BLI5_HAECO
ID BLI5_HAECO Reviewed; 195 AA.
AC D3GGZ8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Kunitz-type protein bli-5 {ECO:0000305};
DE AltName: Full=Blistered cuticle protein 5 {ECO:0000250|UniProtKB:O62247};
DE AltName: Full=Kunitz-type protease inhibitor bli-5 {ECO:0000250|UniProtKB:O62247};
DE Flags: Precursor;
GN Name=bli-5 {ECO:0000312|EMBL:ACZ64266.1};
GN ORFNames=HCOI_00600900 {ECO:0000312|EMBL:CDL94089.1};
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Haemonchidae; Haemonchus.
OX NCBI_TaxID=6289 {ECO:0000312|EMBL:ACZ64266.1};
RN [1] {ECO:0000312|EMBL:ACZ64266.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=19716386; DOI=10.1016/j.molbiopara.2009.08.005;
RA Stepek G., McCormack G., Page A.P.;
RT "The kunitz domain protein BLI-5 plays a functionally conserved role in
RT cuticle formation in a diverse range of nematodes.";
RL Mol. Biochem. Parasitol. 169:1-11(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHco3(ISE);
RX PubMed=23985316; DOI=10.1186/gb-2013-14-8-r88;
RA Laing R., Kikuchi T., Martinelli A., Tsai I.J., Beech R.N., Redman E.,
RA Holroyd N., Bartley D.J., Beasley H., Britton C., Curran D., Devaney E.,
RA Gilabert A., Hunt M., Jackson F., Johnston S.L., Kryukov I., Li K.,
RA Morrison A.A., Reid A.J., Sargison N., Saunders G.I., Wasmuth J.D.,
RA Wolstenholme A., Berriman M., Gilleard J.S., Cotton J.A.;
RT "The genome and transcriptome of Haemonchus contortus, a key model parasite
RT for drug and vaccine discovery.";
RL Genome Biol. 14:R88.01-R88.16(2013).
CC -!- FUNCTION: Appears to lack serine protease inhibitor activity in vitro
CC when tested with bovine pancreatic alpha-chymotrypsin and elastase. May
CC be involved in cuticle biosynthesis. {ECO:0000269|PubMed:19716386}.
CC -!- CAUTION: Appears to have serine protease activity in vitro
CC (PubMed:19716386). However, it is uncertain if this activity is genuine
CC as bli-5 lacks all the catalytic features of serine proteases.
CC {ECO:0000269|PubMed:19716386, ECO:0000305}.
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DR EMBL; FJ812515; ACZ64266.1; -; Genomic_DNA.
DR EMBL; CAVP010054834; CDL94089.1; -; Genomic_DNA.
DR AlphaFoldDB; D3GGZ8; -.
DR SMR; D3GGZ8; -.
DR WBParaSite; HCON_00022050-00001; HCON_00022050-00001; HCON_00022050.
DR OMA; SREWVCL; -.
DR Proteomes; UP000025227; Unplaced.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..195
FT /note="Kunitz-type protein bli-5"
FT /evidence="ECO:0000255"
FT /id="PRO_5007650919"
FT DOMAIN 120..190
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 120..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 164..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 195 AA; 21543 MW; BC580C8FA00DE536 CRC64;
MKTALLSLIL FSCHIWAVKH QAKKCTEDRE CEEIWPGSTC QRARCRCPEN YVRRKSPSRE
WVCLSVNDAA TGQVGPPLTC PLPDGAGYQV ILRGSSTNNL LSPPVLCSSK TNDCETGYEC
IQGLSPVDGL DGACCPDQIT TCAHPIFDHE SGTLERWGFD GSECVKFKWD PEKPSSANNF
KTKLQCESYC VNIFA
