ID   EXE2_HELSC              Reviewed;          84 AA.
AC   C6EVG2;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Exendin-2-long;
DE   Contains:
DE     RecName: Full=Exendin-2;
DE     AltName: Full=Helodermin;
DE     AltName: Full=VIP-like 2;
DE   Flags: Precursor;
OS   Heloderma suspectum cinctum (Banded Gila monster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Neoanguimorpha; Helodermatidae; Heloderma.
OX   NCBI_TaxID=537493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 47-81, AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=19837656; DOI=10.1093/molbev/msp251;
RA   Fry B.G., Roelants K., Winter K., Hodgson W.C., Griesman L., Kwok H.F.,
RA   Scanlon D., Karas J., Shaw C., Wong L., Norman J.A.;
RT   "Novel venom proteins produced by differential domain-expression strategies
RT   in beaded lizards and gila monsters (genus Heloderma).";
RL   Mol. Biol. Evol. 27:395-407(2010).
RN   [2]
RP   FUNCTION.
RX   PubMed=9928018; DOI=10.1111/j.1749-6632.1998.tb11184.x;
RA   Gourlet P., Vandermeers A., Van Rampelbergh J., De Neef P., Cnudde J.,
RA   Waelbroeck M., Robberecht P.;
RT   "Analogues of VIP, helodermin, and PACAP discriminate between rat and human
RT   VIP1 and VIP2 receptors.";
RL   Ann. N. Y. Acad. Sci. 865:247-252(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=15003357; DOI=10.1016/j.peptides.2003.11.010;
RA   Tsueshita T., Onyukusel H., Sethi V., Gandhi S., Rubinstein I.;
RT   "Helospectin I and II evoke vasodilation in the intact peripheral
RT   microcirculation.";
RL   Peptides 25:65-69(2004).
CC   -!- FUNCTION: Has vasoactive intestinal peptide(VIP)/secretin-like
CC       biological activity. Interacts with rat and human VIP receptors 1
CC       (VIPR1) and 2 (VIPR2), with the highest affinity for the human VIPR2.
CC       Induces hypotension that is mediated by relaxation of cardiac smooth
CC       muscle. {ECO:0000269|PubMed:15003357, ECO:0000269|PubMed:19837656,
CC       ECO:0000269|PubMed:9928018}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the glucagon family. {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; EU790960; ACE95062.1; -; mRNA.
DR   AlphaFoldDB; C6EVG2; -.
DR   SMR; C6EVG2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR   InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR   Pfam; PF00123; Hormone_2; 1.
DR   SMART; SM00070; GLUCA; 1.
DR   PROSITE; PS00260; GLUCAGON; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues;
KW   G-protein coupled receptor impairing toxin; Hypotensive agent; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..44
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000414098"
FT   PEPTIDE         47..83
FT                   /note="Exendin-2-long"
FT                   /id="PRO_0000414099"
FT   PEPTIDE         47..81
FT                   /note="Exendin-2"
FT                   /id="PRO_0000414100"
SQ   SEQUENCE   84 AA;  9531 MW;  4CC1F9B3177897FD CRC64;
     MKSILWLCVF GLLIATLFPV SWQMAIKSRL SSEDSETDQR LFESKRHSDA IFTEEYSKLL
     AKLALQKYLA SILGSRTSPP PPSR