDPNNQGGLN LQQRLGNQWA VGHLMGKKSL
     QDTDFEEMES FAKRNVENMK AESERELRHA QLVVRNILEQ YLKNMQN