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
//