ID A0A3Q1EW32_9TELE Unreviewed; 794 AA.
AC A0A3Q1EW32;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Furin, paired basic amino acid cleaving enzyme {ECO:0000313|Ensembl:ENSAPOP00000008022.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000008022.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000008022.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1EW32; -.
DR Ensembl; ENSAPOT00000003938.1; ENSAPOP00000008022.1; ENSAPOG00000010191.1.
DR GeneTree; ENSGT00940000157220; -.
DR Proteomes; UP000257200; 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}; Reference proteome {ECO:0000313|Proteomes:UP000257200};
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 686..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 398..531
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 121..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 322
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 794 AA; 86430 MW; 1C01ED1A9D7F2E09 CRC64;
MAWARTGQSR MRDVFGDYYH FRHHAVEKRA LSGHKGMHIR LQKEPQVLWA EQQVVRKRKK
RDVYDNPTDP DFPKQWYLST PTHQDLNTKA AWAQGYTGRG VVVTILDDGI EKDHPDLISN
YDPEASYDVN DGDADPQPRY TQRNENRHGT RCAGEVAAAA NNDVCGVGVA YNAKIGGVRM
LDGEVTDVVE AHSLSLNPQH IHIYSASWGP EDDGKSLDGP AKLAKEAFLQ GITKGRSGLG
SIFVWASGNG GREQDSCNCD GYTNSIYTLS ISSTTQSGNV PWYSEPCSST LATTFSSGNP
GEKQIVTTDL RQKCTDSHTG TSASAPLAAG IIALALEANM NLTWRDMQHL VVRTSQPRHL
SAGDWKTNGV GRRVSHSYGY GLLDAGAIVG LAQNWTTVGP QHQCVNTMLT EPRDIGNKLV
FSKSVDACWG RPEYVSSLEH VQARLTLSHN QRGKLAIHLI SPLGTRSTLL FPRPNDFSSE
GFNDWAFMTT HSWDEDPQGE WTLEIENVAA NGRDYGVLSQ FTLILWGTGP SVVNPSSPDF
PRPSNNSCKT FDAQQICIEC SPGFSLFLQG CVKLCPPGFT SGQQLLNLSL ENWVDLSSVQ
ACLPCNPACL TCSGTGPTDC LSCPSHSHLV LTSCLHQNQV QRKSPLSGGL QVDGAQPEGE
SPAAADHHSG ETEEPPGLGV APSTQLPVVV AVLSCAFILA AFVGVFLLLQ IRSGGAAFGW
RTKLPSGYSD TRGVRVGFGF GFRQGRERKA RICYKGIPTV WADEDMIAYE SESDSEEVDG
HSERTAFIKT QSLI
//
