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Database: UniProt
Entry: A0A0V0WZ98_9BILA
LinkDB: A0A0V0WZ98_9BILA
Original site: A0A0V0WZ98_9BILA 
ID   A0A0V0WZ98_9BILA        Unreviewed;       659 AA.
AC   A0A0V0WZ98;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Neuroendocrine convertase 2 {ECO:0000256|ARBA:ARBA00039626};
DE            EC=3.4.21.94 {ECO:0000256|ARBA:ARBA00039000};
DE   AltName: Full=Prohormone convertase 2 {ECO:0000256|ARBA:ARBA00042708};
GN   Name=PCSK2 {ECO:0000313|EMBL:KRX81001.1};
GN   ORFNames=T06_8638 {ECO:0000313|EMBL:KRX81001.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81001.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX81001.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX81001.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00036323};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX81001.1}.
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DR   EMBL; JYDK01000035; KRX81001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0WZ98; -.
DR   STRING; 92179.A0A0V0WZ98; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 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; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
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; 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   3: Inferred from homology;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..659
FT                   /note="Neuroendocrine convertase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006872155"
FT   DOMAIN          496..632
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        219
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        394
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   659 AA;  73549 MW;  AE7DAF8DFE817BA1 CRC64;
     MRLFFSFQLF LFCAHPPWIA KGAGAGNAFY TNSFHVHLHS GGQEAAHRLA KRHGFINVGP
     VLRSSNEWHF IQPSLPNIRK KRSIFHHRKL ARDPEVRHVV QQVGFKRAKR GFRNFEQKSA
     QSEDLFPPME SPTDPLYPYQ WYLKNTGQWG GKPNLDLNVE KAWALGYTGK NVTTAIMDDG
     VDYMHPDLKD NFNVAASYDF SGNDPYPYPR YTDDWFNSHG TRCAGEIAAI RGNGVCGVGV
     AYNSKIAGIR MLDQPYMTDL IEANSMSHEP NLIDIYSASW GPTDDGRTVD GPRNATMRAI
     VKGVNEGRHG LGNIFVWASG DGGEDDDCNC DGYASSMWTI SINSAINNGE NAHYDESCSS
     TLASTFSNGG KNRETGVTTT DLYGQCTKSH SGTSAAAPEA AGVFALALEA NPKLTWRDLQ
     HLTVLTSNRN SLFDGRCREI VDLRIPGVRK MHRFSRDNCS HFEWQVNGVG LEFNHLFGFG
     VLDAAEMVIL AKAWQTVPAR FHCDAGSIWE PHRIPSSGTL VLEINTNACR GTETEVNYLE
     HVQAVISLNS TRRGDVTLYL ISPAGTQSMI LSRRPKDDDH TDGFTNWPFM TTHTWGEGSS
     GTWRLVVRFQ GPNRQAGWIN RWTLMLHGTK EQPYSSIQPT SDRQNSKLQL VQRAHKRTG
//
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