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
//