ID   GLUC_TORMA              Reviewed;          29 AA.
AC   P09567;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Glucagon;
GN   Name=gcg;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=4076759; DOI=10.1016/0016-6480(85)90073-5;
RA   Conlon J.M., Thim L.;
RT   "Primary structure of glucagon from an elasmobranchian fish. Torpedo
RT   marmorata.";
RL   Gen. Comp. Endocrinol. 60:398-405(1985).
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   PIR; S07211; S07211.
DR   AlphaFoldDB; P09567; -.
DR   SMR; P09567; -.
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; 1.
DR   PRINTS; PR00275; GLUCAGON.
DR   SMART; SM00070; GLUCA; 1.
DR   PROSITE; PS00260; GLUCAGON; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hormone; Secreted.
FT   PEPTIDE         1..29
FT                   /note="Glucagon"
FT                   /id="PRO_0000043929"
SQ   SEQUENCE   29 AA;  3511 MW;  04D96392086F0227 CRC64;
     HSEGTFTSDY SKYLDNRRAK DFVQWLMNT