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Database: UniProt/SWISS-PROT
Entry: NEC2_MOUSE
LinkDB: NEC2_MOUSE
Original site: NEC2_MOUSE 
ID   NEC2_MOUSE              Reviewed;         637 AA.
AC   P21661; Q80WU1;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   05-DEC-2018, entry version 170.
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=Nec-2, Nec2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=2169760; DOI=10.1089/dna.1990.9.415;
RA   Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
RA   Chretien M.;
RT   "cDNA sequence of two distinct pituitary proteins homologous to Kex2
RT   and furin gene products: tissue-specific mRNAs encoding candidates for
RT   pro-hormone processing proteinases.";
RL   DNA Cell Biol. 9:415-424(1990).
RN   [2]
RP   ERRATUM.
RX   PubMed=2264933; DOI=10.1089/dna.1990.9.789;
RA   Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
RA   Chretien M.;
RL   DNA Cell Biol. 9:789-789(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in the processing of hormone and other protein
CC       precursors at sites comprised of pairs of basic amino acid
CC       residues. Responsible for the release of glucagon from proglucagon
CC       in pancreatic A cells (By similarity).
CC       {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;
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}.
DR   EMBL; M55669; AAA39376.1; -; mRNA.
DR   EMBL; BC052013; AAH52013.2; -; mRNA.
DR   EMBL; BC057348; AAH57348.1; -; mRNA.
DR   CCDS; CCDS16810.1; -.
DR   PIR; B35571; KXMSC2.
DR   RefSeq; NP_032818.1; NM_008792.4.
DR   UniGene; Mm.294493; -.
DR   UniGene; Mm.447466; -.
DR   ProteinModelPortal; P21661; -.
DR   SMR; P21661; -.
DR   IntAct; P21661; 1.
DR   MINT; P21661; -.
DR   STRING; 10090.ENSMUSP00000028905; -.
DR   MEROPS; S08.073; -.
DR   iPTMnet; P21661; -.
DR   PhosphoSitePlus; P21661; -.
DR   PaxDb; P21661; -.
DR   PeptideAtlas; P21661; -.
DR   PRIDE; P21661; -.
DR   Ensembl; ENSMUST00000028905; ENSMUSP00000028905; ENSMUSG00000027419.
DR   GeneID; 18549; -.
DR   KEGG; mmu:18549; -.
DR   UCSC; uc008mqf.2; mouse.
DR   CTD; 5126; -.
DR   MGI; MGI:97512; Pcsk2.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; KOG3526; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   GeneTree; ENSGT00940000156965; -.
DR   HOVERGEN; HBG008705; -.
DR   InParanoid; P21661; -.
DR   KO; K01360; -.
DR   OMA; PQRGVLK; -.
DR   OrthoDB; EOG091G05HI; -.
DR   TreeFam; TF314277; -.
DR   PMAP-CutDB; P21661; -.
DR   PRO; PR:P21661; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000027419; Expressed in 158 organ(s), highest expression level in islet of Langerhans.
DR   CleanEx; MM_PCSK2; -.
DR   ExpressionAtlas; P21661; baseline and differential.
DR   Genevisible; P21661; MM.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0034230; P:enkephalin processing; IDA:BHF-UCL.
DR   GO; GO:0030070; P:insulin processing; ISO:MGI.
DR   GO; GO:0034231; P:islet amyloid polypeptide processing; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IEP:HGNC.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
DR   GO; GO:0016540; P:protein autoprocessing; IDA:HGNC.
DR   GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR   GO; GO:0006508; P:proteolysis; IMP:MGI.
DR   CDD; cd04059; Peptidases_S8_Protein_converta; 1.
DR   Gene3D; 2.60.120.260; -; 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; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25    108       {ECO:0000255}.
FT                                /FTId=PRO_0000027067.
FT   CHAIN       109    637       Neuroendocrine convertase 2.
FT                                /FTId=PRO_0000027068.
FT   DOMAIN      161    452       Peptidase S8.
FT   DOMAIN      460    596       P/Homo B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01173}.
FT   ACT_SITE    166    166       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    207    207       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    383    383       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    374    374       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    513    513       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    523    523       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    224    375       {ECO:0000250}.
FT   DISULFID    316    346       {ECO:0000250}.
FT   DISULFID    467    493       {ECO:0000250}.
SQ   SEQUENCE   637 AA;  70785 MW;  B69F2DCCD00FB0E6 CRC64;
     MEGGCGSQWK AAGFLFCVMV FASAERPVFT NHFLVELHKD GEEEARQVAA EHGFGVRKLP
     FAEGLYHFYH NGLAKAKRRR SLHHKRQLER DPRIKMALQQ EGFDRKKRGY RDINEIDINM
     NDPLFTKQWY LFNTGQADGT PGLDLNVAEA WELGYTGKGV TIGIMDDGID YLHPDLAYNY
     NADASYDFSS NDPYPYPRYT DDWFNSHGTR CAGEVSAAAS NNICGVGVAY NSKVAGIRML
     DQPFMTDIIE ASSISHMPQL IDIYSASWGP TDNGKTVDGP RELTLQAMAD GVNKGRGGKG
     SIYVWASGDG GSYDDCNCDG YASSMWTISI NSAINDGRTA LYDESCSSTL ASTFSNGRKR
     NPEAGVATTD LYGNCTLRHS GTSAAAPEAA GVFALALEAN LDLTWRDMQH LTVLTSKRNQ
     LHDEVHQWRR NGVGLEFNHL FGYGVLDAGA MVKMAKDWKT VPERFHCVGG SVQNPEKIPP
     TGKLVLTLKT NACEGKENFV RYLEHVQAVI TVNATRRGDL NINMTSPMGT KSILLSRRPR
     DDDSKVGFDK WPFMTTHTWG EDARGTWTLE LGFVGSAPQK GLLKEWTLML HGTQSAPYID
     QVVRDYQSKL AMSKKQELEE ELDEAVERSL QSILRKN
//
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