LBP_RABIT
ID LBP_RABIT Reviewed; 482 AA.
AC P17454;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Lipopolysaccharide-binding protein;
DE Short=LBP;
DE Flags: Precursor;
GN Name=LBP;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2402637; DOI=10.1126/science.2402637;
RA Schumann R.R., Leong S.R., Flaggs G.W., Gray P.W., Wright S.D.,
RA Mathison J.C., Tobias P.S., Ulevitch R.J.;
RT "Structure and function of lipopolysaccharide binding protein.";
RL Science 249:1429-1431(1990).
RN [2]
RP PROTEIN SEQUENCE OF 27-66, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Serum;
RX PubMed=2427635; DOI=10.1084/jem.164.3.777;
RA Tobias P.S., Soldau K., Ulevitch R.J.;
RT "Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit
RT serum.";
RL J. Exp. Med. 164:777-793(1986).
CC -!- FUNCTION: Plays a role in the innate immune response (PubMed:2402637).
CC Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a
CC glycolipid present in the outer membrane of all Gram-negative bacteria
CC (PubMed:2427635). Acts as an affinity enhancer for CD14, facilitating
CC its association with LPS (By similarity). Promotes the release of
CC cytokines in response to bacterial lipopolysaccharide (PubMed:2402637).
CC {ECO:0000250|UniProtKB:P18428, ECO:0000269|PubMed:2402637,
CC ECO:0000269|PubMed:2427635}.
CC -!- SUBUNIT: When bound to LPS, interacts (via C-terminus) with soluble and
CC membrane-bound CD14. {ECO:0000250|UniProtKB:P18428}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2402637,
CC ECO:0000269|PubMed:2427635}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
CC {ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:2427635}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; M35534; AAA99235.1; -; mRNA.
DR PIR; B35843; B35843.
DR AlphaFoldDB; P17454; -.
DR SMR; P17454; -.
DR STRING; 9986.ENSOCUP00000011712; -.
DR PRIDE; P17454; -.
DR eggNOG; KOG4160; Eukaryota.
DR InParanoid; P17454; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IDA:BHF-UCL.
DR GO; GO:0006953; P:acute-phase response; IDA:BHF-UCL.
DR GO; GO:0006968; P:cellular defense response; IDA:BHF-UCL.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; IDA:BHF-UCL.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IDA:BHF-UCL.
DR GO; GO:0008228; P:opsonization; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR030675; BPI/LBP.
DR InterPro; IPR032942; BPI/LBP/Plunc.
DR InterPro; IPR030180; LBP.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR10504; PTHR10504; 1.
DR PANTHER; PTHR10504:SF66; PTHR10504:SF66; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR PIRSF; PIRSF002417; Lipid_binding_protein; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Lipid transport;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2427635"
FT CHAIN 27..482
FT /note="Lipopolysaccharide-binding protein"
FT /id="PRO_0000017160"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..199
FT /evidence="ECO:0000250|UniProtKB:Q61805"
FT CONFLICT 57
FT /note="E -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="S -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 54001 MW; 628A6E0A647200C2 CRC64;
MGTWARALLG STLLSLLLAA APGALGTNPG LITRITDKGL EYAAREGLLA LQRKLLEVTL
PDSDGDFRIK HFGRAQYKFY SLKIPRFELL RGTLRPLPGQ GLSLDISDAY IHVRGSWKVR
KAFLRLKNSF DLYVKGLTIS VHLVLGSESS GRPTVTTSSC SSDIQNVELD IEGDLEELLN
LLQSQIDARL REVLESKICR QIEEAVTAHL QPYLQTLPVT TQIDSFAGID YSLMEAPRAT
AGMLDVMFKG EIFPLDHRSP VDFLAPAMNL PEAHSRMVYF SISDYVFNTA SLAYHKSGYW
NFSITDAMVP ADLNIRRTTK SFRPFVPLLA NLYPNMNLEL QGTVNSEQLV NLSTENLLEE
PEMDIEALVV LPSSAREPVF RLGVATNVSA TLTLNTRKIT GFLKPGRLQV ELKESKVGGF
NVELLEALLN YYILNNLYPK VNEKLAHRFP LPLLRHIQLY DLLLQTHENF LLVGANIQYR
RV
