ID A0A1I8MU29_MUSDO Unreviewed; 993 AA.
AC A0A1I8MU29;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Furin-like protease 1 {ECO:0000313|RefSeq:XP_011294848.1};
GN Name=101893498 {ECO:0000313|EnsemblMetazoa:MDOA008443-PB};
GN Synonyms=LOC101893498 {ECO:0000313|RefSeq:XP_011294848.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA008443-PB};
RN [1] {ECO:0000313|RefSeq:XP_011294848.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26156588;
RA Li D., Liang Y., Wang X., Wang L., Qi M., Yu Y., Luan Y.;
RT "Transcriptomic Analysis of Musca domestica to Reveal Key Genes of the
RT Prophenoloxidase-Activating System.";
RL G3 (Bethesda) 5:1827-1841(2015).
RN [2] {ECO:0000313|EnsemblMetazoa:MDOA008443-PB}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA008443-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_011294848.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-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_011294848.1; XM_011296546.2.
DR STRING; 7370.A0A1I8MU29; -.
DR EnsemblMetazoa; MDOA008443-RB; MDOA008443-PB; MDOA008443.
DR KEGG; mde:101893498; -.
DR VEuPathDB; VectorBase:MDOA008443; -.
DR eggNOG; KOG3525; Eukaryota.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; 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: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; 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:UP000694905};
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 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 933..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 598..727
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 215..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 523
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 993 AA; 111394 MW; 32CA931BC8AB2EEE CRC64;
MKNDVVRWST QKRRKTYSKL CCNQENKKFP AYCAGEISYN TTFLGSSYAS GSLIQSVRCD
TLYNNIILAE DVNKYGSTNY PERRNWHNYL NEYRHESRRH SSNRKCRSSY WSTLIFEIGI
AIFLCSFQVS LVSCSEFESG SVIDDRSLLH ELDYADKESS FENHYTHTWA VHIPDGDMDS
KADAVAHDNG FVNMGKIFQD HYLFAHHKVA KRSVEPSTNH QSRLDEDGRV TWSKQQIAKS
RRKRDFIRMR PSRTSSRSAS SRVKAMPFTD PKWEHMWYLN RGGDLDMNVI PAWKEGITGK
GIVVTILDDG LESDHPDIIN NYDPKASYDV NSHDEDPMPH YDLADSNRHG TRCAGEVAAT
ANNSICAVGI AFGASVGGVR MLDGDVTDAV EARSLSLNPQ HIDIYSASWG PDDDGKTVDG
PGELASRAFI EGVTKGRAGK GSIFIWASGN GGREMDNCNC DGYTNSIWTL SISSATEDGF
VPWYSEKCSS TLATTYSSGS QAEKQVVTTD LHHSCTVSHT GTSASAPLAA GIAALVLESN
NNLTWRDMQH IVVRTAKPAN LMDPTWSKNG VGRRVSHSFG YGLMDAAAMV KLARQWKTVP
EQQRCEINAP HVDKVIPPKS HITLQLSVKN CLNINFLEHV QAKITLTSQR RGDIQINLIS
PAGTKVTLLT PRVHDTSHSG FNQWPFMSVH TWGESPHGNW QLEIHNEGRY MAQITQWDLI
FYGTEEPAQP DDPVPMATDK FNLVTAEAER NNFDYGSNSQ WRDTPKLGES GMENHDRTNT
SCLKATINLQ CLVCAPPTFF YRGRCYDMCP THTYIARGQL HVDMTYNNLR GQAPDYEELQ
ANDRKKRSRG AEVGETDDDG HTLNSQTAFI CEPCDKSCFN CFGPLSSECK TCYSGSQLKR
RLNTNESYCV NFSERSSGNA IASQRSDRDY RSLLFLVFLV PSVIIILVVL LNKSEIRFNI
CKCQRKAGIE SSVDYRYDRV SLIADEEAQE ELD
//