ID A0A0V0UUJ0_9BILA Unreviewed; 655 AA.
AC A0A0V0UUJ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Furin {ECO:0000313|EMBL:KRX54663.1};
DE Flags: Fragment;
GN ORFNames=T09_12004 {ECO:0000313|EMBL:KRX54663.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX54663.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX54663.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX54663.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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:KRX54663.1}.
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DR EMBL; JYDN01000164; KRX54663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UUJ0; -.
DR STRING; 181606.A0A0V0UUJ0; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; 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:SF3; FURIN-LIKE PROTEASE 1, ISOFORMS 1_1-X_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}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054681};
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 634..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..608
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX54663.1"
SQ SEQUENCE 655 AA; 72730 MW; 8CDBC570CB32BD34 CRC64;
LYEMLHSPLV STFFGLLYLA LSRGTVARVY SNQWAVEVVG GPAVADALAS KHGFVNLGSI
FGNFYLYSHS KIRKRSVRPA RTSQKALRSE PQILWVEQQV VKKRVKRDVP MTIDPPTPKQ
ATPGFYSSCL TNSSNTFCQY TVNDPEWPKM WYLNRGKGLD HNVREAWELG YTGKNVVVTI
LDDGLEWTHP DIEPNYDPKA SFDLNERDAD PMPRYEPTNE NRHGTRCAGE VAAVLNNTLC
IVGIAYHAGI GGIRMLDGEV NDAIEASSLS YNRQHIDIYS ASWGPDDNGK TLDGPDRMAS
LAFQEGVREG RGGKGSIFVW ASGNGGRDSD SCNCDGYTNS IYTLSISSAT ENGRVPWYSE
ACSSTLATTY SSGSNNDKMI VTTDLHHGCT SFHTGTSASA PLAAGICALT LEANPDLTWR
DMQHIVVRTA RPEGLTANDW SVNGVGRSVS HSFGYGLMDA GAMVRLARNW TNVSEQHQCR
TLYRLSRKGK TIPKESIVKM RMVTDGCFND PKRKVAYLEH VQSYITLTSR KRGNLLIFLT
SPSGTKSTLL PRRNHDTTPD GIRNWAFMTT HSWGEKAEGR WTLEIQNDNL DEAHLLKWEL
VLYGTDQPVG PYGLEEEDNL SSSSSSSAKF TRPFAYFILN IFSICFGYFV AHLLK
//