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Database: UniProt
Entry: T1L3Y3_TETUR
LinkDB: T1L3Y3_TETUR
Original site: T1L3Y3_TETUR 
ID   T1L3Y3_TETUR            Unreviewed;       630 AA.
AC   T1L3Y3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
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=107370069 {ECO:0000313|EnsemblMetazoa:tetur37g00120.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur37g00120.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur37g00120.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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}.
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DR   EMBL; CAEY01001062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015793535.1; XM_015938049.1.
DR   AlphaFoldDB; T1L3Y3; -.
DR   STRING; 32264.T1L3Y3; -.
DR   EnsemblMetazoa; tetur37g00120.1; tetur37g00120.1; tetur37g00120.
DR   GeneID; 107370069; -.
DR   KEGG; tut:107370069; -.
DR   eggNOG; KOG3526; Eukaryota.
DR   HOGENOM; CLU_002976_4_4_1; -.
DR   OMA; FHCEAGT; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000015104; 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:UP000015104};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..630
FT                   /note="Neuroendocrine convertase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004592099"
FT   DOMAIN          467..603
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        388
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   630 AA;  70002 MW;  7A5ED19E7F75A591 CRC64;
     MLSSINLIVT LISIICIINC VICNQVFTNS FYVHLNGPYG SDVAHRIAQK HGFINLGPLL
     NSPDEFHFLH RALPHSRTKR SISHTRKLKN DPQVDFAVQQ SGFKRVKRGY RQLILGPEHL
     SLNQEPSDPY FPYQWYLKNV GQNGGKPKLD LNVEAAWAQG YTGKNVTTAI MDDGVDYMHP
     DLRENYNAKA SYDFSSNDPY PYPRYTDDWF NSHGTRCAGE VSAKRDNGIC GVGVAYDSKV
     AGIRMLDQPY MTDLIEANSM GHEPDLIDIY SASWGPTDDG KTVDGPRNAT MRAIVRGVNE
     GRKGLGNIYV WASGDGGQDD DCNCDGYAAS MWTISINSAI NNGENAHYDE SCSSTLASTF
     SNGAKDPHTG VATTDLYGKC TKTHSGTSAA APEAAGVFAL ALEANPNLTW RDIQHLTVLT
     SKRNSLYDSK NRFHWNMNGV GLEFNHLFGF GVLDAGAMVA LASIWKTVPP RYHCEAGSIQ
     KTIPIPSNES LFLHIDTSSC AGKDSEVNYI EHIQAVITLN STRRGDVTLF LISPMGTRSM
     ILSRRPKDDD SRDGFTKWPF MTTHTWSENP RGRWTLEIKF DGDKPQKGFF KEWTLMVHGA
     KEPPYKDLPV LDKNSKLAIV KKAHELAFTH
//
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