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GLUC1_PETMA
ID   GLUC1_PETMA             Reviewed;         160 AA.
AC   Q9PUR1; Q9PRZ7; Q9PRZ8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Glucagon-1;
DE   Contains:
DE     RecName: Full=Glucagon-1;
DE     AltName: Full=Glucagon I;
DE   Contains:
DE     RecName: Full=Glucagon-like peptide 1-I;
DE              Short=GLP-1I;
DE   Contains:
DE     RecName: Full=Glucagon-like peptide 2-I;
DE              Short=GLP-2I;
DE   Flags: Precursor;
GN   Name=gcg1;
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Intestine;
RX   PubMed=10555286; DOI=10.1093/oxfordjournals.molbev.a026067;
RA   Irwin D.M., Huner O., Youson J.H.;
RT   "Lamprey proglucagon and the origin of glucagon-like peptides.";
RL   Mol. Biol. Evol. 16:1548-1557(1999).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 43-71 AND 82-113.
RC   TISSUE=Intestine;
RX   PubMed=8405897; DOI=10.1006/gcen.1993.1109;
RA   Conlon J.M., Nielsen P.F., Youson J.H.;
RT   "Primary structures of glucagon and glucagon-like peptide isolated from the
RT   intestine of the parasitic phase lamprey Petromyzon marinus.";
RL   Gen. Comp. Endocrinol. 91:96-104(1993).
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; AF159707; AAF09186.1; -; mRNA.
DR   AlphaFoldDB; Q9PUR1; -.
DR   SMR; Q9PUR1; -.
DR   STRING; 7757.ENSPMAP00000002387; -.
DR   PRIDE; Q9PUR1; -.
DR   Proteomes; UP000245300; Unplaced.
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; 3.
DR   PROSITE; PS00260; GLUCAGON; 2.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000305"
FT   PROPEP          23..40
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011371"
FT   PEPTIDE         43..71
FT                   /note="Glucagon-1"
FT                   /id="PRO_0000011372"
FT   PROPEP          74..79
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011373"
FT   PEPTIDE         82..113
FT                   /note="Glucagon-like peptide 1-I"
FT                   /id="PRO_0000011374"
FT   PROPEP          116..127
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011375"
FT   PEPTIDE         130..160
FT                   /note="Glucagon-like peptide 2-I"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011376"
FT   REGION          112..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   160 AA;  18042 MW;  9A52C530D5A74072 CRC64;
     MSDPGFLAAP VLLLLLVSLA SASLEQAASR DDDSAERPLS KRHSEGTFTS DYSKYLENKQ
     AKDFVRWLMN AKRGGSELQR RHADGTFTND MTSYLDAKAA RDFVSWLARS DKSRRDGGDH
     LAENSEDKRH AEDVNALLDR TMAKTFIEWL EKQNSNDQTD
 
 
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