ID   NEC2_PONAB              Reviewed;         638 AA.
AC   Q5REC2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   02-SEP-2026, entry version 118.
DE   RecName: Full=Neuroendocrine convertase 2;
DE            Short=NEC 2;
DE            EC=3.4.21.94 {ECO:0000250|UniProtKB:P16519};
DE   AltName: Full=Prohormone convertase 2;
DE   AltName: Full=Proprotein convertase 2;
DE            Short=PC2;
DE   Flags: Precursor;
GN   Name=PCSK2; Synonyms=NEC2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Mediates the release of insulin from
CC       proinsulin. {ECO:0000250|UniProtKB:P16519}.
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; Evidence={ECO:0000250|UniProtKB:P16519};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250|UniProtKB:P16519}. Secreted
CC       {ECO:0000250|UniProtKB:P16519}. Note=Localized in the secretion
CC       granules. {ECO:0000250|UniProtKB:P16519}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR857610; CAH89885.1; -; mRNA.
DR   RefSeq; NP_001124879.1; NM_001131407.1.
DR   AlphaFoldDB; Q5REC2; -.
DR   SMR; Q5REC2; -.
DR   FunCoup; Q5REC2; 454.
DR   STRING; 9601.ENSPPYP00000011989; -.
DR   MEROPS; S08.073; -.
DR   GlyCosmos; Q5REC2; 3 sites, No reported glycans.
DR   Ensembl; ENSPPYT00000012461.3; ENSPPYP00000011989.2; ENSPPYG00000010725.3.
DR   GeneID; 100171744; -.
DR   KEGG; pon:100171744; -.
DR   CTD; 5126; -.
DR   eggNOG; KOG3526; Eukaryota.
DR   GeneTree; ENSGT00940000156965; -.
DR   HOGENOM; CLU_002976_4_4_1; -.
DR   InParanoid; Q5REC2; -.
DR   OMA; LAKQWHS; -.
DR   OrthoDB; 300641at2759; -.
DR   Proteomes; UP000001595; Chromosome 20.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0070013; C:intracellular organelle lumen; IEA:UniProtKB-ARBA.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
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; ISS:UniProtKB.
DR   GO; GO:0034230; P:enkephalin processing; IEA:Ensembl.
DR   GO; GO:0030070; P:insulin processing; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR   GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   FunFam; 2.60.120.260:FF:000020; neuroendocrine convertase 2; 1.
DR   FunFam; 3.30.70.850:FF:000003; neuroendocrine convertase 2 isoform X1; 1.
DR   FunFam; 3.40.50.200:FF:000004; Proprotein convertase type 2; 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.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle; Disulfide bond;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..109
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000262584"
FT   CHAIN           110..638
FT                   /note="Neuroendocrine convertase 2"
FT                   /id="PRO_0000262585"
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"
SQ   SEQUENCE   638 AA;  70566 MW;  789B0D2EFD32F396 CRC64;
     MKGGCVSQWK AAAGFLFCVM VFASAERPVF TNHFLVELHK GGEDEARQVA 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
//