ID   LBP_BOVIN               Reviewed;         481 AA.
AC   Q2TBI0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Lipopolysaccharide-binding protein;
DE            Short=LBP;
DE   Flags: Precursor;
GN   Name=LBP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC       {ECO:0000305}.
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DR   EMBL; BC110172; AAI10173.1; -; mRNA.
DR   RefSeq; NP_001033763.1; NM_001038674.2.
DR   AlphaFoldDB; Q2TBI0; -.
DR   SMR; Q2TBI0; -.
DR   STRING; 9913.ENSBTAP00000022428; -.
DR   PaxDb; Q2TBI0; -.
DR   PeptideAtlas; Q2TBI0; -.
DR   PRIDE; Q2TBI0; -.
DR   GeneID; 512242; -.
DR   KEGG; bta:512242; -.
DR   CTD; 3929; -.
DR   eggNOG; KOG4160; Eukaryota.
DR   InParanoid; Q2TBI0; -.
DR   OrthoDB; 1242894at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB.
DR   GO; GO:0006953; P:acute-phase response; IEA:InterPro.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; ISS:UniProtKB.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
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:0000250"
FT   CHAIN           26..481
FT                   /note="Lipopolysaccharide-binding protein"
FT                   /id="PRO_0000239847"
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   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        159..198
FT                   /evidence="ECO:0000250|UniProtKB:Q61805"
SQ   SEQUENCE   481 AA;  53698 MW;  B6FD8C2C2D4FD014 CRC64;
     MVTSTGTLPS LLLGTLLTFT SGALGANPGL VVRITDQGLE YVAQEELLAL QSKLHKVTLP
     DFNGDVRIKH FGSVDYRFHS LNIQSCKLLG SALKLLPNQG LHFSISDSFI QVTGDWKVRK
     RILRLDGSFD VKVKGITISV NLLLDSEPSG RPKVAVSSCS SHIRDVEVHI SGDLGWLLNL
     FHNQIESRFR RVLESKICEI IEDSVTSELQ PYLQTLPVTT EIDHLAGLDY SLMGAPQATA
     QMLDVMFKGE IFSRDDRFPV AFLAPVMNLP EEHSRMVYFA ISDYAFNTAS LVYHKAGFLN
     FTITDDVIPP DSSIRQNTKS FRAFVPRIAR LYPNTNLELQ GAVISAPCLN FSPGNLSTAA
     QMEIEAFVLL PNSVKEPVFR LSVATNVSAM LTFNTSKITG FLEPGKIQVE LKESKVGRFN
     VELLEALLNY YLLNNFYPKV NDKLAEGFPL PLLRKIQLYD PILQIHKDFL FLGTNVRYLR
     V