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GLUC2_LOPAM
ID   GLUC2_LOPAM             Reviewed;         122 AA.
AC   P04092;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Glucagon-2;
DE   AltName: Full=Glucagon II;
DE   Contains:
DE     RecName: Full=Glicentin-related polypeptide;
DE              Short=GRPP;
DE   Contains:
DE     RecName: Full=Glucagon-2;
DE     AltName: Full=Glucagon II;
DE   Contains:
DE     RecName: Full=Glucagon-like peptide 2;
DE     AltName: Full=Glucagon-like peptide II;
DE   Flags: Precursor;
GN   Name=gcg2;
OS   Lophius americanus (American angler) (Anglerfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Lophiiformes; Lophiidae; Lophius.
OX   NCBI_TaxID=8073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6338015; DOI=10.1016/s0021-9258(18)32858-8;
RA   Lund P.K., Goodman R.H., Montminy M.R., Dee P.C., Habener J.F.;
RT   "Anglerfish islet pre-proglucagon II. Nucleotide and corresponding amino
RT   acid sequence of the cDNA.";
RL   J. Biol. Chem. 258:3280-3284(1983).
RN   [2]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=3526301; DOI=10.1016/0196-9781(86)90232-9;
RA   Noe B.D., Andrews P.C.;
RT   "Specific glucagon-related peptides isolated from anglerfish islets are
RT   metabolic cleavage products of (pre)proglucagon-II.";
RL   Peptides 7:331-336(1986).
CC   -!- FUNCTION: Promotes hydrolysis of glycogen and lipids, and raises the
CC       blood sugar level.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: Produced in the A cells of the islets of Langerhans in
CC       response to a drop in blood sugar concentration.
CC   -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR   EMBL; V00632; CAA23905.1; -; mRNA.
DR   PIR; A05150; GCAF2.
DR   AlphaFoldDB; P04092; -.
DR   SMR; P04092; -.
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; 1.
DR   Pfam; PF00123; Hormone_2; 2.
DR   PRINTS; PR00275; GLUCAGON.
DR   SMART; SM00070; GLUCA; 2.
DR   PROSITE; PS00260; GLUCAGON; 2.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Hormone; Secreted; Signal.
FT   SIGNAL          1..21
FT   PEPTIDE         22..49
FT                   /note="Glicentin-related polypeptide"
FT                   /id="PRO_0000011347"
FT   PEPTIDE         52..80
FT                   /note="Glucagon-2"
FT                   /id="PRO_0000011348"
FT   PROPEP          83..86
FT                   /id="PRO_0000011349"
FT   PEPTIDE         89..119
FT                   /note="Glucagon-like peptide 2"
FT                   /id="PRO_0000011350"
FT   PROPEP          122
FT                   /id="PRO_0000011351"
SQ   SEQUENCE   122 AA;  14171 MW;  5140AC47EF915519 CRC64;
     MTSLHSLAGL LLLMIIQSSW QMPDQDPDRN SMLLNENSML TEPIEPLNMK RHSEGTFSND
     YSKYLETRRA QDFVQWLKNS KRNGLFRRHA DGTYTSDVSS YLQDQAAKDF VSWLKAGRGR
     RE
 
 
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