GLUC1_LOPAM
ID GLUC1_LOPAM Reviewed; 124 AA.
AC P01278;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Glucagon-1;
DE AltName: Full=Glucagon I;
DE Contains:
DE RecName: Full=Glicentin-related polypeptide;
DE Short=GRPP;
DE Contains:
DE RecName: Full=Glucagon-1;
DE AltName: Full=Glucagon I;
DE Contains:
DE RecName: Full=Glucagon-like peptide 1;
DE AltName: Full=Glucagon-like peptide I;
DE Flags: Precursor;
GN Name=gcg1;
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=7043459; DOI=10.1073/pnas.79.2.345;
RA Lund P.K., Goodman R.H., Dee P.C., Habener J.F.;
RT "Pancreatic preproglucagon cDNA contains two glucagon-related coding
RT sequences arranged in tandem.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:345-349(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-83.
RX PubMed=6165720; DOI=10.1016/s0021-9258(19)69015-0;
RA Lund P.K., Goodman R.H., Habener J.F.;
RT "Pancreatic pre-proglucagons are encoded by two separate mRNAs.";
RL J. Biol. Chem. 256:6515-6518(1981).
RN [3]
RP PROTEIN SEQUENCE OF 53-81 AND 91-124.
RX PubMed=3058456; DOI=10.1210/endo-123-6-2639;
RA Nichols R., Lee T.D., Andrews P.C.;
RT "Pancreatic proglucagon processing: isolation and structures of glucagon
RT and glucagon-like peptide from gene I.";
RL Endocrinology 123:2639-2645(1988).
CC -!- FUNCTION: Glucagon plays a key role in glucose metabolism and
CC homeostasis. Regulates blood glucose by increasing gluconeogenesis and
CC decreasing glycolysis.
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; V00633; CAA23906.1; -; mRNA.
DR PIR; S06458; GCAF.
DR AlphaFoldDB; P01278; -.
DR SMR; P01278; -.
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; Direct protein sequencing; Hormone;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PEPTIDE 26..50
FT /note="Glicentin-related polypeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000011343"
FT PEPTIDE 53..81
FT /note="Glucagon-1"
FT /id="PRO_0000011344"
FT PROPEP 84..88
FT /evidence="ECO:0000250"
FT /id="PRO_0000011345"
FT PEPTIDE 91..124
FT /note="Glucagon-like peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000011346"
FT REGION 28..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 124 AA; 14165 MW; 22D142C9009B0D7A CRC64;
MKRIHSLAGI LLVLGLIQSS CRVLMQEADP SSSLEADSTL KDEPRELSNM KRHSEGTFSN
DYSKYLEDRK AQEFVRWLMN NKRSGVAEKR HADGTFTSDV SSYLKDQAIK DFVDRLKAGQ
VRRE
