ID   NEC1_BOVIN              Reviewed;         753 AA.
AC   Q9GLR1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-NOV-2023, entry version 123.
DE   RecName: Full=Neuroendocrine convertase 1;
DE            Short=NEC 1;
DE            EC=3.4.21.93;
DE   AltName: Full=Prohormone convertase 1;
DE   AltName: Full=Proprotein convertase 1;
DE            Short=PC1;
DE   Flags: Precursor;
GN   Name=PCSK1;
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       Substrates include POMC, renin, enkephalin, dynorphin, somatostatin,
CC       insulin and AGRP. {ECO:0000250|UniProtKB:P63239}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of protein hormones, neuropeptides and renin from
CC         their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.;
CC         EC=3.4.21.93;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250}. Note=Localized in the secretion granules. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF186405; AAG17017.1; -; mRNA.
DR   RefSeq; NP_776837.1; NM_174412.2.
DR   AlphaFoldDB; Q9GLR1; -.
DR   SMR; Q9GLR1; -.
DR   STRING; 9913.ENSBTAP00000027775; -.
DR   MEROPS; S08.072; -.
DR   GlyCosmos; Q9GLR1; 2 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000027775; -.
DR   GeneID; 281967; -.
DR   KEGG; bta:281967; -.
DR   CTD; 5122; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   InParanoid; Q9GLR1; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0016486; P:peptide hormone processing; IBA:GO_Central.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 6.10.250.3320; -; 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; IPR022005; Proho_convert.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12177; Proho_convert; 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   Calcium; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..110
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000244606"
FT   CHAIN           111..753
FT                   /note="Neuroendocrine convertase 1"
FT                   /id="PRO_0000244607"
FT   DOMAIN          129..450
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          460..597
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   REGION          617..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        382
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        225..374
FT                   /evidence="ECO:0000250"
FT   DISULFID        317..347
FT                   /evidence="ECO:0000250"
FT   DISULFID        467..494
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   753 AA;  83807 MW;  577AFEACB47B0A59 CRC64;
     MGRRAWTLQC TAFSLFCAWC AMNSVKAKKQ FVNEWAAEIP GGPEAASAIA QELGYDLLGQ
     IGSLENHYLF KHRNHPRRSR RSALHITKRL SDDDRVIWAE QQYEKERSKR SVLRDSALDL
     FNDPMWNQQW YLQDTRMTAT LPKLDLHVIP VWQKGITGKG VVITVLDDGL EWNHTDIYAN
     YDPEASYDFN DNDHDPFPRY DLINENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM
     LDGIVTDAIE ASLIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
     SIFVWASGNG GRQGDNCDCD GYTDSIYTIS INSASQQGLS PWYAEKCSST LATSYSSGDY
     TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
     ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPSTWSS VPEKKECVVK DNDFEPRALK
     ANGEVIIEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE
     RDTSPNGFKN WDFMSVHTWG ENPIGTWTLR IADMSGRIQN EGRIVTWKLI LHGTSSQPEH
     MKQPRVYTSY NTVQNDRRGV EKVVDSGEEQ PTQEGLDENA QASQSPSGSG VGGRRDELAE
     GAPSEAMLRL LQSAFSKNSP SKQSPKKPPS AKPNIPYENF YEALERLNKP SQLKDSEDSL
     YNDYVDGFYN TKPYKHRDDR LLQALVDLLR EEN
//