BLI5_CAEEL
ID BLI5_CAEEL Reviewed; 202 AA.
AC O62247;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Kunitz-type protein bli-5 {ECO:0000305};
DE AltName: Full=Blistered cuticle protein 5 {ECO:0000312|WormBase:F45G2.5};
DE AltName: Full=Kunitz-type protease inhibitor bli-5 {ECO:0000303|PubMed:16500660};
DE Flags: Precursor;
GN Name=bli-5 {ECO:0000312|WormBase:F45G2.5};
GN ORFNames=F45G2.5 {ECO:0000312|WormBase:F45G2.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP SER-56.
RX PubMed=16500660; DOI=10.1016/j.ijpara.2006.01.004;
RA Page A.P., McCormack G., Birnie A.J.;
RT "Biosynthesis and enzymology of the Caenorhabditis elegans cuticle:
RT identification and characterization of a novel serine protease inhibitor.";
RL Int. J. Parasitol. 36:681-689(2006).
RN [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Appears to lack serine protease inhibitor activity in vitro
CC when tested with bovine pancreatic alpha-chymotrypsin and elastase
CC (PubMed:19716386). Involved in cuticle biosynthesis (PubMed:16500660,
CC PubMed:19716386). {ECO:0000269|PubMed:16500660,
CC ECO:0000269|PubMed:19716386}.
CC -!- TISSUE SPECIFICITY: Expressed in larval and adult hypodermis,
CC hermaphrodite vulva and adult excretory cell and duct.
CC {ECO:0000269|PubMed:16500660}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in larvae and adults.
CC Expression increases during L2-L3 molting stage an prior L3-L4 molting
CC stage. {ECO:0000269|PubMed:19716386}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes blisters in the
CC cuticle and abnormal localization of collagen col-19 in cuticle
CC dorso/ventral annulae and lateral alea. {ECO:0000269|PubMed:16500660,
CC 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; BX284603; CAB07614.1; -; Genomic_DNA.
DR PIR; T22237; T22237.
DR RefSeq; NP_499772.1; NM_067371.1.
DR AlphaFoldDB; O62247; -.
DR SMR; O62247; -.
DR STRING; 6239.F45G2.5; -.
DR PaxDb; O62247; -.
DR EnsemblMetazoa; F45G2.5.1; F45G2.5.1; WBGene00000255.
DR GeneID; 185812; -.
DR KEGG; cel:CELE_F45G2.5; -.
DR CTD; 185812; -.
DR WormBase; F45G2.5; CE16048; WBGene00000255; bli-5.
DR eggNOG; KOG4295; Eukaryota.
DR HOGENOM; CLU_1373315_0_0_1; -.
DR InParanoid; O62247; -.
DR OMA; SREWVCL; -.
DR OrthoDB; 1262308at2759; -.
DR PhylomeDB; O62247; -.
DR PRO; PR:O62247; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000255; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:WormBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; IDA:WormBase.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IDA:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Disulfide bond; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..202
FT /note="Kunitz-type protein bli-5"
FT /evidence="ECO:0000255"
FT /id="PRO_5004159996"
FT DOMAIN 135..184
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 135..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 158..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT MUTAGEN 56
FT /note="S->L: In 518; blistered cuticle associated with
FT abnormal localization of collagen col-19 in dorso/ventral
FT annulae and lateral alea. Loss of struts separating the
FT external and internal cuticle layers."
FT /evidence="ECO:0000269|PubMed:16500660"
SQ SEQUENCE 202 AA; 22633 MW; D366671FED7E354C CRC64;
MVSIHNSFIL LMLMISICFC EKCLTNEECD LKWPDAICVR GRCRCSENTI RKKSASREWV
CLATNDATGN SGPPLTCPTP EGAGYQVMYR KDGEPVKCSS KKKPDTCPEG FECIQGLSIL
GALDGVCCPD RAKTCVHPIF DHPDDGYLSR WGFDGEQCIE FKWNPERPSS ANNFKTRAHC
EDYCIGSING ITNYHQSNFH LF