ID A0A0Q3UPR8_AMAAE Unreviewed; 789 AA.
AC A0A0Q3UPR8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=furin {ECO:0000256|ARBA:ARBA00038993};
DE EC=3.4.21.75 {ECO:0000256|ARBA:ARBA00038993};
DE AltName: Full=Dibasic-processing enzyme {ECO:0000256|ARBA:ARBA00041232};
DE AltName: Full=Paired basic amino acid residue-cleaving enzyme {ECO:0000256|ARBA:ARBA00042784};
GN ORFNames=AAES_162962 {ECO:0000313|EMBL:KQK73882.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK73882.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK73882.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK73882.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of mature proteins from their proproteins by cleavage
CC of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and
CC Yaa is Arg or Lys. Releases albumin, complement component C3 and von
CC Willebrand factor from their respective precursors.; EC=3.4.21.75;
CC Evidence={ECO:0000256|ARBA:ARBA00035756};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Endosome membrane {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00004530}. Golgi apparatus,
CC trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004393}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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:KQK73882.1}.
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DR EMBL; LMAW01003125; KQK73882.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3UPR8; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:SF1; FURIN; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..789
FT /note="furin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006208345"
FT TRANSMEM 708..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 445..577
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 161..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 789 AA; 86119 MW; 32C5CE478826A8BB CRC64;
MDLRSCSLLL LWTLVVALAL LAQEVLAQRI YTNTWAVLVP AGPQEADRLA RKHGFLNLGL
IFGDYYHFRH SGVVKRSLSP HQPWHSXLAR XPQVQWLEQQ VAKRRTKRDV FMEPTDPKFP
QQWYLYNTNQ RDLNVRQAWE QGYTGKGIVV SILDDGIEKN HPDLEGNYDP GASFDVNDQD
PDPQPRYTQM NDNRHGTRCA GEVAAVANNG ICGVGVAYNA RIGGVRMLDG EVTDAVEAHS
LGLNPNHIHI YSASWGPEDD GKTVDGPARL AEEAFFRGVS QGRGGLGSIF VWASGNGGRE
HDSCNCDGYT NSIYTLSISS TTQYGNVPWY SEACSSTLAT TYSSGNQNEK QIVTTDLRQK
CTESHTGTSA SAPLAAGIIA LALEANKNLT WRDMQHLVVQ TSKPAHLNTN DWVTNGVGRK
VSHSYGYGLL DAGAMVSLAK NWTTVGPQRK CVIDVLTEPK DIGKRLEVRR KVDACLGKAN
YISRLEHAQA RLTLSYNRRG DLAIHLVSPM GTRSTLLAAR PHDFSADGFN DWAFMTTHSW
DEDPSGEWVL EIENTSDANN YGTLTKFTLV LXGTATDSPS LSNQLESSGC KTLTSSQTCV
VCEEGYYLHQ KSCLKHCPPG FAPGVQSTHY ELENSVEPIA PHLCLPCHPS CATCAGPGPN
QCLTCPAHSH FSSLDLSCSH QTQSSRASPA LADGEGLAEA PPPTNLPVLI ASLSCVIIVV
IFVSIFLVLQ ARSGFSLRGV KVYALDSGII SYKGLPSDIW QEEGPSESDG EDNEAHSERT
AFIRDQSAL
//
