ID A0A0V1BA38_TRISP Unreviewed; 672 AA.
AC A0A0V1BA38;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Neuroendocrine convertase 2 {ECO:0000313|EMBL:KRY33848.1};
GN Name=PCSK2 {ECO:0000313|EMBL:KRY33848.1};
GN ORFNames=T01_11466 {ECO:0000313|EMBL:KRY33848.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY33848.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY33848.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY33848.1};
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 -!- 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:KRY33848.1}.
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DR EMBL; JYDH01000076; KRY33848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BA38; -.
DR STRING; 6334.A0A0V1BA38; -.
DR InParanoid; A0A0V1BA38; -.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016486; P:peptide hormone processing; IEA:UniProt.
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:UP000054776};
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..672
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006874998"
FT DOMAIN 496..645
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 672 AA; 74975 MW; 7D0C1F08F3B2756D 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 MHRSSRDNCS HFEWQVNGVG LEFNHLFGFG
VLDAAEMVIL AKAWQTVPAR FHCDAGSIWE PQCFRAFDFS VLFSSRIPSS GTLVLEIDTN
ACRGTETEVN YLEHVQAVVS LNSTRRGDVT LYLISPAGTQ SMILSRRPKD DDHTDGFTNW
PFMTTHTWGE GSSGTWRLVV RFQGPNRQAG WINRWTLMLH GTKEQPYSSI QPTSDRQNSK
LQLVQRAHKR TG
//
