Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P55095

- GLUC_MOUSE

UniProt

P55095 - GLUC_MOUSE

Protein

Glucagon

Gene

Gcg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia By similarity.By similarity
    GLP-1 is a potent stimulator of glucose-dependent insulin release. Play important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Have growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation By similarity.By similarity
    GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability By similarity.By similarity
    Oxyntomodulin significantly reduces food intake.By similarity
    Glicentin may modulate gastric acid secretion and gastro-pyloro-duodenal activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei52 – 532Cleavage; by PCSK2
    Sitei83 – 842Cleavage; by PCSK1 and PCSK2
    Sitei91 – 922Cleavage; by PCSK1
    Sitei97 – 982Cleavage; by PCSK1
    Sitei130 – 1312Cleavage; by PCSK1
    Sitei145 – 1462Cleavage; by PCSK1

    GO - Molecular functioni

    1. glucagon receptor binding Source: RefGenome
    2. hormone activity Source: RefGenome

    GO - Biological processi

    1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RefGenome
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of execution phase of apoptosis Source: MGI
    4. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    5. positive regulation of calcium ion import Source: UniProtKB
    6. positive regulation of cAMP biosynthetic process Source: UniProtKB
    7. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    8. positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter Source: MGI
    9. positive regulation of histone H3-K4 methylation Source: MGI
    10. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    11. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    12. positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
    13. positive regulation of protein binding Source: UniProtKB
    14. positive regulation of protein kinase activity Source: UniProtKB
    15. protein kinase A signaling Source: UniProtKB
    16. regulation of insulin secretion Source: MGI
    17. response to starvation Source: RefGenome

    Keywords - Molecular functioni

    Hormone

    Enzyme and pathway databases

    ReactomeiREACT_207651. G alpha (q) signalling events.
    REACT_210399. Glucagon signaling in metabolic regulation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucagon
    Cleaved into the following 8 chains:
    Oxyntomodulin
    Short name:
    OXM
    Short name:
    OXY
    Glucagon-like peptide 1
    Short name:
    GLP-1
    Glucagon-like peptide 1(7-37)
    Short name:
    GLP-1(7-37)
    Glucagon-like peptide 1(7-36)
    Short name:
    GLP-1(7-36)
    Glucagon-like peptide 2
    Short name:
    GLP-2
    Gene namesi
    Name:Gcg
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:95674. Gcg.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular space Source: MGI
    3. secretory granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Peptidei21 – 8969GlicentinBy similarityPRO_0000011273Add
    BLAST
    Peptidei21 – 5030Glicentin-related polypeptideBy similarityPRO_0000011274Add
    BLAST
    Peptidei53 – 8937OxyntomodulinBy similarityPRO_0000011275Add
    BLAST
    Peptidei53 – 8129GlucagonBy similarityPRO_0000011276Add
    BLAST
    Propeptidei84 – 896By similarityPRO_0000011277
    Peptidei92 – 12837Glucagon-like peptide 1By similarityPRO_0000011278Add
    BLAST
    Peptidei98 – 12831Glucagon-like peptide 1(7-37)By similarityPRO_0000011279Add
    BLAST
    Peptidei98 – 12730Glucagon-like peptide 1(7-36)By similarityPRO_0000011280Add
    BLAST
    Propeptidei131 – 14515By similarityPRO_0000011281Add
    BLAST
    Peptidei146 – 17833Glucagon-like peptide 2By similarityPRO_0000011282Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei127 – 1271Arginine amideBy similarity

    Post-translational modificationi

    Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas By similarity.By similarity

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues

    Proteomic databases

    MaxQBiP55095.
    PaxDbiP55095.
    PRIDEiP55095.

    PTM databases

    PhosphoSiteiP55095.

    Miscellaneous databases

    PMAP-CutDBP55095.

    Expressioni

    Tissue specificityi

    Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP-1 and GLP-2 are also secreted in selected neurons in the brain.

    Inductioni

    Glucagon release is stimulated by hypoglycemia and inhibited by hyperglycemia, insulin, and somatostatin. GLP-1 and GLP-2 are induced in response to nutrient ingestion By similarity.By similarity

    Gene expression databases

    BgeeiP55095.
    CleanExiMM_GCG.
    GenevestigatoriP55095.

    Structurei

    3D structure databases

    ProteinModelPortaliP55095.
    SMRiP55095. Positions 53-81, 98-127, 146-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glucagon family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG42743.
    GeneTreeiENSGT00390000005372.
    HOGENOMiHOG000231876.
    HOVERGENiHBG003010.
    InParanoidiP55095.
    KOiK05259.
    OMAiQTEAHED.
    OrthoDBiEOG7WMCM1.
    PhylomeDBiP55095.
    TreeFamiTF332333.

    Family and domain databases

    InterProiIPR015550. Glucagon-like.
    IPR000532. Glucagon_GIP_secretin_VIP.
    [Graphical view]
    PANTHERiPTHR11418. PTHR11418. 1 hit.
    PfamiPF00123. Hormone_2. 3 hits.
    [Graphical view]
    PRINTSiPR00275. GLUCAGON.
    SMARTiSM00070. GLUCA. 3 hits.
    [Graphical view]
    PROSITEiPS00260. GLUCAGON. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P55095-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTIYFVAGL LIMLVQGSWQ HALQDTEENP RSFPASQTEA HEDPDEMNED    50
    KRHSQGTFTS DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE 100
    GTFTSDVSSY LEGQAAKEFI AWLVKGRGRR DFPEEVAIAE ELGRRHADGS 150
    FSDEMSTILD NLATRDFINW LIQTKITDKK 180
    Length:180
    Mass (Da):20,906
    Last modified:October 1, 1996 - v1
    Checksum:i595AA6DD9A589950
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46845 mRNA. Translation: CAA86902.1.
    AF276754 mRNA. Translation: AAK96898.1.
    AK007911 mRNA. Translation: BAB25344.1.
    AK148544 mRNA. Translation: BAE28612.1.
    BC012975 mRNA. Translation: AAH12975.1.
    CCDSiCCDS16066.1.
    PIRiA57294.
    RefSeqiNP_032126.1. NM_008100.3.
    UniGeneiMm.45494.

    Genome annotation databases

    EnsembliENSMUST00000102733; ENSMUSP00000099794; ENSMUSG00000000394.
    GeneIDi14526.
    KEGGimmu:14526.
    UCSCiuc008jvj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46845 mRNA. Translation: CAA86902.1 .
    AF276754 mRNA. Translation: AAK96898.1 .
    AK007911 mRNA. Translation: BAB25344.1 .
    AK148544 mRNA. Translation: BAE28612.1 .
    BC012975 mRNA. Translation: AAH12975.1 .
    CCDSi CCDS16066.1.
    PIRi A57294.
    RefSeqi NP_032126.1. NM_008100.3.
    UniGenei Mm.45494.

    3D structure databases

    ProteinModelPortali P55095.
    SMRi P55095. Positions 53-81, 98-127, 146-178.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P55095.

    Proteomic databases

    MaxQBi P55095.
    PaxDbi P55095.
    PRIDEi P55095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102733 ; ENSMUSP00000099794 ; ENSMUSG00000000394 .
    GeneIDi 14526.
    KEGGi mmu:14526.
    UCSCi uc008jvj.1. mouse.

    Organism-specific databases

    CTDi 2641.
    MGIi MGI:95674. Gcg.

    Phylogenomic databases

    eggNOGi NOG42743.
    GeneTreei ENSGT00390000005372.
    HOGENOMi HOG000231876.
    HOVERGENi HBG003010.
    InParanoidi P55095.
    KOi K05259.
    OMAi QTEAHED.
    OrthoDBi EOG7WMCM1.
    PhylomeDBi P55095.
    TreeFami TF332333.

    Enzyme and pathway databases

    Reactomei REACT_207651. G alpha (q) signalling events.
    REACT_210399. Glucagon signaling in metabolic regulation.

    Miscellaneous databases

    ChiTaRSi GCG. mouse.
    NextBioi 286168.
    PMAP-CutDB P55095.
    PROi P55095.
    SOURCEi Search...

    Gene expression databases

    Bgeei P55095.
    CleanExi MM_GCG.
    Genevestigatori P55095.

    Family and domain databases

    InterProi IPR015550. Glucagon-like.
    IPR000532. Glucagon_GIP_secretin_VIP.
    [Graphical view ]
    PANTHERi PTHR11418. PTHR11418. 1 hit.
    Pfami PF00123. Hormone_2. 3 hits.
    [Graphical view ]
    PRINTSi PR00275. GLUCAGON.
    SMARTi SM00070. GLUCA. 3 hits.
    [Graphical view ]
    PROSITEi PS00260. GLUCAGON. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Processing of mouse proglucagon by recombinant prohormone convertase 1 and immunopurified prohormone convertase 2 in vitro."
      Rothenberg M.E., Eilertson C.D., Klein K., Zhou Y., Linberg I., McDonald J.K., Mackin R.B., Noe B.D.
      J. Biol. Chem. 270:10136-10146(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreatic islet.
    2. "Mouse glucagon full length cDNA."
      Shamsadin R., Knepel W.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Pancreas.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.
    5. "GLP-1 and GLP-1(7-36) amide: influences on basal and stimulated insulin and glucagon secretion in the mouse."
      Fridolf T., Bottcher G., Sundler F., Ahren B.
      Pancreas 6:208-215(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF GLP-1 AND GLP-1(7-36) AMIDE.
    6. "Role of the prohormone convertase PC3 in the processing of proglucagon to glucagon-like peptide 1."
      Rouille Y., Kantengwa S., Irminger J.C., Halban P.A.
      J. Biol. Chem. 272:32810-32816(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING BY PCSK1.
    7. "Severe defect in proglucagon processing in islet A-cells of prohormone convertase 2 null mice."
      Furuta M., Zhou A., Webb G., Carroll R., Ravazzola M., Orci L., Steiner D.F.
      J. Biol. Chem. 276:27197-27202(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING BY PCSK2.
    8. "Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis."
      Drucker D.J.
      Mol. Endocrinol. 17:161-171(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    9. "Glucagon and regulation of glucose metabolism."
      Jiang G., Zhang B.B.
      Am. J. Physiol. 284:E671-E678(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    10. Cited for: REVIEW.
    11. Cited for: REVIEW.

    Entry informationi

    Entry nameiGLUC_MOUSE
    AccessioniPrimary (citable) accession number: P55095
    Secondary accession number(s): Q3UFE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3