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Database: UniProt/SWISS-PROT
Entry: NEC2_BOVIN
LinkDB: NEC2_BOVIN
Original site: NEC2_BOVIN 
ID   NEC2_BOVIN              Reviewed;         638 AA.
AC   Q9GLR0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-OCT-2017, entry version 98.
DE   RecName: Full=Neuroendocrine convertase 2;
DE            Short=NEC 2;
DE            EC=3.4.21.94;
DE   AltName: Full=Prohormone convertase 2;
DE   AltName: Full=Proprotein convertase 2;
DE            Short=PC2;
DE   Flags: Precursor;
GN   Name=PCSK2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal medulla;
RX   PubMed=10945231; DOI=10.1089/10445490050085906;
RA   Hwang S.-R., Ng S.-M., Steineckert B., Seidah N.G., Hook V.Y.H.;
RT   "Molecular cloning demonstrates structural features of homologous
RT   bovine prohormone convertases 1 and 2.";
RL   DNA Cell Biol. 19:409-419(2000).
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Release of protein hormones and neuropeptides
CC       from their precursors, generally by hydrolysis of -Lys-
CC       Arg-|- bonds.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250}. Note=Localized in the secretion granules.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
DR   EMBL; AF186406; AAG17018.1; -; mRNA.
DR   RefSeq; NP_776838.1; NM_174413.3.
DR   UniGene; Bt.5563; -.
DR   ProteinModelPortal; Q9GLR0; -.
DR   SMR; Q9GLR0; -.
DR   STRING; 9913.ENSBTAP00000050841; -.
DR   MEROPS; S08.073; -.
DR   PaxDb; Q9GLR0; -.
DR   PRIDE; Q9GLR0; -.
DR   GeneID; 281968; -.
DR   KEGG; bta:281968; -.
DR   CTD; 5126; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; KOG3526; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   HOGENOM; HOG000192536; -.
DR   HOVERGEN; HBG008705; -.
DR   InParanoid; Q9GLR0; -.
DR   KO; K01360; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; ISS:AgBase.
DR   GO; GO:0016486; P:peptide hormone processing; ISS:AgBase.
DR   GO; GO:0016540; P:protein autoprocessing; ISS:AgBase.
DR   GO; GO:0006508; P:proteolysis; ISS:AgBase.
DR   CDD; cd04059; Peptidases_S8_Protein_converta; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR009020; Peptidase/Inhibitor_I9.
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; IPR002884; PrprotnconvertsP.
DR   InterPro; IPR032815; S8_pro-domain.
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   SUPFAM; SSF54897; SSF54897; 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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Cytoplasmic vesicle; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   PROPEP       26    109       {ECO:0000255}.
FT                                /FTId=PRO_0000244608.
FT   CHAIN       110    638       Neuroendocrine convertase 2.
FT                                /FTId=PRO_0000244609.
FT   DOMAIN      162    453       Peptidase S8.
FT   DOMAIN      461    597       P/Homo B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01173}.
FT   ACT_SITE    167    167       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    208    208       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    384    384       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    375    375       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    514    514       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    524    524       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   638 AA;  70247 MW;  DFF114AD9EC2AE68 CRC64;
     MRGGCISQGK AAAGLLFCVM VFASAERPVF TNHFLVELHR GGEEKARQVA AEHGFGVRKL
     PFAEGLYHFY HNGLAKARRR RSLQHQQQLE RDPRVKRALQ QEGFNRKKRG YRDINEIDIN
     VNDPLFTKQW YLINTGQADG TPGLDLNVAE AWELGYTGKG VTIGIMDDGI DYLHPDLASN
     YNAEASYDFS SNDPYPYPRY TDDWSNSHGT RCAGEVSAAA NNNICGVGVA YGSKVAGIRM
     LDQPFMTDII EASSISHMPQ LIDIYSASWG PTDNGKTVDG PRELTLQAMA DGVNKGRGGK
     GSIYVWASGD GGSYDDCNCD GYASSMWTIS INSAINDGRT ALYDESCSST LASTFSNGRK
     RNPEAGVATT DLYGNCTLRH SGTSAAAPEA AGVFALALEA NLGLTWRDMQ HLTVLTSKRN
     QLHDEVHQWR RNGVGLEFNH LFGYGVLDAG AMVKMAKDWK TVPERFHCVG GSVQNPEKIP
     TTGKPVLTLT TDACEGKENF VRYLEHVQAV VTVNATRRGD LNINMTSPMG TKSILLSRRP
     RGDDAKVGFD KWPFMTTHTW GEDARGTWIL ELGFVGSAPQ KGVLMEWTLM LHGTQSAPYI
     DQVVRDYQSK LAMSKKEELE EELDEAVQRS LKSILGKD
//
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