BLI_ONCVO
ID BLI_ONCVO Reviewed; 693 AA.
AC A0A044RE18; Q7Z0F0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Endoprotease bli {ECO:0000305};
DE EC=3.4.21.75 {ECO:0000269|PubMed:12855702};
DE AltName: Full=Blisterase {ECO:0000303|PubMed:12855702};
DE Flags: Precursor;
GN Name=Bli {ECO:0000303|PubMed:12855702};
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282 {ECO:0000312|Proteomes:UP000024404};
RN [1] {ECO:0000312|EMBL:AAO12507.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=12855702; DOI=10.1074/jbc.m302601200;
RA Poole C.B., Jin J., McReynolds L.A.;
RT "Cloning and biochemical characterization of blisterase, a subtilisin-like
RT convertase from the filarial parasite, Onchocerca volvulus.";
RL J. Biol. Chem. 278:36183-36190(2003).
RN [2] {ECO:0000312|Proteomes:UP000024404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA Berriman M.;
RT "Genome sequencing of Onchocerca volvulus.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R
CC consensus motif. {ECO:0000269|PubMed:12855702}.
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:0000269|PubMed:12855702};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12855702};
CC Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958};
CC -!- ACTIVITY REGULATION: Inhibited by the propeptide before the second
CC cleavage. Inhibited by ethylenediaminetetraacetic acid (EDTA), ZnSO(4)
CC and chloroketone DEC-RVKR-CMK. {ECO:0000269|PubMed:12855702}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. Active from pH 7.0 to 8.5.
CC {ECO:0000269|PubMed:12855702};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12855702}.
CC -!- PTM: The inhibition peptide, which plays the role of an intramolecular
CC chaperone, is probably autocatalytically removed in the endoplasmic
CC reticulum (ER) and remains non-covalently bound as a potent
CC autoinhibitor. Probably following transport to the trans Golgi, a
CC second cleavage within the inhibition propeptide results in propeptide
CC dissociation and bli activation. {ECO:0000269|PubMed:12855702}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
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DR EMBL; AY157026; AAO12507.1; -; mRNA.
DR EMBL; CBVM010000012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A044RE18; -.
DR SMR; A0A044RE18; -.
DR STRING; 6282.A0A044RE18; -.
DR MEROPS; S08.031; -.
DR EnsemblMetazoa; OVOC11771; OVOC11771; WBGene00248580.
DR OMA; FHDWSLL; -.
DR Proteomes; UP000024404; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090472; P:dibasic protein processing; IDA:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 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 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; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 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 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..116
FT /note="Inhibition peptide"
FT /evidence="ECO:0000305|PubMed:12855702"
FT /id="PRO_0000439880"
FT CHAIN 117..693
FT /note="Endoprotease bli"
FT /evidence="ECO:0000305|PubMed:12855702"
FT /id="PRO_5004295169"
FT DOMAIN 167..482
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 490..628
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 215..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 414
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 299..304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 338..341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT SITE 84..85
FT /note="Cleavage, second; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT SITE 116..117
FT /note="Cleavage, first; by autolysis"
FT /evidence="ECO:0000305|PubMed:12855702"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 257..406
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 349..379
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 497..526
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT CONFLICT 661..693
FT /note="EKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV -> VHGPQSFFFSFLCLY
FT NS (in Ref. 1; AAO12507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 76800 MW; B593B7670ED4B94F CRC64;
MYWQLVRILV LFDCLQKILA IEHDSICIAD VDDACPEPSH TVMRLRERND KKAHLIAKQH
GLEIRGQPFL DGKSYFVTHI SKQRSRRRKR EIISRLQEHP DILSIEEQRP RVRRKRDFLY
PDIAHELAGS STNIRHTGLI SNTEPRIDFI QHDAPVLPFP DPLYKEQWYL NNGAQGGFDM
NVQAAWLLGY AGRNISVSIL DDGIQRDHPD LAANYDPLAS TDINGHDDDP TPQDDGDNKH
GTRCAGEVAS IAGNVYCGVG VAFHAKIGGV RMLDGPVSDS VEAASLSLNR HHIDIYSASW
GPEDDGRTFD GPGPLAREAF YRGVKAGRGG KGSIFVWASG NGGSRQDSCS ADGYTTSVYT
LSVSSATIDN RSPWYLEECP STIATTYSSA NMNQPAIITV DVPHGCTRSH TGTSASAPLA
AGIIALALEA NPNLTWRDMQ HIVLRTANPV PLLNNPGWSV NGVGRRINNK FGYGLMDAGA
LVKLALIWKT VPEQHICTYD YKLEKPNPRP ITGNFQMNFS LEVNGCESGT PVLYLEHVQV
LATFRFGKRG DLKLTLFSPR GTSSVLLPPR PQDFNSNGIH KWPFLSVQTW GEDPRGKWTL
MVESVSTNRN VGGTFHDWSL LLYGTAEPAQ PNDPRHSSVV PSSVSAESPF DRITQHIASQ
EKKKKQRDSR DWQPKKVENK KSLLVSAQPE LRV
