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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
 
 
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