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Database: UniProt
Entry: A0A3B4DCZ4_PYGNA
LinkDB: A0A3B4DCZ4_PYGNA
Original site: A0A3B4DCZ4_PYGNA 
ID   A0A3B4DCZ4_PYGNA        Unreviewed;       800 AA.
AC   A0A3B4DCZ4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Furin, paired basic amino acid cleaving enzyme {ECO:0000313|Ensembl:ENSPNAP00000022297.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000022297.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000022297.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR   AlphaFoldDB; A0A3B4DCZ4; -.
DR   Ensembl; ENSPNAT00000034441.1; ENSPNAP00000022297.1; ENSPNAG00000029710.1.
DR   GeneTree; ENSGT00940000157220; -.
DR   OMA; HNEWTAF; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00064; FU; 1.
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; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_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:SF11; FURIN PRECURSOR; 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   SMART; SM00261; FU; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        668..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          388..520
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          104..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        97
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        312
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   800 AA;  87171 MW;  271477686E7B4A80 CRC64;
     MTEVFGDYYH FQHRRVVKRS LSGHRGVHVR LHSEPQVVWA EQQVAKRRRK RDIYSEPTDP
     KFPQQWYLYN INRRDLHVKE AWAQGFTGRG VVITILDDGI EKDHPDLAQN YDPDASYDVN
     DRDPDPQPRY TQLNDNRHGT RCAGEVAAAA NNGVCGVGVA YNARIGGVRM LDGEVTDVVE
     AQSLSLNSQH IHIYSASWGP EDDGKTVDGP AKLAKEAFLQ GVTEGRGGLG SIFVWASGNG
     GREKDSCNCD GYTNSIYTLS ISSTTQYGNV PWYSEACSST LATTYSSGNL NEKQIVTTDL
     RKKCTDSHTG TSASAPLAAG IIALALEANM NLTWRDMQHL VVRTAHPAHL ITSDWRTNGV
     GRLVSHSYGY GLLDASAMVA LARNWSSVGP QHKCVIDMLT EPREVRNQLL FSKSVEACSG
     QLDFVSSLEH VQARLTLSYS HRGNLAIHLI SPLGTRSTLL APRPQDNSAE GFNDWAFMTT
     HAWDEDPRGE WTLEIENVAG LNDYGVLSQF TLILYGTGSS SADLSASDFS RPSNNSCKTF
     DAQQICIECS AGSSLYLQGC VKACPPGFTS GLQLLNLSLE NWVEQSSVQA CLPCHPACLT
     CSGPGEAECL SCPSHSHLVA TSCLRQNQVQ RKSPAGPTQN VQRGDGSDSD PDLDSDGPSP
     QKGLSSHLPV LVAVLSCAFI LATFAAVFVL LQLHSGAANA SFYRRTKLPV TDSSGRGMRV
     AFGFGLSRDW TSSRVAYRGI PTVWGDEDTA GGMNSESDSE ELDCHRRASW CSHFLSAVLP
     CPGLLREELR SKNTQHCACS
//
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