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-MAY-2022, entry version 115.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 bovine
RT 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 residues.
CC Responsible for the release of glucagon from proglucagon in pancreatic
CC A cells (By similarity). {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF186406; AAG17018.1; -; mRNA.
DR RefSeq; NP_776838.1; NM_174413.3.
DR AlphaFoldDB; 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; KOG3526; Eukaryota.
DR InParanoid; Q9GLR0; -.
DR OrthoDB; 308083at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007399; P:nervous system development; ISS:AgBase.
DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; ISS:AgBase.
DR GO; GO:0006508; P:proteolysis; ISS:AgBase.
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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Cytoplasmic vesicle; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..109
FT /evidence="ECO:0000255"
FT /id="PRO_0000244608"
FT CHAIN 110..638
FT /note="Neuroendocrine convertase 2"
FT /id="PRO_0000244609"
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"
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
