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Database: UniProt/SWISS-PROT
Entry: NEC1_BOVIN
LinkDB: NEC1_BOVIN
Original site: NEC1_BOVIN 
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   22-NOV-2017, entry version 101.
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;
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. Substrates include POMC, renin, enkephalin, dynorphin,
CC       somatostatin, insulin and AGRP. {ECO:0000250|UniProtKB:P63239}.
CC   -!- CATALYTIC ACTIVITY: Release of protein hormones, neuropeptides and
CC       renin from their precursors, generally by hydrolysis of -Lys-
CC       Arg-|- bonds.
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.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
DR   EMBL; AF186405; AAG17017.1; -; mRNA.
DR   RefSeq; NP_776837.1; NM_174412.2.
DR   UniGene; Bt.5562; -.
DR   ProteinModelPortal; Q9GLR1; -.
DR   SMR; Q9GLR1; -.
DR   STRING; 9913.ENSBTAP00000027775; -.
DR   MEROPS; S08.072; -.
DR   PaxDb; Q9GLR1; -.
DR   PRIDE; Q9GLR1; -.
DR   GeneID; 281967; -.
DR   KEGG; bta:281967; -.
DR   CTD; 5122; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   HOGENOM; HOG000192536; -.
DR   HOVERGEN; HBG008705; -.
DR   InParanoid; Q9GLR1; -.
DR   KO; K01359; -.
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   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_sf.
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; IPR022005; Proho_convert.
DR   InterPro; IPR002884; PrprotnconvertsP.
DR   InterPro; IPR032815; S8_pro-domain.
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; 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   Calcium; Cleavage on pair of basic residues; Complete proteome;
KW   Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   PROPEP       28    110       {ECO:0000255}.
FT                                /FTId=PRO_0000244606.
FT   CHAIN       111    753       Neuroendocrine convertase 1.
FT                                /FTId=PRO_0000244607.
FT   DOMAIN      162    451       Peptidase S8.
FT   DOMAIN      460    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    382    382       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    173    173       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    225    374       {ECO:0000250}.
FT   DISULFID    317    347       {ECO:0000250}.
FT   DISULFID    467    494       {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
//
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