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Database: UniProt/SWISS-PROT
Entry: NEC1_MUSCO
LinkDB: NEC1_MUSCO
Original site: NEC1_MUSCO 
ID   NEC1_MUSCO              Reviewed;         753 AA.
AC   P63240; P21662; P22546;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JAN-2019, entry version 85.
DE   RecName: Full=Neuroendocrine convertase 1;
DE            Short=NEC 1;
DE            EC=3.4.21.93;
DE   AltName: Full=Furin homolog;
DE   AltName: Full=PC3;
DE   AltName: Full=Prohormone convertase 1;
DE   AltName: Full=Propeptide-processing protease;
DE   AltName: Full=Proprotein convertase 1;
DE            Short=PC1;
DE   Flags: Precursor;
GN   Name=Pcsk1; Synonyms=Att-1, Nec-1, Nec1;
OS   Mus cookii (Cook's mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1988934; DOI=10.1073/pnas.88.2.340;
RA   Smeekens S.P., Avruch A.S., Lamendola J., Chan S.J., Steiner D.F.;
RT   "Identification of a cDNA encoding a second putative prohormone
RT   convertase related to PC2 in AtT20 cells and islets of Langerhans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:340-344(1991).
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:
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC       Note=Localized in the secretion granules.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
DR   EMBL; M58507; AAA39896.1; -; mRNA.
DR   ProteinModelPortal; P63240; -.
DR   SMR; P63240; -.
DR   MEROPS; S08.072; -.
DR   PRIDE; P63240; -.
DR   KEGG; ag:AAA39896; -.
DR   MGI; MGI:97511; Pcsk1.
DR   HOVERGEN; HBG008705; -.
DR   KO; K01359; -.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
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   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   CDD; cd04059; Peptidases_S8_Protein_converta; 1.
DR   Gene3D; 2.60.120.260; -; 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; IPR022005; Proho_convert.
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; 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   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; Cytoplasmic vesicle;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   PROPEP       28    110       {ECO:0000255}.
FT                                /FTId=PRO_0000027061.
FT   CHAIN       111    753       Neuroendocrine convertase 1.
FT                                /FTId=PRO_0000027062.
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    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    645    645       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;  84147 MW;  95B78441BE8BD9CD CRC64;
     MEQRGWTLQC TAFAFFCVWC ALSSVKAKRQ FVNEWAAEIP GGQEAASAIA EELGYDLLGQ
     IGSLENHYLF KHKSHPRRSR RSALHITKRL SDDDRVTWAE QQYEKERSKR SVQKDSALDL
     FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWEKGITGKG VVITVLDDGL EWNHTDIYAN
     YDPEASYDFN DNDHDPFPRY DLTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM
     LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
     SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
     TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
     ASNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECVVK DNNFEPRALK
     ANGEVIVEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAVG TSTVLLAERE
     RDTSPNGFKN WDFMSVHTWG ENPVGTWTLK ITDMSGRMQN EGRIVNWKLI LHGTSSQPEH
     MKQPRVYTSY NTVQNDRRGV EKMVNVVEKR PTQKSLNGNL LVPKNSSSSN VEGRRDEQVQ
     GTPSKAMLRL LQSAFSKNAL SKQSPKKSPS AKLSIPYESF YEALEKLNKP SKLEGSEDSL
     YSDYVDVFYN TKPYKHRDDR LLQALMDILN EEN
//
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