ID   NEC2_HUMAN              Reviewed;         638 AA.
AC   P16519; B1ANH9; B4DFQ3; Q14927; Q5JYQ1; Q8IWA8; Q9NQG3; Q9NUG1; Q9UJC6;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=Neuroendocrine convertase 2;
DE            Short=NEC 2;
DE            EC=3.4.21.94;
DE   AltName: Full=KEX2-like endoprotease 2;
DE   AltName: Full=Prohormone convertase 2;
DE   AltName: Full=Proprotein convertase 2;
DE            Short=PC2;
DE   Flags: Precursor;
GN   Name=PCSK2; Synonyms=NEC2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Insulinoma;
RX   PubMed=2154467; DOI=10.1016/s0021-9258(19)39721-2;
RA   Smeekens S.P., Steiner D.F.;
RT   "Identification of a human insulinoma cDNA encoding a novel mammalian
RT   protein structurally related to the yeast dibasic processing protease
RT   Kex2.";
RL   J. Biol. Chem. 265:2997-3000(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=1594602; DOI=10.1073/pnas.89.11.4977;
RA   Ohagi S., Lamendola J., Lebeau M.M., Espinosa R., Takeda J., Smeekens S.P.,
RA   Chan S.J., Steiner D.F.;
RT   "Identification and analysis of the gene encoding human PC2, a prohormone
RT   convertase expressed in neuroendocrine tissues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4977-4981(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Amygdala, and Brain cortex;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP   GLN-244 AND GLU-484.
RC   TISSUE=Brain, and Lung;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX   PubMed=7983775;
RA   Ohagi S., Yoshida H., Nanjo K.;
RT   "Analysis of the gene encoding human PC2, a prohormone processing enzyme.";
RL   Nippon Rinsho 52:2544-2549(1994).
RN   [8]
RP   FUNCTION.
RX   PubMed=9287128; DOI=10.1016/s0014-5793(97)00892-2;
RA   Rouille Y., Bianchi M., Irminger J.C., Halban P.A.;
RT   "Role of the prohormone convertase PC2 in the processing of proglucagon to
RT   glucagon.";
RL   FEBS Lett. 413:119-123(1997).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, VARIANT TRP-430, AND CHARACTERIZATION OF
RP   VARIANTS ASP-77; THR-267; TRP-430 AND VAL-525.
RX   PubMed=28719828; DOI=10.1016/j.diabres.2017.06.023;
RA   Winters A., Ramos-Molina B., Jarvela T.S., Yerges-Armstrong L.,
RA   Pollin T.I., Lindberg I.;
RT   "Functional analysis of PCSK2 coding variants: A founder effect in the Old
RT   Order Amish population.";
RL   Diabetes Res. Clin. Pract. 131:82-90(2017).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-424.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Serine endopeptidase which is involved in the processing of
CC       hormone and other protein precursors at sites comprised of pairs of
CC       basic amino acid residues. Responsible for the release of glucagon from
CC       proglucagon in pancreatic A cells. {ECO:0000269|PubMed:28719828,
CC       ECO:0000269|PubMed:9287128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of protein hormones and neuropeptides from their
CC         precursors, generally by hydrolysis of -Lys-Arg-|- bonds.;
CC         EC=3.4.21.94;
CC   -!- INTERACTION:
CC       P16519; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-514360, EBI-18924329;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Secreted
CC       {ECO:0000269|PubMed:28719828}. Note=Localized in the secretion
CC       granules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P16519-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16519-2; Sequence=VSP_043358;
CC       Name=3;
CC         IsoId=P16519-3; Sequence=VSP_045873;
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; J05252; AAA60032.1; -; mRNA.
DR   EMBL; M95971; AAA59919.1; -; Genomic_DNA.
DR   EMBL; M95960; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95961; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95962; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95963; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95964; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95965; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95966; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95967; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95968; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95969; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; M95970; AAA59919.1; JOINED; Genomic_DNA.
DR   EMBL; AK294200; BAG57514.1; -; mRNA.
DR   EMBL; AK312341; BAG35262.1; -; mRNA.
DR   EMBL; AL031664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL121779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10279.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10280.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10281.1; -; Genomic_DNA.
DR   EMBL; BC005815; AAH05815.1; -; mRNA.
DR   EMBL; BC040546; AAH40546.1; -; mRNA.
DR   EMBL; S75955; AAD14202.1; -; Genomic_DNA.
DR   CCDS; CCDS13125.1; -. [P16519-1]
DR   CCDS; CCDS56179.1; -. [P16519-2]
DR   CCDS; CCDS56180.1; -. [P16519-3]
DR   PIR; A45382; KXHUC2.
DR   RefSeq; NP_001188457.1; NM_001201528.1. [P16519-3]
DR   RefSeq; NP_001188458.1; NM_001201529.2. [P16519-2]
DR   RefSeq; NP_002585.2; NM_002594.4. [P16519-1]
DR   AlphaFoldDB; P16519; -.
DR   SMR; P16519; -.
DR   IntAct; P16519; 2.
DR   STRING; 9606.ENSP00000262545; -.
DR   BindingDB; P16519; -.
DR   ChEMBL; CHEMBL2433; -.
DR   DrugBank; DB00030; Insulin human.
DR   GuidetoPHARMACOLOGY; 2383; -.
DR   MEROPS; S08.073; -.
DR   GlyConnect; 1551; 3 N-Linked glycans (1 site).
DR   GlyCosmos; P16519; 3 sites, 3 glycans.
DR   GlyGen; P16519; 3 sites, 3 N-linked glycans (1 site).
DR   iPTMnet; P16519; -.
DR   PhosphoSitePlus; P16519; -.
DR   BioMuta; PCSK2; -.
DR   DMDM; 13124785; -.
DR   EPD; P16519; -.
DR   MassIVE; P16519; -.
DR   PaxDb; 9606-ENSP00000262545; -.
DR   PeptideAtlas; P16519; -.
DR   ProteomicsDB; 3261; -.
DR   ProteomicsDB; 53377; -. [P16519-1]
DR   ProteomicsDB; 53378; -. [P16519-2]
DR   Antibodypedia; 9205; 242 antibodies from 33 providers.
DR   DNASU; 5126; -.
DR   Ensembl; ENST00000262545.7; ENSP00000262545.2; ENSG00000125851.10. [P16519-1]
DR   Ensembl; ENST00000377899.5; ENSP00000367131.1; ENSG00000125851.10. [P16519-3]
DR   Ensembl; ENST00000536609.1; ENSP00000437458.1; ENSG00000125851.10. [P16519-2]
DR   GeneID; 5126; -.
DR   KEGG; hsa:5126; -.
DR   MANE-Select; ENST00000262545.7; ENSP00000262545.2; NM_002594.5; NP_002585.2.
DR   UCSC; uc002wpl.4; human. [P16519-1]
DR   AGR; HGNC:8744; -.
DR   CTD; 5126; -.
DR   DisGeNET; 5126; -.
DR   GeneCards; PCSK2; -.
DR   HGNC; HGNC:8744; PCSK2.
DR   HPA; ENSG00000125851; Tissue enhanced (adrenal gland, retina, thyroid gland).
DR   MIM; 162151; gene.
DR   neXtProt; NX_P16519; -.
DR   OpenTargets; ENSG00000125851; -.
DR   PharmGKB; PA33091; -.
DR   VEuPathDB; HostDB:ENSG00000125851; -.
DR   eggNOG; KOG3526; Eukaryota.
DR   GeneTree; ENSGT00940000156965; -.
DR   HOGENOM; CLU_002976_4_4_1; -.
DR   InParanoid; P16519; -.
DR   OMA; LAKQWHS; -.
DR   OrthoDB; 5474719at2759; -.
DR   PhylomeDB; P16519; -.
DR   TreeFam; TF314277; -.
DR   PathwayCommons; P16519; -.
DR   Reactome; R-HSA-264876; Insulin processing.
DR   SignaLink; P16519; -.
DR   SIGNOR; P16519; -.
DR   BioGRID-ORCS; 5126; 10 hits in 1154 CRISPR screens.
DR   ChiTaRS; PCSK2; human.
DR   GeneWiki; Proprotein_convertase_2; -.
DR   GenomeRNAi; 5126; -.
DR   Pharos; P16519; Tchem.
DR   PRO; PR:P16519; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P16519; Protein.
DR   Bgee; ENSG00000125851; Expressed in islet of Langerhans and 151 other cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR   GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0034230; P:enkephalin processing; ISS:BHF-UCL.
DR   GO; GO:0030070; P:insulin processing; IDA:BHF-UCL.
DR   GO; GO:0034231; P:islet amyloid polypeptide processing; ISS:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:UniProtKB.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IDA:BHF-UCL.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
DR   Genevisible; P16519; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..109
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027065"
FT   CHAIN           110..638
FT                   /note="Neuroendocrine convertase 2"
FT                   /id="PRO_0000027066"
FT   DOMAIN          129..453
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          461..597
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   ACT_SITE        167
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        384
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        225..376
FT                   /evidence="ECO:0000250|UniProtKB:P23188"
FT   DISULFID        317..347
FT                   /evidence="ECO:0000250|UniProtKB:P23188"
FT   DISULFID        468..494
FT                   /evidence="ECO:0000250|UniProtKB:P23188"
FT   VAR_SEQ         1..19
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045873"
FT   VAR_SEQ         60..94
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043358"
FT   VARIANT         77
FT                   /note="A -> D (no effect on secretion; no effect on
FT                   proglucagon processing; dbSNP:rs201718679)"
FT                   /evidence="ECO:0000269|PubMed:28719828"
FT                   /id="VAR_079730"
FT   VARIANT         244
FT                   /note="P -> Q (in dbSNP:rs17854040)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_069075"
FT   VARIANT         267
FT                   /note="A -> T (decreased secretion; reduced proglucagon
FT                   processing; dbSNP:rs144151196)"
FT                   /evidence="ECO:0000269|PubMed:28719828"
FT                   /id="VAR_079731"
FT   VARIANT         424
FT                   /note="D -> N (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs780820865)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036548"
FT   VARIANT         430
FT                   /note="R -> W (no effect on secretion; no effect on
FT                   proglucagon processing; dbSNP:rs200711626)"
FT                   /evidence="ECO:0000269|PubMed:28719828"
FT                   /id="VAR_079732"
FT   VARIANT         484
FT                   /note="K -> E (in dbSNP:rs17857236)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_069076"
FT   VARIANT         525
FT                   /note="M -> V (no effect on secretion; no effect on
FT                   proglucagon processing; dbSNP:rs139619496)"
FT                   /evidence="ECO:0000269|PubMed:28719828"
FT                   /id="VAR_079733"
FT   CONFLICT        283..284
FT                   /note="EL -> DV (in Ref. 1; AAA60032)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   638 AA;  70565 MW;  323623FBDA6086B2 CRC64;
     MKGGCVSQWK AAAGFLFCVM VFASAERPVF TNHFLVELHK GGEDKARQVA AEHGFGVRKL
     PFAEGLYHFY HNGLAKAKRR RSLHHKQQLE RDPRVKMALQ QEGFDRKKRG YRDINEIDIN
     MNDPLFTKQW YLINTGQADG TPGLDLNVAE AWELGYTGKG VTIGIMDDGI DYLHPDLASN
     YNAEASYDFS SNDPYPYPRY TDDWFNSHGT RCAGEVSAAA NNNICGVGVA YNSKVAGIRM
     LDQPFMTDII EASSISHMPQ LIDIYSASWG PTDNGKTVDG PRELTLQAMA DGVNKGRGGK
     GSIYVWASGD GGSYDDCNCD GYASSMWTIS INSAINDGRT ALYDESCSST LASTFSNGRK
     RNPEAGVATT DLYGNCTLRH SGTSAAAPEA AGVFALALEA NLGLTWRDMQ HLTVLTSKRN
     QLHDEVHQWR RNGVGLEFNH LFGYGVLDAG AMVKMAKDWK TVPERFHCVG GSVQDPEKIP
     STGKLVLTLT TDACEGKENF VRYLEHVQAV ITVNATRRGD LNINMTSPMG TKSILLSRRP
     RDDDSKVGFD KWPFMTTHTW GEDARGTWTL ELGFVGSAPQ KGVLKEWTLM LHGTQSAPYI
     DQVVRDYQSK LAMSKKEELE EELDEAVERS LKSILNKN
//