EGFLR_HOLDI
ID EGFLR_HOLDI Reviewed; 317 AA.
AC Q1HAY7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 23-FEB-2022, entry version 37.
DE RecName: Full=Epidermal growth factor-like protein {ECO:0000312|EMBL:BAE94686.1};
DE AltName: Full=LPS recognition protein {ECO:0000303|PubMed:16849495};
DE Short=LPR {ECO:0000303|PubMed:16849495};
DE Flags: Precursor;
GN Name=EGF-like {ECO:0000312|EMBL:BAE94686.1};
OS Holotrichia diomphalia (Korean black chafer).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Melolonthinae; Holotrichia.
OX NCBI_TaxID=33394 {ECO:0000312|EMBL:BAE94686.1};
RN [1] {ECO:0000312|EMBL:BAE94686.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-43; 79-85; 86-104;
RP 118-146; 197-203; 206-212 AND 232-238, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Plasma {ECO:0000312|EMBL:BAE94686.1};
RX PubMed=16849495; DOI=10.4049/jimmunol.177.3.1838;
RA Ju J.S., Cho M.H., Brade L., Kim J.H., Park J.W., Ha N.C., Soederhaell I.,
RA Soederhaell K., Brade H., Lee B.L.;
RT "A novel 40-kDa protein containing six repeats of an epidermal growth
RT factor-like domain functions as a pattern recognition protein for
RT lipopolysaccharide.";
RL J. Immunol. 177:1838-1845(2006).
CC -!- FUNCTION: Binds to lipopolysaccharides (LPS) present on the cell walls
CC of Gram-negative bacteria, behaving as a pattern recognition receptor
CC (PRR) (PubMed:16849495). Induces bacterial aggregation and enhances
CC their subsequent clearance by the innate immune response
CC (PubMed:16849495). Binds to the inner core oligosaccharides region of
CC rough-type bacterial LPS (PubMed:16849495). Displays activity against
CC the Gram-negative bacterium E.coli (PubMed:16849495). Does not display
CC any activity against the Gram-positive bacterium S.aureus or the fungi
CC C.albicans (PubMed:16849495). {ECO:0000269|PubMed:16849495}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16849495}.
CC Note=Detected in larval plasma. {ECO:0000269|PubMed:16849495}.
CC -!- MISCELLANEOUS: In mouse bone marrow-derived mast cells (BMMC), inhibits
CC LPS-induced expression of the inflammatory cytokine Interleukin-6 (IL-
CC 6). {ECO:0000269|PubMed:16849495}.
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DR EMBL; AB201466; BAE94686.1; -; mRNA.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0140367; P:antibacterial innate immune response; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0032497; P:detection of lipopolysaccharide; IDA:UniProtKB.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR SMART; SM00181; EGF; 5.
DR SUPFAM; SSF57184; SSF57184; 2.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Immunity; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:16849495"
FT CHAIN 24..317
FT /note="Epidermal growth factor-like protein"
FT /evidence="ECO:0000269|PubMed:16849495"
FT /id="PRO_5004190114"
FT DOMAIN 93..128
FT /note="EGF-like 1"
FT /evidence="ECO:0000305|PubMed:16849495"
FT DOMAIN 130..161
FT /note="EGF-like 2"
FT /evidence="ECO:0000305|PubMed:16849495"
FT DOMAIN 163..195
FT /note="EGF-like 3"
FT /evidence="ECO:0000305|PubMed:16849495"
FT DOMAIN 208..243
FT /note="EGF-like 4"
FT /evidence="ECO:0000305|PubMed:16849495"
FT DOMAIN 245..280
FT /note="EGF-like 5"
FT /evidence="ECO:0000305|PubMed:16849495"
FT DOMAIN 282..315
FT /note="EGF-like 6"
FT /evidence="ECO:0000305|PubMed:16849495"
FT REGION 24..33
FT /note="May be required for E.coli agglutination activity"
FT /evidence="ECO:0000269|PubMed:16849495"
FT DISULFID 98..107
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 102..113
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 115..127
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 131..140
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 135..145
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 147..160
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 164..174
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 168..180
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 182..194
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 213..222
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 217..228
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 230..242
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 246..255
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 250..261
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 263..279
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 283..292
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 287..298
FT /evidence="ECO:0000303|PubMed:16849495"
FT DISULFID 300..314
FT /evidence="ECO:0000303|PubMed:16849495"
SQ SEQUENCE 317 AA; 33037 MW; AA3F208126B9DB4F CRC64;
MDFKIFLFLT AIFMIVGVTV STATTNPTAP RAYRPRINTT AGVCELEVPI VNILPPELKH
TAHTIRGNGS APGFSKIKIC CSGYKIVAHT PFHCTPDCPS GCGLGNCTAP NVCTCNKGAG
FGPDGKCISV CPGRCLNGQC YGNFCNCNSG FVLEPNGRYC TGGCTRNCGP GGQCVGNNQC
SCLSGFALNS QGTCQMICAP GFQQMGSACE PLCPKGCVNG ECVAPGQCRC KSGYALNSSK
VCAPKCSQPC YNGFCSAPNV CTCKEGYIKD ATSRNGNRCI AYCAAGCPNG TCSAPNFCIC
KQGYIKQSKG SNVCVKQ
