ID   GLUC2_XENLA             Reviewed;         219 AA.
AC   O42144; Q5D082;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Glucagon-2;
DE   AltName: Full=Glucagon II;
DE   Contains:
DE     RecName: Full=Glucagon;
DE   Contains:
DE     RecName: Full=Glucagon-like peptide 1A;
DE              Short=GLP-1A;
DE   Contains:
DE     RecName: Full=Glucagon-like peptide 1B;
DE              Short=GLP-1B;
DE   Contains:
DE     RecName: Full=Glucagon-like peptide 1C;
DE              Short=GLP-1C;
DE   Flags: Precursor;
GN   Name=gcg2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=9223287; DOI=10.1073/pnas.94.15.7915;
RA   Irwin D.M., Satkunarajah M., Wen Y., Brubaker P.L., Pederson R.A.,
RA   Wheeler M.B.;
RT   "The Xenopus proglucagon gene encodes novel GLP-1-like peptides with
RT   insulinotropic properties.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7915-7920(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes hydrolysis of glycogen and lipids, and raises the
CC       blood sugar level.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR   EMBL; AF004433; AAB65661.1; -; mRNA.
DR   EMBL; BC054234; AAH54234.1; -; mRNA.
DR   RefSeq; NP_001079787.1; NM_001086318.2.
DR   AlphaFoldDB; O42144; -.
DR   SMR; O42144; -.
DR   DNASU; 379477; -.
DR   GeneID; 379477; -.
DR   KEGG; xla:379477; -.
DR   CTD; 100136748; -.
DR   OMA; ESRNGPM; -.
DR   OrthoDB; 1349644at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 379477; Expressed in pancreas and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR015550; Glucagon.
DR   InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR   PANTHER; PTHR11418; PTHR11418; 2.
DR   Pfam; PF00123; Hormone_2; 4.
DR   PRINTS; PR00275; GLUCAGON.
DR   SMART; SM00070; GLUCA; 4.
DR   PROSITE; PS00260; GLUCAGON; 3.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000305"
FT   PROPEP          21..50
FT                   /id="PRO_0000011401"
FT   PEPTIDE         53..81
FT                   /note="Glucagon"
FT                   /id="PRO_0000011402"
FT   PROPEP          84..95
FT                   /id="PRO_0000011403"
FT   PEPTIDE         97..133
FT                   /note="Glucagon-like peptide 1A"
FT                   /id="PRO_0000011404"
FT   PROPEP          136..140
FT                   /id="PRO_0000011405"
FT   PEPTIDE         142..172
FT                   /note="Glucagon-like peptide 1B"
FT                   /id="PRO_0000011406"
FT   PROPEP          175..178
FT                   /id="PRO_0000011407"
FT   PEPTIDE         180..210
FT                   /note="Glucagon-like peptide 1C"
FT                   /id="PRO_0000011408"
FT   PROPEP          213..219
FT                   /id="PRO_0000011409"
FT   REGION          23..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   219 AA;  25271 MW;  ACC699233C362CE0 CRC64;
     MKSTCYMIGI LLLILQNTYQ SPVPEADGSS RSVKAARNEA VDDSEQLKEV KRHSQGTFTS
     DYSKYLDSRR AQDFVQWLMN TKRSGGLSRR NADYERHAEG TFTSDVTQHL DEKAAKEFID
     WLINGGPTKE IISRRNAEIE RHAEGTYTND VTEYLEEKAT KAFIEWLIKG KPKKIRYSRH
     AEGTFTNDMT NYLEEKAAKE FVGWLINGRP KRKDLLEEH