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Neuroendocrine convertase 2 (NEC 2) (EC 3.4.21.94) (KEX2-like endoprotease 2) (Prohormone convertase 2) (Proprotein convertase 2) (PC2)

 NEC2_RAT                Reviewed;         637 AA.
P28841;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=Neuroendocrine convertase 2;
Short=NEC 2;
EC=3.4.21.94;
AltName: Full=KEX2-like endoprotease 2;
AltName: Full=Prohormone convertase 2;
AltName: Full=Proprotein convertase 2;
Short=PC2;
Flags: Precursor;
Name=Pcsk2; Synonyms=Nec-2, Nec2, Rpc2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1791845; DOI=10.1210/mend-5-12-2014;
Bloomquist B.T., Eipper B.A., Mains R.E.;
"Prohormone-converting enzymes: regulation and evaluation of function
using antisense RNA.";
Mol. Endocrinol. 5:2014-2024(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1954888; DOI=10.1210/endo-129-6-3053;
Hakes D.J., Birch N.P., Mezey A., Dixon J.E.;
"Isolation of two complementary deoxyribonucleic acid clones from a
rat insulinoma cell line based on similarities to Kex2 and furin
sequences and the specific localization of each transcript to
endocrine and neuroendocrine tissues in rats.";
Endocrinology 129:3053-3063(1991).
-!- FUNCTION: Involved in the processing of hormone and other protein
precursors at sites comprised of pairs of basic amino acid
residues. Responsible for the release of glucagon from proglucagon
in pancreatic A cells (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Release of protein hormones and neuropeptides
from their precursors, generally by hydrolysis of -Lys-
Arg-|- bonds.
-!- INTERACTION:
P27682:Scg5; NbExp=4; IntAct=EBI-988244, EBI-988232;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
Note=Localized in the secretion granules.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
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EMBL; M76706; AAA40946.1; -; mRNA.
EMBL; M83746; AAA41477.1; -; mRNA.
PIR; B41556; KXRTC2.
RefSeq; NP_036878.1; NM_012746.1.
UniGene; Rn.89052; -.
ProteinModelPortal; P28841; -.
SMR; P28841; -.
IntAct; P28841; 3.
STRING; 10116.ENSRNOP00000007249; -.
MEROPS; S08.073; -.
PhosphoSitePlus; P28841; -.
UniCarbKB; P28841; -.
PaxDb; P28841; -.
PRIDE; P28841; -.
Ensembl; ENSRNOT00000007249; ENSRNOP00000007249; ENSRNOG00000005438.
GeneID; 25121; -.
KEGG; rno:25121; -.
UCSC; RGD:3273; rat.
CTD; 5126; -.
RGD; 3273; Pcsk2.
eggNOG; KOG3525; Eukaryota.
eggNOG; KOG3526; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; P28841; -.
KO; K01360; -.
OMA; PQRGVLK; -.
OrthoDB; EOG091G05HI; -.
PhylomeDB; P28841; -.
TreeFam; TF314277; -.
Reactome; R-RNO-264876; Insulin processing.
PRO; PR:P28841; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000005438; -.
Genevisible; P28841; RN.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:BHF-UCL.
GO; GO:0034230; P:enkephalin processing; ISO:RGD.
GO; GO:0030070; P:insulin processing; ISO:RGD.
GO; GO:0034231; P:islet amyloid polypeptide processing; IMP:BHF-UCL.
GO; GO:0007399; P:nervous system development; ISO:RGD.
GO; GO:0016486; P:peptide hormone processing; IMP:RGD.
GO; GO:0016540; P:protein autoprocessing; ISO:RGD.
GO; GO:0016485; P:protein processing; ISO:RGD.
GO; GO:0006508; P:proteolysis; IMP:RGD.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR002884; PrprotnconvertsP.
InterPro; IPR032815; S8_pro-domain.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
Protease; Reference proteome; Serine protease; Signal; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 108 {ECO:0000255}.
/FTId=PRO_0000027071.
CHAIN 109 637 Neuroendocrine convertase 2.
/FTId=PRO_0000027072.
DOMAIN 161 452 Peptidase S8.
DOMAIN 460 596 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
ACT_SITE 166 166 Charge relay system. {ECO:0000250}.
ACT_SITE 207 207 Charge relay system. {ECO:0000250}.
ACT_SITE 383 383 Charge relay system. {ECO:0000250}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 523 523 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 224 375 {ECO:0000250}.
DISULFID 316 346 {ECO:0000250}.
DISULFID 467 493 {ECO:0000250}.
CONFLICT 320 320 G -> GI (in Ref. 2; AAA41477).
{ECO:0000305}.
CONFLICT 342 342 Y -> H (in Ref. 2; AAA41477).
{ECO:0000305}.
SEQUENCE 637 AA; 70753 MW; 45DCB85B2CDA4B19 CRC64;
MEGGCGSQWK AAGLLFCVMV FASAERPVFT NHFLVELHKD GEEEARQVAA EHGFGVRKLP
FAEGLYHFYH NGLAKAKRRR SLHHKRQLER DPRIKMALQQ EGFDRKKRGY RDINEIDINM
NDPLFTKQWY LFNTGQADGT PGLDLNVAEA WELGYTGKGV TIGIMDDGID YLHPDLAYNY
NSDASYDFSS NDPYPYPRYT DDWFNSHGTR CAGEVSAAAS NNICGVGVAY NSKVAGIRML
DQPFMTDIIE ASSISHMPQL IDIYSASWGP TDNGKTVDGP RELTLQAMAD GVNKGRGGKG
SIYVWASGDG GSYDDCNCDG YASSMWTISI NSAINDGRTA LYDESCSSTL ASTFSNGRKR
NPEAGVATTD LYGNCTLRHS GTSAAAPEAA GVFALALEAN VDLTWRDMQH LTVLTSKRNQ
LHDEVHQWRR NGVGLEFNHL FGYGVLDAGA MVKMAKDWKT VPERFHCVGG SVQNPEKIPP
TGKLVLTLQT NACEGKENFV RYLEHVQAVI TVNATRRGDL NINMTSPMGT KSILLSRRPR
DDDSKVGFDK WPFMTTHTWG EDARGTWTLE LGFVGSAPQK GLLKEWTLML HGTQSAPYID
QVVRDYQSKL AMSKKQELEE ELDEAVERSL QSILRKN


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