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 05-OCT-2010, entry version 102. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-436. RX MEDLINE=90385281; 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]. RX MEDLINE=94292492; PubMed=7517398; RA Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L., RA Lane J.C., Leong S.R., Thornton M.B., Miller K.L., Scott R.W.; RT "Bactericidal/permeability-increasing protein and lipopolysaccharide RT (LPS)-binding protein. LPS binding properties and effects on LPS- RT mediated cell 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 RT binding protein (LBP) and bactericidal permeability increasing protein RT (BPI) is highly conserved."; RL Biochem. Biophys. Res. Commun. 236:427-430(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=98110577; 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) RT and phospholipid transfer protein (PLTP) genes suggests a common gene RT family of 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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MEDLINE=21638749; 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394, AND MASS RP SPECTROMETRY. 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [11] RP 3D-STRUCTURE MODELING. RX MEDLINE=98227852; PubMed=9568897; RA Beamer L.J., Carroll S.F., Eisenberg D.; RT "The BPI/LBP family of proteins: a structural analysis of conserved RT regions."; RL Protein Sci. 7:906-914(1998). CC -!- FUNCTION: Binds to the lipid A moiety of bacterial CC lipopolysaccharides (LPS), a glycolipid present in the outer CC membrane of all Gram-negative bacteria. The LBP/LPS complex seems CC to interact with the CD14 receptor. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP CC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IPI; IPI00032311; -. DR PIR; A35843; A35843. DR PIR; A54136; A54136. DR RefSeq; NP_004130.2; -. DR UniGene; Hs.154078; -. DR ProteinModelPortal; P18428; -. DR SMR; P18428; 26-478. DR DIP; DIP-90N; -. DR STRING; P18428; -. DR TCDB; 1.C.40.1.2; bactericidal permeability increasing protein (BPIP) family. DR PeptideAtlas; P18428; -. DR PRIDE; P18428; -. DR Ensembl; ENST00000217407; ENSP00000217407; ENSG00000129988. DR GeneID; 3929; -. DR KEGG; hsa:3929; -. DR UCSC; uc002xic.1; human. DR CTD; 3929; -. DR GeneCards; GC20P036974; -. DR H-InvDB; HIX0015804; -. DR HGNC; HGNC:6517; LBP. DR HPA; CAB025905; -. DR HPA; HPA001508; -. DR MIM; 151990; gene. DR PharmGKB; PA29235; -. DR eggNOG; prNOG13159; -. DR HOGENOM; HBG278860; -. DR HOVERGEN; HBG002797; -. DR InParanoid; P18428; -. DR OMA; RNHRSPV; -. DR OrthoDB; EOG9FJBV8; -. DR PhylomeDB; P18428; -. DR Pathway_Interaction_DB; il6_7pathway; IL6-mediated signaling events. DR Reactome; REACT_6900; Signaling in Immune system. DR NextBio; 15427; -. DR ArrayExpress; P18428; -. DR Bgee; P18428; -. DR CleanEx; HS_LBP; -. DR Genevestigator; P18428; -. DR GermOnline; ENSG00000129988; Homo sapiens. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0051636; F:Gram-negative bacterial cell surface binding; IDA:BHF-UCL. DR GO; GO:0051637; F:Gram-positive bacterial cell surface binding; IDA:BHF-UCL. DR GO; GO:0008289; F:lipid binding; IEA:InterPro. DR GO; GO:0001530; F:lipopolysaccharide binding; ISS:BHF-UCL. DR GO; GO:0070891; F:lipoteichoic acid binding; IDA:MGI. DR GO; GO:0005102; F: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:0071223; P:cellular response to lipoteichoic acid; IDA:MGI. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:BHF-UCL. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEP:BHF-UCL. DR GO; GO:0032490; P:detection of molecule of bacterial origin; IDA:BHF-UCL. DR GO; GO:0045087; P:innate immune response; IC:BHF-UCL. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. 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:0002281; P:macrophage activation involved in immune re...; ISS:BHF-UCL. DR GO; GO:0032720; P:negative regulation of tumor necrosis facto...; IDA:BHF-UCL. DR GO; GO:0008228; P:opsonization; IC:BHF-UCL. DR GO; GO:0032755; P:positive regulation of interleukin-6 produc...; IDA:BHF-UCL. DR GO; GO:0032757; P:positive regulation of interleukin-8 produc...; IDA:BHF-UCL. DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL. DR GO; GO:0060265; P:positive regulation of respiratory burst in...; ISS:BHF-UCL. DR GO; GO:0034145; P:positive regulation of toll-like receptor 4...; IDA:BHF-UCL. DR GO; GO:0032760; P:positive regulation of tumor necrosis facto...; IDA:BHF-UCL. DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom. 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 Pfam; PF01273; LBP_BPI_CETP; 1. DR Pfam; PF02886; LBP_BPI_CETP_C; 1. DR SMART; SM00328; BPI1; 1. DR SMART; SM00329; BPI2; 1. DR SUPFAM; SSF55394; Bactericidal_perm-incr_a/b_dom; 2. DR PROSITE; PS00400; LBP_BPI_CETP; 1. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Complete proteome; Glycoprotein; KW Lipid transport; Polymorphism; Secreted; Signal; Transport. FT SIGNAL 1 25 FT CHAIN 26 481 Lipopolysaccharide-binding protein. FT /FTId=PRO_0000017158. FT CARBOHYD 300 300 N-linked (GlcNAc...) (Potential). FT CARBOHYD 355 355 N-linked (GlcNAc...) (Potential). FT CARBOHYD 386 386 N-linked (GlcNAc...) (Potential). FT CARBOHYD 394 394 N-linked (GlcNAc...). FT VARIANT 9 9 P -> L (in dbSNP:rs2232580). FT /FTId=VAR_028243. FT VARIANT 111 111 R -> Q (in dbSNP:rs2232583). FT /FTId=VAR_049737. FT VARIANT 125 125 L -> I (in dbSNP:rs2232585). FT /FTId=VAR_028244. FT VARIANT 147 147 E -> K (in dbSNP:rs36015492). FT /FTId=VAR_049738. FT VARIANT 157 157 S -> C (in dbSNP:rs2232586). FT /FTId=VAR_061293. FT VARIANT 166 166 V -> M (in dbSNP:rs5744204). FT /FTId=VAR_028245. FT VARIANT 242 242 M -> I (in dbSNP:rs2232601). FT /FTId=VAR_028246. FT VARIANT 283 283 D -> G (in dbSNP:rs2232607). FT /FTId=VAR_028247. FT VARIANT 294 294 H -> R (in dbSNP:rs2232608). FT /FTId=VAR_028248. FT VARIANT 333 333 P -> L (in dbSNP:rs2232613). FT /FTId=VAR_028249. FT VARIANT 339 339 L -> F (in dbSNP:rs5744212). FT /FTId=VAR_028250. FT VARIANT 364 364 I -> T (in dbSNP:rs2232615). FT /FTId=VAR_049739. FT VARIANT 436 436 F -> L (in dbSNP:rs2232618). FT /FTId=VAR_028251. FT VARIANT 445 445 A -> T (in dbSNP:rs2232619). FT /FTId=VAR_028252. FT CONFLICT 6 6 R -> H (in Ref. 2). FT CONFLICT 22 22 E -> C (in Ref. 2). FT CONFLICT 82 82 N -> K (in Ref. 4; AAC39547). FT CONFLICT 128 128 S -> F (in Ref. 4; AAC39547). FT CONFLICT 154 157 VTAS -> GYCL (in Ref. 1; AAA59493). FT CONFLICT 174 174 L -> S (in Ref. 1; AAA59493). FT CONFLICT 257 257 R -> S (in Ref. 4; AAC39547). FT CONFLICT 266 270 VMSLP -> A (in Ref. 1; AAA59493). FT CONFLICT 369 369 L -> H (in Ref. 4; AAC39547). 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 //