NEC2_HUMAN
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 03-AUG-2022, entry version 204.
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: Involved in the processing of hormone and other protein
CC precursors at sites comprised of pairs of basic amino acid residues.
CC Responsible for the release of glucagon from proglucagon in pancreatic
CC A cells. {ECO:0000269|PubMed:28719828, 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 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; P16519; -.
DR PeptideAtlas; P16519; -.
DR PRIDE; P16519; -.
DR ProteomicsDB; 3261; -.
DR ProteomicsDB; 53377; -. [P16519-1]
DR ProteomicsDB; 53378; -. [P16519-2]
DR Antibodypedia; 9205; 220 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 CTD; 5126; -.
DR DisGeNET; 5126; -.
DR GeneCards; PCSK2; -.
DR HGNC; HGNC:8744; PCSK2.
DR HPA; ENSG00000125851; Tissue enhanced (adrenal gland, brain, 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; PFMTDVI; -.
DR OrthoDB; 308083at2759; -.
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 1078 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 150 other tissues.
DR Genevisible; P16519; HS.
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:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:BHF-UCL.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 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 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; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 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.
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"
FT DISULFID 317..347
FT /evidence="ECO:0000250"
FT DISULFID 468..494
FT /evidence="ECO:0000250"
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
