GLUC_MOUSE
ID GLUC_MOUSE Reviewed; 180 AA.
AC P55095; Q3UFE9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Pro-glucagon;
DE Contains:
DE RecName: Full=Glicentin;
DE Contains:
DE RecName: Full=Glicentin-related polypeptide;
DE Short=GRPP;
DE Contains:
DE RecName: Full=Oxyntomodulin;
DE Short=OXM;
DE Short=OXY;
DE Contains:
DE RecName: Full=Glucagon;
DE Contains:
DE RecName: Full=Glucagon-like peptide 1;
DE Short=GLP-1;
DE Contains:
DE RecName: Full=Glucagon-like peptide 1(7-37);
DE Short=GLP-1(7-37);
DE Contains:
DE RecName: Full=Glucagon-like peptide 1(7-36);
DE Short=GLP-1(7-36);
DE Contains:
DE RecName: Full=Glucagon-like peptide 2;
DE Short=GLP-2;
DE Flags: Precursor;
GN Name=Gcg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=7730317; DOI=10.1074/jbc.270.17.10136;
RA Rothenberg M.E., Eilertson C.D., Klein K., Zhou Y., Linberg I.,
RA McDonald J.K., Mackin R.B., Noe B.D.;
RT "Processing of mouse proglucagon by recombinant prohormone convertase 1 and
RT immunopurified prohormone convertase 2 in vitro.";
RL J. Biol. Chem. 270:10136-10146(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shamsadin R., Knepel W.;
RT "Mouse glucagon full length cDNA.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION OF GLP-1 AND GLP-1(7-36) AMIDE.
RX PubMed=1886889;
RA Fridolf T., Bottcher G., Sundler F., Ahren B.;
RT "GLP-1 and GLP-1(7-36) amide: influences on basal and stimulated insulin
RT and glucagon secretion in the mouse.";
RL Pancreas 6:208-215(1991).
RN [6]
RP PROTEOLYTIC PROCESSING BY PCSK1.
RX PubMed=9407057; DOI=10.1074/jbc.272.52.32810;
RA Rouille Y., Kantengwa S., Irminger J.C., Halban P.A.;
RT "Role of the prohormone convertase PC3 in the processing of proglucagon to
RT glucagon-like peptide 1.";
RL J. Biol. Chem. 272:32810-32816(1997).
RN [7]
RP PROTEOLYTIC PROCESSING BY PCSK2.
RX PubMed=11356850; DOI=10.1074/jbc.m103362200;
RA Furuta M., Zhou A., Webb G., Carroll R., Ravazzola M., Orci L.,
RA Steiner D.F.;
RT "Severe defect in proglucagon processing in islet A-cells of prohormone
RT convertase 2 null mice.";
RL J. Biol. Chem. 276:27197-27202(2001).
RN [8]
RP REVIEW.
RX PubMed=10605628; DOI=10.1210/edrv.20.6.0385;
RA Kieffer T.J., Habener J.F.;
RT "The glucagon-like peptides.";
RL Endocr. Rev. 20:876-913(1999).
RN [9]
RP REVIEW.
RX PubMed=10322410; DOI=10.1016/s1043-2760(98)00136-2;
RA Drucker D.J.;
RT "Glucagon-like peptide 2.";
RL Trends Endocrinol. Metab. 10:153-156(1999).
RN [10]
RP REVIEW.
RX PubMed=12626323; DOI=10.1152/ajpendo.00492.2002;
RA Jiang G., Zhang B.B.;
RT "Glucagon and regulation of glucose metabolism.";
RL Am. J. Physiol. 284:E671-E678(2003).
RN [11]
RP REVIEW.
RX PubMed=14719035; DOI=10.1139/y03-107;
RA Brubaker P.L., Anini Y.;
RT "Direct and indirect mechanisms regulating secretion of glucagon-like
RT peptide-1 and glucagon-like peptide-2.";
RL Can. J. Physiol. Pharmacol. 81:1005-1012(2003).
RN [12]
RP REVIEW.
RX PubMed=12554744; DOI=10.1210/me.2002-0306;
RA Drucker D.J.;
RT "Glucagon-like peptides: regulators of cell proliferation, differentiation,
RT and apoptosis.";
RL Mol. Endocrinol. 17:161-171(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-105; SER-108; SER-150
RP AND SER-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP INDUCTION BY EXERCISE (GLUCAGON-LIKE PEPTIDE 1), FUNCTION (GLUCAGON-LIKE
RP PEPTIDE 1), AND TISSUE SPECIFICITY (GLUCAGON-LIKE PEPTIDE 1).
RX PubMed=22037645; DOI=10.1038/nm.2513;
RA Ellingsgaard H., Hauselmann I., Schuler B., Habib A.M., Baggio L.L.,
RA Meier D.T., Eppler E., Bouzakri K., Wueest S., Muller Y.D., Hansen A.M.,
RA Reinecke M., Konrad D., Gassmann M., Reimann F., Halban P.A., Gromada J.,
RA Drucker D.J., Gribble F.M., Ehses J.A., Donath M.Y.;
RT "Interleukin-6 enhances insulin secretion by increasing glucagon-like
RT peptide-1 secretion from L cells and alpha cells.";
RL Nat. Med. 17:1481-1489(2011).
CC -!- FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and
CC homeostasis. Regulates blood glucose by increasing gluconeogenesis and
CC decreasing glycolysis. A counterregulatory hormone of insulin, raises
CC plasma glucose levels in response to insulin-induced hypoglycemia.
CC Plays an important role in initiating and maintaining hyperglycemic
CC conditions in diabetes. {ECO:0000305|PubMed:10605628,
CC ECO:0000305|PubMed:12626323}.
CC -!- FUNCTION: [Glucagon-like peptide 1]: Potent stimulator of glucose-
CC dependent insulin release. Also stimulates insulin release in response
CC to IL6 (PubMed:22037645). Plays important roles on gastric motility and
CC the suppression of plasma glucagon levels. May be involved in the
CC suppression of satiety and stimulation of glucose disposal in
CC peripheral tissues, independent of the actions of insulin. Has growth-
CC promoting activities on intestinal epithelium. May also regulate the
CC hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH,
CC oxytocin, and vasopressin secretion. Increases islet mass through
CC stimulation of islet neogenesis and pancreatic beta cell proliferation.
CC Inhibits beta cell apoptosis (Probable). {ECO:0000269|PubMed:22037645,
CC ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744,
CC ECO:0000305|PubMed:14719035}.
CC -!- FUNCTION: [Glucagon-like peptide 2]: Stimulates intestinal growth and
CC up-regulates villus height in the small intestine, concomitant with
CC increased crypt cell proliferation and decreased enterocyte apoptosis.
CC The gastrointestinal tract, from the stomach to the colon is the
CC principal target for GLP-2 action. Plays a key role in nutrient
CC homeostasis, enhancing nutrient assimilation through enhanced
CC gastrointestinal function, as well as increasing nutrient disposal.
CC Stimulates intestinal glucose transport and decreases mucosal
CC permeability. {ECO:0000305|PubMed:10322410,
CC ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744,
CC ECO:0000305|PubMed:14719035}.
CC -!- FUNCTION: [Oxyntomodulin]: Significantly reduces food intake. Inhibits
CC gastric emptying in humans. Suppression of gastric emptying may lead to
CC increased gastric distension, which may contribute to satiety by
CC causing a sensation of fullness. {ECO:0000305|PubMed:10605628,
CC ECO:0000305|PubMed:12554744}.
CC -!- FUNCTION: [Glicentin]: May modulate gastric acid secretion and the
CC gastro-pyloro-duodenal activity. May play an important role in
CC intestinal mucosal growth in the early period of life.
CC {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22037645}.
CC -!- SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted
CC {ECO:0000269|PubMed:22037645}.
CC -!- TISSUE SPECIFICITY: [Glucagon]: Secreted in the A cells of the islets
CC of Langerhans. {ECO:0000269|PubMed:22037645}.
CC -!- TISSUE SPECIFICITY: [Glucagon-like peptide 1]: Secreted in the A cells
CC of the islets of Langerhans (PubMed:22037645). Secreted from
CC enteroendocrine L cells throughout the gastrointestinal tract
CC (PubMed:22037645). Also secreted in selected neurons in the brain.
CC {ECO:0000269|PubMed:22037645}.
CC -!- TISSUE SPECIFICITY: [Glucagon-like peptide 2]: Secreted from
CC enteroendocrine cells throughout the gastrointestinal tract. Also
CC secreted in selected neurons in the brain.
CC -!- TISSUE SPECIFICITY: [Glicentin]: Secreted from enteroendocrine cells
CC throughout the gastrointestinal tract.
CC -!- TISSUE SPECIFICITY: [Oxyntomodulin]: Secreted from enteroendocrine
CC cells throughout the gastrointestinal tract.
CC -!- INDUCTION: [Glucagon]: Release is stimulated by hypoglycemia and
CC inhibited by hyperglycemia, insulin, and somatostatin.
CC {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12626323}.
CC -!- INDUCTION: [Glucagon-like peptide 1]: Production by pancreatic and
CC inestinal L cells is increased by exercise in an IL6-dependent manner
CC (PubMed:22037645). High-fat diet increases pancreatic content
CC (PubMed:22037645). {ECO:0000269|PubMed:22037645}.
CC -!- INDUCTION: [Glucagon-like peptide 2]: Induced in response to nutrient
CC ingestion. {ECO:0000305|PubMed:10322410, ECO:0000305|PubMed:10605628,
CC ECO:0000305|PubMed:12554744, ECO:0000305|PubMed:14719035}.
CC -!- PTM: Proglucagon is post-translationally processed in a tissue-specific
CC manner in pancreatic A cells and intestinal L cells. In pancreatic A
CC cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In
CC the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and
CC oxyntomodulin. GLP-1 is further N-terminally truncated by post-
CC translational processing in the intestinal L cells resulting in GLP-
CC 1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither
CC important for the metabolism of GLP-1 nor for its effects on the
CC endocrine pancreas (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR EMBL; Z46845; CAA86902.1; -; mRNA.
DR EMBL; AF276754; AAK96898.1; -; mRNA.
DR EMBL; AK007911; BAB25344.1; -; mRNA.
DR EMBL; AK148544; BAE28612.1; -; mRNA.
DR EMBL; BC012975; AAH12975.1; -; mRNA.
DR CCDS; CCDS16066.1; -.
DR PIR; A57294; A57294.
DR RefSeq; NP_032126.1; NM_008100.4.
DR AlphaFoldDB; P55095; -.
DR SMR; P55095; -.
DR STRING; 10090.ENSMUSP00000099794; -.
DR iPTMnet; P55095; -.
DR PhosphoSitePlus; P55095; -.
DR MaxQB; P55095; -.
DR PaxDb; P55095; -.
DR PRIDE; P55095; -.
DR ProteomicsDB; 271001; -.
DR Antibodypedia; 3506; 1906 antibodies from 45 providers.
DR DNASU; 14526; -.
DR Ensembl; ENSMUST00000102733; ENSMUSP00000099794; ENSMUSG00000000394.
DR GeneID; 14526; -.
DR KEGG; mmu:14526; -.
DR UCSC; uc008jvj.1; mouse.
DR CTD; 2641; -.
DR MGI; MGI:95674; Gcg.
DR VEuPathDB; HostDB:ENSMUSG00000000394; -.
DR eggNOG; ENOG502RYPR; Eukaryota.
DR GeneTree; ENSGT00390000005372; -.
DR InParanoid; P55095; -.
DR OMA; KRNGQQG; -.
DR OrthoDB; 1349644at2759; -.
DR PhylomeDB; P55095; -.
DR TreeFam; TF332333; -.
DR Reactome; R-MMU-163359; Glucagon signaling in metabolic regulation.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 14526; 0 hits in 59 CRISPR screens.
DR ChiTaRS; Gcg; mouse.
DR PRO; PR:P55095; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P55095; protein.
DR Bgee; ENSMUSG00000000394; Expressed in dorsal pancreas and 41 other tissues.
DR ExpressionAtlas; P55095; baseline and differential.
DR Genevisible; P55095; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0031767; F:gastric inhibitory polypeptide receptor binding; ISO:MGI.
DR GO; GO:0031769; F:glucagon receptor binding; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032099; P:negative regulation of appetite; ISO:MGI.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IDA:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IDA:MGI.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IGI:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB.
DR GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
DR GO; GO:0014823; P:response to activity; IDA:UniProtKB.
DR InterPro; IPR015550; Glucagon.
DR InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR PANTHER; PTHR11418; PTHR11418; 1.
DR Pfam; PF00123; Hormone_2; 3.
DR PRINTS; PR00275; GLUCAGON.
DR SMART; SM00070; GLUCA; 3.
DR PROSITE; PS00260; GLUCAGON; 4.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Hormone; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250|UniProtKB:P01274"
FT PEPTIDE 21..89
FT /note="Glicentin"
FT /evidence="ECO:0000250|UniProtKB:P01274"
FT /id="PRO_0000011273"
FT PEPTIDE 21..50
FT /note="Glicentin-related polypeptide"
FT /evidence="ECO:0000250|UniProtKB:P09686"
FT /id="PRO_0000011274"
FT PEPTIDE 53..89
FT /note="Oxyntomodulin"
FT /evidence="ECO:0000250|UniProtKB:P06883"
FT /id="PRO_0000011275"
FT PEPTIDE 53..81
FT /note="Glucagon"
FT /evidence="ECO:0000250|UniProtKB:P01275"
FT /id="PRO_0000011276"
FT PROPEP 84..89
FT /evidence="ECO:0000250|UniProtKB:P01275"
FT /id="PRO_0000011277"
FT PEPTIDE 92..128
FT /note="Glucagon-like peptide 1"
FT /evidence="ECO:0000250|UniProtKB:P01275"
FT /id="PRO_0000011278"
FT PEPTIDE 98..128
FT /note="Glucagon-like peptide 1(7-37)"
FT /evidence="ECO:0000250|UniProtKB:P01275"
FT /id="PRO_0000011279"
FT PEPTIDE 98..127
FT /note="Glucagon-like peptide 1(7-36)"
FT /evidence="ECO:0000250|UniProtKB:P01275"
FT /id="PRO_0000011280"
FT PROPEP 131..145
FT /evidence="ECO:0000250|UniProtKB:P15438"
FT /id="PRO_0000011281"
FT PEPTIDE 146..178
FT /note="Glucagon-like peptide 2"
FT /evidence="ECO:0000250|UniProtKB:P15438"
FT /id="PRO_0000011282"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 52..53
FT /note="Cleavage; by PCSK2"
FT SITE 83..84
FT /note="Cleavage; by PCSK1 and PCSK2"
FT SITE 91..92
FT /note="Cleavage; by PCSK1"
FT SITE 97..98
FT /note="Cleavage; by PCSK1"
FT SITE 130..131
FT /note="Cleavage; by PCSK1"
FT SITE 145..146
FT /note="Cleavage; by PCSK1"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Arginine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 180 AA; 20906 MW; 595AA6DD9A589950 CRC64;
MKTIYFVAGL LIMLVQGSWQ HALQDTEENP RSFPASQTEA HEDPDEMNED KRHSQGTFTS
DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE GTFTSDVSSY LEGQAAKEFI
AWLVKGRGRR DFPEEVAIAE ELGRRHADGS FSDEMSTILD NLATRDFINW LIQTKITDKK
