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LYS7_CAEEL
ID   LYS7_CAEEL              Reviewed;         283 AA.
AC   O16202;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Lysozyme-like protein 7 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=lys-7 {ECO:0000312|WormBase:C02A12.4};
GN   ORFNames=C02A12.4 {ECO:0000312|WormBase:C02A12.4};
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   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12176330; DOI=10.1016/s0960-9822(02)00928-4;
RA   Mallo G.V., Kurz C.L., Couillault C., Pujol N., Granjeaud S., Kohara Y.,
RA   Ewbank J.J.;
RT   "Inducible antibacterial defense system in C. elegans.";
RL   Curr. Biol. 12:1209-1214(2002).
RN   [3] {ECO:0000305}
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16809667; DOI=10.1101/gr.50823006;
RA   O'Rourke D., Baban D., Demidova M., Mott R., Hodgkin J.;
RT   "Genomic clusters, putative pathogen recognition molecules, and
RT   antimicrobial genes are induced by infection of C. elegans with M.
RT   nematophilum.";
RL   Genome Res. 16:1005-1016(2006).
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17526726; DOI=10.1128/mcb.02070-06;
RA   Alper S., McBride S.J., Lackford B., Freedman J.H., Schwartz D.A.;
RT   "Specificity and complexity of the Caenorhabditis elegans innate immune
RT   response.";
RL   Mol. Cell. Biol. 27:5544-5553(2007).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21399680; DOI=10.1371/journal.pone.0016839;
RA   Marsh E.K., van den Berg M.C., May R.C.;
RT   "A two-gene balance regulates Salmonella typhimurium tolerance in the
RT   nematode Caenorhabditis elegans.";
RL   PLoS ONE 6:E16839-E16839(2011).
RN   [6] {ECO:0000305}
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21931778; DOI=10.1371/journal.pone.0024619;
RA   Boehnisch C., Wong D., Habig M., Isermann K., Michiels N.K., Roeder T.,
RA   May R.C., Schulenburg H.;
RT   "Protist-type lysozymes of the nematode Caenorhabditis elegans contribute
RT   to resistance against pathogenic Bacillus thuringiensis.";
RL   PLoS ONE 6:E24619-E24619(2011).
RN   [7] {ECO:0000305}
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22841995; DOI=10.1016/j.bbapap.2012.07.008;
RA   Kesika P., Balamurugan K.;
RT   "Studies on Shigella boydii infection in Caenorhabditis elegans and
RT   bioinformatics analysis of immune regulatory protein interactions.";
RL   Biochim. Biophys. Acta 1824:1449-1456(2012).
RN   [8] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=24972867; DOI=10.1242/bio.20148334;
RA   Kong C., Tan M.W., Nathan S.;
RT   "Orthosiphon stamineus protects Caenorhabditis elegans against
RT   Staphylococcus aureus infection through immunomodulation.";
RL   Biol. Open 3:644-655(2014).
CC   -!- FUNCTION: Plays a role in resistance to Gram-positive bacteria
CC       B.thuringiensis and M.nematophilum and Gram-negative bacteria S.boydii
CC       or S.flexneri infection and to fungus C.neoformans infection
CC       (PubMed:16809667, PubMed:21399680, PubMed:21931778, PubMed:22841995).
CC       Plays a role in susceptibility to Gram-negative bacterium S.typhimurium
CC       infection (PubMed:21399680). {ECO:0000269|PubMed:16809667,
CC       ECO:0000269|PubMed:21399680, ECO:0000269|PubMed:21931778,
CC       ECO:0000269|PubMed:22841995}.
CC   -!- TISSUE SPECIFICITY: Expressed in intestine (PubMed:12176330,
CC       PubMed:24972867). Expressed in rectal gland cells and head neurons
CC       (PubMed:17526726). {ECO:0000269|PubMed:12176330,
CC       ECO:0000269|PubMed:17526726, ECO:0000269|PubMed:24972867}.
CC   -!- INDUCTION: Induced by Gram-negative bacterium S.marcescens infection
CC       (PubMed:12176330). Induced by Gram-positive bacterium M.nematophilum
CC       infection (PubMed:16809667). Transiently induced by Gram-negative
CC       bacteria S.boydii and S.flexneri (PubMed:22841995). Down-regulated by
CC       exposure to Gram-positive bacterium B.thuringiensis spore toxins
CC       (PubMed:21931778). Down-regulated by exposure to Gram-negative bacteria
CC       S.marcescens or P.aeruginosa infection (PubMed:17526726). Down-
CC       regulated by Gram-positive bacterium S.aureus infection in the anterior
CC       part of the intestine (PubMed:24972867). {ECO:0000269|PubMed:12176330,
CC       ECO:0000269|PubMed:16809667, ECO:0000269|PubMed:17526726,
CC       ECO:0000269|PubMed:21931778, ECO:0000269|PubMed:22841995,
CC       ECO:0000269|PubMed:24972867}.
CC   -!- DISRUPTION PHENOTYPE: Increased abl-1, fat-5, clec-60 and rga-6 mRNA
CC       levels (PubMed:21399680). Reduced survival in response to fungus
CC       C.neoformans infection (PubMed:21399680). Reduced survival in response
CC       to bacterium B.thuringiensis infection (PubMed:21931778). Increased
CC       survival in response to bacterium S.typhimurium infection
CC       (PubMed:21399680). Susceptibility to S.typhimurium infection is
CC       abolished in an abl-1 (ok171) mutant background (PubMed:21399680).
CC       Compared to wild-type, mutants grown in presence of bacterium
CC       M.nematophilum are more constipated, the tail swelling is increased,
CC       growth is slower and they are arrested at the L3 larval stage
CC       (PubMed:16809667). Survival rate is similar to wild-type in response to
CC       bacteria S.aureus or P.aruginosa infection (PubMed:21399680). In
CC       absence of infection, lifespan and brood size is similar to wild-type
CC       (PubMed:21399680). {ECO:0000269|PubMed:16809667,
CC       ECO:0000269|PubMed:21399680, ECO:0000269|PubMed:21931778}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
CC   -!- CAUTION: Lacks conserved active site residues, suggesting it has no
CC       catalytic activity. {ECO:0000305}.
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DR   EMBL; BX284605; CCD62480.1; -; Genomic_DNA.
DR   PIR; T03857; T03857.
DR   RefSeq; NP_503972.1; NM_071571.6.
DR   AlphaFoldDB; O16202; -.
DR   SMR; O16202; -.
DR   STRING; 6239.C02A12.4; -.
DR   EPD; O16202; -.
DR   PaxDb; O16202; -.
DR   PeptideAtlas; O16202; -.
DR   EnsemblMetazoa; C02A12.4.1; C02A12.4.1; WBGene00003096.
DR   GeneID; 178772; -.
DR   KEGG; cel:CELE_C02A12.4; -.
DR   UCSC; C02A12.4.1; c. elegans.
DR   CTD; 178772; -.
DR   WormBase; C02A12.4; CE07828; WBGene00003096; lys-7.
DR   eggNOG; ENOG502S5RB; Eukaryota.
DR   GeneTree; ENSGT00970000195882; -.
DR   HOGENOM; CLU_073372_1_0_1; -.
DR   InParanoid; O16202; -.
DR   OMA; TCIRINQ; -.
DR   OrthoDB; 1437716at2759; -.
DR   PhylomeDB; O16202; -.
DR   PRO; PR:O16202; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00003096; Expressed in adult organism and 2 other tissues.
DR   GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IMP:WormBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR002053; Glyco_hydro_25.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Immunity; Innate immunity; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..283
FT                   /note="Lysozyme-like protein 7"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004157182"
FT   DOMAIN          53..273
FT                   /note="Ch-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
SQ   SEQUENCE   283 AA;  30880 MW;  DF4C69A31C925FD3 CRC64;
     MAHKSIVIFS VLAVLCHSAS VKVPPIVDSS LPVKFSEVIA EPAPNVPSNL ASYAYALDIY
     VQTTLSQLQC IKQAGYCAVF VRAYNPAGQG SFDTSSCVTI QNAYKAGLGI EIYMTPQPVS
     NKQGYQQLDE IIQGLTARAI TVRAIWIQVT SPTNWPNNAN SNINFINSIV SRARQSGLTV
     GIYTSYYDWN QITTGWSNIG NDVLLWYWNV YSGGVTGETP ANFNDFRKFG CWTAPSVKQF
     AQDETVCGIT VNRDVYLAGN VLKAVEEDGK IYAGGFVQGS LKI
 
 
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