ID   LBP_RAT                 Reviewed;         481 AA.
AC   Q63313;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Lipopolysaccharide-binding protein;
DE            Short=LBP;
DE   Flags: Precursor;
GN   Name=Lbp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8021509;
RA   Su G.L., Freeswick P.D., Geller D.A., Wang Q., Shapiro R.A., Wan Y.H.,
RA   Billiar T.R., Tweardy D.J., Simmons R.L., Wang S.C.;
RT   "Molecular cloning, characterization, and tissue distribution of rat
RT   lipopolysaccharide binding protein. Evidence for extrahepatic expression.";
RL   J. Immunol. 153:743-752(1994).
CC   -!- FUNCTION: Plays a role in the innate immune response. Binds to the
CC       lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid
CC       present in the outer membrane of all Gram-negative bacteria. Acts as an
CC       affinity enhancer for CD14, facilitating its association with LPS.
CC       Promotes the release of cytokines in response to bacterial
CC       lipopolysaccharide. {ECO:0000250|UniProtKB:P18428}.
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:0000250|UniProtKB:P18428}.
CC       Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}.
CC       Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
CC       granules. {ECO:0000250|UniProtKB:P17213}.
CC   -!- TISSUE SPECIFICITY: Detected in lung, liver, heart and kidney.
CC       {ECO:0000269|PubMed:8021509}.
CC   -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC       {ECO:0000305}.
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DR   EMBL; L32132; AAA21835.1; -; mRNA.
DR   PIR; I56246; I56246.
DR   AlphaFoldDB; Q63313; -.
DR   SMR; Q63313; -.
DR   STRING; 10116.ENSRNOP00000019787; -.
DR   GlyGen; Q63313; 2 sites.
DR   PaxDb; Q63313; -.
DR   RGD; 61865; Lbp.
DR   eggNOG; KOG4160; Eukaryota.
DR   InParanoid; Q63313; -.
DR   PhylomeDB; Q63313; -.
DR   Reactome; R-RNO-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR   Reactome; R-RNO-166020; Transfer of LPS from LBP carrier to CD14.
DR   Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
DR   PRO; PR:Q63313; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071723; F:lipopeptide binding; ISO:RGD.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IDA:RGD.
DR   GO; GO:0070891; F:lipoteichoic acid binding; ISO:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR   GO; GO:0006953; P:acute-phase response; ISO:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR   GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:RGD.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR   GO; GO:0032490; P:detection of molecule of bacterial origin; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; ISO:RGD.
DR   GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; ISO:RGD.
DR   GO; GO:0015920; P:lipopolysaccharide transport; ISO:RGD.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0033036; P:macromolecule localization; ISO:RGD.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; ISS:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR   GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR   GO; GO:0045919; P:positive regulation of cytolysis; ISO:RGD.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; IDA:RGD.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:RGD.
DR   GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IDA:RGD.
DR   GO; GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; ISO:RGD.
DR   GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISO:RGD.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0090559; P:regulation of membrane permeability; IMP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
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   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Disulfide bond; Glycoprotein; Immunity;
KW   Innate immunity; Lipid transport; Membrane; Reference proteome; Secreted;
KW   Signal; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..481
FT                   /note="Lipopolysaccharide-binding protein"
FT                   /id="PRO_0000017161"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        159..198
FT                   /evidence="ECO:0000250|UniProtKB:Q61805"
SQ   SEQUENCE   481 AA;  53600 MW;  23E67CB9CC97D2FC CRC64;
     MKSATGPLLP TLLGLLLLSI PRTQGVNPAM VVRITDKGLE YAAKEGLLSL QRELYKITLP
     DFSGDFKIKA VGRGQYEFHS LEIQSCQLRG SSLKPLPGRG LSLSISDSSI SVRGKWKVRR
     SFVKLHGSFD LDVKSVTISV DLLLGVDPSE RPTVTASGCS NRIRDLELHV SGNVGWLLNL
     FHNQIESKLQ KVLESKICEM IQKSVTSDLQ PYLQTLPVTA DIDTILGIDY SLVAAPQAKA
     QTLDVMFKGE IFNRNHRSPV TTPTPTMSLP EDSKQMVYFA ISDQAFNIAT RVYHQAGYLN
     FTITDDMLPP DSNIRLNTKA FRPFTPLITR KYPDMNLELL GTVVSAPLLN VSPGNLSLAP
     QMEIEGFVIL PSSARESVFR LGVVTNVFVS LTFDNSKVTG MLHPEKAQVR LIESKVGMFN
     VNLFQAFLNY YLLNSLYPDV NDELAKGFPL PLPRRIKLHD LDFQIHKNFL YLGANVQYMR
     V