LBP_HUMAN
ID LBP_HUMAN Reviewed; 481 AA.
AC P18428; B2R938; O43438; Q92672; Q9H403; Q9UD66;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Lipopolysaccharide-binding protein;
DE Short=LBP;
DE Flags: Precursor;
GN Name=LBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-40, VARIANT LEU-436,
RP SUBCELLULAR LOCATION, AND TISSUE 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 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7517398; DOI=10.1016/s0021-9258(17)32454-7;
RA Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L., Lane J.C.,
RA Leong S.R., Thornton M.B., Miller K.L., Scott R.W.;
RT "Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-
RT binding protein. LPS binding properties and effects on LPS-mediated cell
RT activation.";
RL J. Biol. Chem. 269:17411-17416(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-436.
RX PubMed=9240454; DOI=10.1006/bbrc.1997.6970;
RA Hubacek J.A., Buchler C., Aslanidis C., Schmitz G.;
RT "The genomic organization of the genes for human lipopolysaccharide binding
RT protein (LBP) and bactericidal permeability increasing protein (BPI) is
RT highly conserved.";
RL Biochem. Biophys. Res. Commun. 236:427-430(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9441745; DOI=10.1006/geno.1997.5030;
RA Kirschning C.J., Au-Young J., Lamping N., Reuter D., Pfeil D.,
RA Seilhamer J.J., Schumann R.R.;
RT "Similar organization of the lipopolysaccharide-binding protein (LBP) and
RT phospholipid transfer protein (PLTP) genes suggests a common gene family of
RT lipid-binding proteins.";
RL Genomics 46:416-425(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-436.
RC TISSUE=Liver;
RA Long J.Y., Liu J.Q., Xue Y.N., Wang H.X.;
RT "Cloning and sequencing of human lipopolysaccharide-binding protein gene.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:469-471(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
RA Sutton C.L., Smith R.I.F., Centola M.B., Theofan G.;
RT "Cloning and characterization of the human LBP upstream sequence.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, AND INTERACTION WITH CD14 AND LIPOPOLYSACCHARIDE.
RX PubMed=1698311; DOI=10.1126/science.1698311;
RA Wright S.D., Ramos R.A., Tobias P.S., Ulevitch R.J., Mathison J.C.;
RT "CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding
RT protein.";
RL Science 249:1431-1433(1990).
RN [11]
RP REVIEW.
RX PubMed=17481951; DOI=10.1016/j.ijmm.2007.04.001;
RA Jerala R.;
RT "Structural biology of the LPS recognition.";
RL Int. J. Med. Microbiol. 297:353-363(2007).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP FUNCTION.
RX PubMed=20133493; DOI=10.1093/intimm/dxq005;
RA Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.;
RT "Lipopolysaccharide-binding protein-mediated Toll-like receptor 4
RT dimerization enables rapid signal transduction against lipopolysaccharide
RT stimulation on membrane-associated CD14-expressing cells.";
RL Int. Immunol. 22:271-280(2010).
RN [14]
RP FUNCTION, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP GLYCOSYLATION, VARIANT LEU-333, AND CHARACTERIZATION OF VARIANT LEU-333.
RX PubMed=24120359; DOI=10.1016/j.immuni.2013.09.005;
RA Eckert J.K., Kim Y.J., Kim J.I., Guertler K., Oh D.Y., Sur S., Lundvall L.,
RA Hamann L., van der Ploeg A., Pickkers P., Giamarellos-Bourboulis E.,
RA Kubarenko A.V., Weber A.N., Kabesch M., Kumpf O., An H.J., Lee J.O.,
RA Schumann R.R.;
RT "The crystal structure of lipopolysaccharide binding protein reveals the
RT location of a frequent mutation that impairs innate immunity.";
RL Immunity 39:647-660(2013).
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
CC (PubMed:7517398, PubMed:24120359). Acts as an affinity enhancer for
CC CD14, facilitating its association with LPS. Promotes the release of
CC cytokines in response to bacterial lipopolysaccharide (PubMed:7517398,
CC PubMed:24120359). {ECO:0000269|PubMed:1698311,
CC ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:24120359,
CC ECO:0000269|PubMed:7517398, ECO:0000305|PubMed:17481951}.
CC -!- SUBUNIT: When bound to LPS, interacts (via C-terminus) with soluble and
CC membrane-bound CD14. {ECO:0000269|PubMed:1698311,
CC ECO:0000305|PubMed:17481951}.
CC -!- INTERACTION:
CC P18428; P23560-2: BDNF; NbExp=3; IntAct=EBI-3927059, EBI-12275524;
CC P18428; Q13162: PRDX4; NbExp=4; IntAct=EBI-3927059, EBI-2211957;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2402637,
CC ECO:0000269|PubMed:24120359, ECO:0000269|PubMed:7517398}. Cytoplasmic
CC granule membrane {ECO:0000250|UniProtKB:P17213}. Note=Membrane-
CC associated in polymorphonuclear Leukocytes (PMN) granules.
CC {ECO:0000250|UniProtKB:P17213}.
CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC {ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:24120359}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; M35533; AAA59493.1; -; mRNA.
DR EMBL; X98657; CAA67226.1; -; Genomic_DNA.
DR EMBL; X98658; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98659; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98660; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98661; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98662; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98663; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98664; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98665; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98666; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98667; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; X98668; CAA67226.1; JOINED; Genomic_DNA.
DR EMBL; AF013512; AAC39547.1; -; Genomic_DNA.
DR EMBL; AF013500; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013501; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013502; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013503; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013504; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013505; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013506; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013507; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013508; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013509; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013510; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF013511; AAC39547.1; JOINED; Genomic_DNA.
DR EMBL; AF105067; AAD21962.1; -; mRNA.
DR EMBL; AK313625; BAG36385.1; -; mRNA.
DR EMBL; AL080249; CAC10462.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76034.1; -; Genomic_DNA.
DR EMBL; L42172; AAA66446.1; -; Genomic_DNA.
DR CCDS; CCDS13304.1; -.
DR PIR; A35843; A35843.
DR PIR; A54136; A54136.
DR RefSeq; NP_004130.2; NM_004139.4.
DR AlphaFoldDB; P18428; -.
DR SMR; P18428; -.
DR BioGRID; 110121; 17.
DR DIP; DIP-90N; -.
DR IntAct; P18428; 15.
DR STRING; 9606.ENSP00000217407; -.
DR TCDB; 1.C.40.1.2; the bactericidal permeability increasing protein (bpip) family.
DR GlyConnect; 1985; 6 N-Linked glycans (1 site).
DR GlyGen; P18428; 4 sites, 6 N-linked glycans (1 site).
DR iPTMnet; P18428; -.
DR PhosphoSitePlus; P18428; -.
DR BioMuta; LBP; -.
DR DMDM; 116242615; -.
DR CPTAC; non-CPTAC-1140; -.
DR jPOST; P18428; -.
DR MassIVE; P18428; -.
DR MaxQB; P18428; -.
DR PaxDb; P18428; -.
DR PeptideAtlas; P18428; -.
DR PRIDE; P18428; -.
DR ProteomicsDB; 53558; -.
DR TopDownProteomics; P18428; -.
DR Antibodypedia; 777; 406 antibodies from 37 providers.
DR DNASU; 3929; -.
DR Ensembl; ENST00000217407.3; ENSP00000217407.2; ENSG00000129988.6.
DR GeneID; 3929; -.
DR KEGG; hsa:3929; -.
DR MANE-Select; ENST00000217407.3; ENSP00000217407.2; NM_004139.5; NP_004130.2.
DR UCSC; uc002xic.3; human.
DR CTD; 3929; -.
DR DisGeNET; 3929; -.
DR GeneCards; LBP; -.
DR HGNC; HGNC:6517; LBP.
DR HPA; ENSG00000129988; Tissue enriched (liver).
DR MIM; 151990; gene.
DR neXtProt; NX_P18428; -.
DR OpenTargets; ENSG00000129988; -.
DR PharmGKB; PA30303; -.
DR VEuPathDB; HostDB:ENSG00000129988; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230353; -.
DR HOGENOM; CLU_028970_3_2_1; -.
DR InParanoid; P18428; -.
DR OMA; NPYMEID; -.
DR OrthoDB; 1242894at2759; -.
DR PhylomeDB; P18428; -.
DR TreeFam; TF315617; -.
DR PathwayCommons; P18428; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-166020; Transfer of LPS from LBP carrier to CD14.
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P18428; -.
DR BioGRID-ORCS; 3929; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; LBP; human.
DR GeneWiki; Lipopolysaccharide-binding_protein; -.
DR GenomeRNAi; 3929; -.
DR Pharos; P18428; Tbio.
DR PRO; PR:P18428; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P18428; protein.
DR Bgee; ENSG00000129988; Expressed in right lobe of liver and 105 other tissues.
DR Genevisible; P18428; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071723; F:lipopeptide binding; IDA:AgBase.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
DR GO; GO:0070891; F:lipoteichoic acid binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR GO; GO:0006953; P:acute-phase response; IEP:BHF-UCL.
DR GO; GO:0006968; P:cellular defense response; ISS:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:BHF-UCL.
DR GO; GO:0032490; P:detection of molecule of bacterial origin; IDA:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; ISS:BHF-UCL.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0015920; P:lipopolysaccharide transport; IDA:BHF-UCL.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0033036; P:macromolecule localization; IDA:AgBase.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0008228; P:opsonization; ISS:BHF-UCL.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0045919; P:positive regulation of cytolysis; IDA:AgBase.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; ISS:BHF-UCL.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; 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; Membrane;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2402637"
FT CHAIN 26..481
FT /note="Lipopolysaccharide-binding protein"
FT /id="PRO_0000017158"
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:0000269|PubMed:19159218"
FT DISULFID 159..198
FT /evidence="ECO:0000250|UniProtKB:Q61805"
FT VARIANT 9
FT /note="P -> L (in dbSNP:rs2232580)"
FT /id="VAR_028243"
FT VARIANT 111
FT /note="R -> Q (in dbSNP:rs2232583)"
FT /id="VAR_049737"
FT VARIANT 125
FT /note="L -> I (in dbSNP:rs2232585)"
FT /id="VAR_028244"
FT VARIANT 147
FT /note="E -> K (in dbSNP:rs36015492)"
FT /id="VAR_049738"
FT VARIANT 157
FT /note="S -> C (in dbSNP:rs2232586)"
FT /id="VAR_061293"
FT VARIANT 166
FT /note="V -> M (in dbSNP:rs5744204)"
FT /id="VAR_028245"
FT VARIANT 242
FT /note="M -> I (in dbSNP:rs2232601)"
FT /id="VAR_028246"
FT VARIANT 283
FT /note="D -> G (in dbSNP:rs2232607)"
FT /id="VAR_028247"
FT VARIANT 294
FT /note="H -> R (in dbSNP:rs2232608)"
FT /id="VAR_028248"
FT VARIANT 333
FT /note="P -> L (abolishes lipopolysaccharide binding and
FT causes increased proteolytic degradation of the protein;
FT dbSNP:rs2232613)"
FT /evidence="ECO:0000269|PubMed:24120359"
FT /id="VAR_028249"
FT VARIANT 339
FT /note="L -> F (in dbSNP:rs5744212)"
FT /id="VAR_028250"
FT VARIANT 364
FT /note="I -> T (in dbSNP:rs2232615)"
FT /id="VAR_049739"
FT VARIANT 436
FT /note="F -> L (in dbSNP:rs2232618)"
FT /evidence="ECO:0000269|PubMed:2402637,
FT ECO:0000269|PubMed:9240454, ECO:0000269|Ref.5"
FT /id="VAR_028251"
FT VARIANT 445
FT /note="A -> T (in dbSNP:rs2232619)"
FT /id="VAR_028252"
FT CONFLICT 6
FT /note="R -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="E -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="N -> K (in Ref. 4; AAC39547)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="S -> F (in Ref. 4; AAC39547)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..157
FT /note="VTAS -> GYCL (in Ref. 1; AAA59493)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="L -> S (in Ref. 1; AAA59493)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> S (in Ref. 4; AAC39547)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..270
FT /note="VMSLP -> A (in Ref. 1; AAA59493)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="L -> H (in Ref. 4; AAC39547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 53384 MW; 5A0E4B9E5E604C72 CRC64;
MGALARALPS ILLALLLTST PEALGANPGL VARITDKGLQ YAAQEGLLAL QSELLRITLP
DFTGDLRIPH VGRGRYEFHS LNIHSCELLH SALRPVPGQG LSLSISDSSI RVQGRWKVRK
SFFKLQGSFD VSVKGISISV NLLLGSESSG RPTVTASSCS SDIADVEVDM SGDLGWLLNL
FHNQIESKFQ KVLESRICEM IQKSVSSDLQ PYLQTLPVTT EIDSFADIDY SLVEAPRATA
QMLEVMFKGE IFHRNHRSPV TLLAAVMSLP EEHNKMVYFA ISDYVFNTAS LVYHEEGYLN
FSITDDMIPP DSNIRLTTKS FRPFVPRLAR LYPNMNLELQ GSVPSAPLLN FSPGNLSVDP
YMEIDAFVLL PSSSKEPVFR LSVATNVSAT LTFNTSKITG FLKPGKVKVE LKESKVGLFN
AELLEALLNY YILNTFYPKF NDKLAEGFPL PLLKRVQLYD LGLQIHKDFL FLGANVQYMR
V
