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Database: UniProt
Entry: A0A1S3IZZ9_LINUN
LinkDB: A0A1S3IZZ9_LINUN
Original site: A0A1S3IZZ9_LINUN 
ID   A0A1S3IZZ9_LINUN        Unreviewed;       740 AA.
AC   A0A1S3IZZ9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=PC3-like endoprotease variant B {ECO:0000313|RefSeq:XP_013403777.1};
GN   Name=LOC106169035 {ECO:0000313|RefSeq:XP_013403777.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013403777.1};
RN   [1] {ECO:0000313|RefSeq:XP_013403777.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26383154;
RA   Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA   Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT   "The Lingula genome provides insights into brachiopod evolution and the
RT   origin of phosphate biomineralization.";
RL   Nat. Commun. 6:8301-8301(2015).
RN   [2] {ECO:0000313|RefSeq:XP_013403777.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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DR   RefSeq; XP_013403777.1; XM_013548323.2.
DR   AlphaFoldDB; A0A1S3IZZ9; -.
DR   STRING; 7574.A0A1S3IZZ9; -.
DR   EnsemblMetazoa; XM_013548323.2; XP_013403777.1; LOC106169035.
DR   GeneID; 106169035; -.
DR   KEGG; lak:106169035; -.
DR   InParanoid; A0A1S3IZZ9; -.
DR   OrthoDB; 2916537at2759; -.
DR   Proteomes; UP000085678; Unplaced.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 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.
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:UP000085678};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..740
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010360036"
FT   DOMAIN          460..586
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          610..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        382
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   NON_TER         740
FT                   /evidence="ECO:0000313|RefSeq:XP_013403777.1"
SQ   SEQUENCE   740 AA;  81180 MW;  FE422672023AA2E7 CRC64;
     MTTAAIVAIL WCLVTVTTSS GTLDESVQNI DGDTEDGYTN VWAVEIAGGE DVARRLALKH
     GFEHIAKIYD DYYMFEHKDV PDFDRYSSEE KHGTLSSDPE VKWLKQQKVV KRSLFGQTPG
     GTLGVHDDRW RDQEWYLNNT VLGMNIVEAW ERCRTGQGVN VAVVDDGIDY TNYDLARNFD
     LFNSYDMQVD RKTPMPGIAS DSHGTSAAGI IGAEANDFCG VGIAFDANIA GIRIFGNKRI
     TDALEARALT YNMETVDVYS CSWGMARTGF DLKAIGELSK GAMKKGATEG RGGKGSIYVF
     ASGNGGTNDD SCAYDGFANS IYTIPVGGLT HRGRKLPTGE KCSAMMATAY SKSSMEPNRW
     YDKIFTTGYG QWTCADDFGE SSAAAPMVAA VIALALEANP SLTSRDVMHL ITRSARSDFA
     RYDPDSGWFV NGAGFHVSST FGFGLLDAAK MVDFAERWQN VPEQTKCSKQ MTGINGKLPG
     TTTVDFRSCD IKFVEHVEVF VFVYFAGRGY VKMELESPVG TRSLMIPGRK NDLWSRYLEL
     NVSSVQFWGE QGTGDWKVHI GSIYPDQNHT GTLFDLTVNI YGTKDGFPVK LSTTNNNTCN
     QGVVSGFVPT PYPPSRARPT DVHRPTPAPS TTMAPTVTST RQAESTTKKT LFSCRCSFLD
     TIQSYKFRFV SGSVGLEVSC PTDLTTTQYS TCTFISSPLK GWPPGNQACN CSSVDLNKDT
     GTWLVTYPDV EFRLQVLCPV
//
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