P18428 (LBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipopolysaccharide-binding protein
Short name=LBP

Gene names

Name:

LBP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. The LBP/LPS complex seems to interact with the CD14 receptor.
Subcellular location	Secreted.
Sequence similarities	Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Antibiotic Antimicrobial
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Toll signaling pathway Traceable author statement. Source: Reactome acute-phase response Inferred from expression pattern. Source: BHF-UCL cellular defense response Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL cellular response to lipoteichoic acid Inferred from direct assay. Source: MGI defense response to Gram-negative bacterium Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL defense response to Gram-positive bacterium Inferred from expression pattern. Source: BHF-UCL detection of molecule of bacterial origin Inferred from direct assay. Source: BHF-UCL innate immune response Inferred from sequence or structural similarity. Source: BHF-UCL lipid transport Inferred from electronic annotation. Source: UniProtKB-KW lipopolysaccharide transport Inferred from direct assay. Source: BHF-UCL lipopolysaccharide-mediated signaling pathway Inferred from direct assay. Source: BHF-UCL macrophage activation involved in immune response Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL negative regulation of tumor necrosis factor production Inferred from direct assay. Source: BHF-UCL opsonization Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of interleukin-6 production Inferred from direct assay. Source: BHF-UCL positive regulation of interleukin-8 production Inferred from direct assay. Source: BHF-UCL positive regulation of macrophage activation Inferred from direct assay. Source: BHF-UCL positive regulation of respiratory burst involved in inflammatory response Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of toll-like receptor 4 signaling pathway Inferred from direct assay. Source: BHF-UCL positive regulation of tumor necrosis factor production Inferred from direct assay. Source: BHF-UCL
Cellular component	extracellular space Inferred from direct assay Ref.1. Source: BHF-UCL
Molecular function	Gram-negative bacterial cell surface binding Inferred from direct assay. Source: BHF-UCL Gram-positive bacterial cell surface binding Inferred from direct assay. Source: BHF-UCL lipid binding Inferred from electronic annotation. Source: InterPro lipopolysaccharide binding Inferred from sequence or structural similarity. Source: BHF-UCL lipoteichoic acid binding Inferred from direct assay. Source: MGI receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRDX4	Q13162	4	EBI-3927059,EBI-2211957

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25
	Chain	26 – 481	456	Lipopolysaccharide-binding protein		PRO_0000017158
Amino acid modifications
	Glycosylation	300	1	N-linked (GlcNAc...) Potential
	Glycosylation	355	1	N-linked (GlcNAc...) Potential
	Glycosylation	386	1	N-linked (GlcNAc...) Potential
	Glycosylation	394	1	N-linked (GlcNAc...) Ref.10
Natural variations
	Natural variant	9	1	P → L. Corresponds to variant rs2232580 [ dbSNP | Ensembl ].		VAR_028243
	Natural variant	111	1	R → Q. Corresponds to variant rs2232583 [ dbSNP | Ensembl ].		VAR_049737
	Natural variant	125	1	L → I. Corresponds to variant rs2232585 [ dbSNP | Ensembl ].		VAR_028244
	Natural variant	147	1	E → K. Corresponds to variant rs36015492 [ dbSNP | Ensembl ].		VAR_049738
	Natural variant	157	1	S → C. Corresponds to variant rs2232586 [ dbSNP | Ensembl ].		VAR_061293
	Natural variant	166	1	V → M. Corresponds to variant rs5744204 [ dbSNP | Ensembl ].		VAR_028245
	Natural variant	242	1	M → I. Corresponds to variant rs2232601 [ dbSNP | Ensembl ].		VAR_028246
	Natural variant	283	1	D → G. Corresponds to variant rs2232607 [ dbSNP | Ensembl ].		VAR_028247
	Natural variant	294	1	H → R. Corresponds to variant rs2232608 [ dbSNP | Ensembl ].		VAR_028248
	Natural variant	333	1	P → L. Corresponds to variant rs2232613 [ dbSNP | Ensembl ].		VAR_028249
	Natural variant	339	1	L → F. Corresponds to variant rs5744212 [ dbSNP | Ensembl ].		VAR_028250
	Natural variant	364	1	I → T. Corresponds to variant rs2232615 [ dbSNP | Ensembl ].		VAR_049739
	Natural variant	436	1	F → L. Ref.1 Ref.3 Ref.5 Corresponds to variant rs2232618 [ dbSNP | Ensembl ].		VAR_028251
	Natural variant	445	1	A → T. Corresponds to variant rs2232619 [ dbSNP | Ensembl ].		VAR_028252
Experimental info
	Sequence conflict	6	1	R → H Ref.2
	Sequence conflict	22	1	E → C Ref.2
	Sequence conflict	82	1	N → K in AAC39547. Ref.4
	Sequence conflict	128	1	S → F in AAC39547. Ref.4
	Sequence conflict	154 – 157	4	VTAS → GYCL in AAA59493. Ref.1
	Sequence conflict	174	1	L → S in AAA59493. Ref.1
	Sequence conflict	257	1	R → S in AAC39547. Ref.4
	Sequence conflict	266 – 270	5	VMSLP → A in AAA59493. Ref.1
	Sequence conflict	369	1	L → H in AAC39547. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P18428 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 5A0E4B9E5E604C72	FASTA	481	53,384
	10 20 30 40 50 60 MGALARALPS ILLALLLTST PEALGANPGL VARITDKGLQ YAAQEGLLAL QSELLRITLP 70 80 90 100 110 120 DFTGDLRIPH VGRGRYEFHS LNIHSCELLH SALRPVPGQG LSLSISDSSI RVQGRWKVRK 130 140 150 160 170 180 SFFKLQGSFD VSVKGISISV NLLLGSESSG RPTVTASSCS SDIADVEVDM SGDLGWLLNL 190 200 210 220 230 240 FHNQIESKFQ KVLESRICEM IQKSVSSDLQ PYLQTLPVTT EIDSFADIDY SLVEAPRATA 250 260 270 280 290 300 QMLEVMFKGE IFHRNHRSPV TLLAAVMSLP EEHNKMVYFA ISDYVFNTAS LVYHEEGYLN 310 320 330 340 350 360 FSITDDMIPP DSNIRLTTKS FRPFVPRLAR LYPNMNLELQ GSVPSAPLLN FSPGNLSVDP 370 380 390 400 410 420 YMEIDAFVLL PSSSKEPVFR LSVATNVSAT LTFNTSKITG FLKPGKVKVE LKESKVGLFN 430 440 450 460 470 480 AELLEALLNY YILNTFYPKF NDKLAEGFPL PLLKRVQLYD LGLQIHKDFL FLGANVQYMR V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of lipopolysaccharide binding protein." Schumann R.R., Leong S.R., Flaggs G.W., Gray P.W., Wright S.D., Mathison J.C., Tobias P.S., Ulevitch R.J. Science 249:1429-1431(1990) [PubMed: 2402637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-436.
[2]	"Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-binding protein. LPS binding properties and effects on LPS-mediated cell activation." Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L., Lane J.C., Leong S.R., Thornton M.B., Miller K.L., Scott R.W. J. Biol. Chem. 269:17411-17416(1994) [PubMed: 7517398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The genomic organization of the genes for human lipopolysaccharide binding protein (LBP) and bactericidal permeability increasing protein (BPI) is highly conserved." Hubacek J.A., Buchler C., Aslanidis C., Schmitz G. Biochem. Biophys. Res. Commun. 236:427-430(1997) [PubMed: 9240454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-436.
[4]	"Similar organization of the lipopolysaccharide-binding protein (LBP) and phospholipid transfer protein (PLTP) genes suggests a common gene family of lipid-binding proteins." Kirschning C.J., Au-Young J., Lamping N., Reuter D., Pfeil D., Seilhamer J.J., Schumann R.R. Genomics 46:416-425(1997) [PubMed: 9441745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Cloning and sequencing of human lipopolysaccharide-binding protein gene." Long J.Y., Liu J.Q., Xue Y.N., Wang H.X. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:469-471(1998) Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-436. Tissue: Liver.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[7]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"Cloning and characterization of the human LBP upstream sequence." Sutton C.L., Smith R.I.F., Centola M.B., Theofan G. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394, MASS SPECTROMETRY. Tissue: Liver.
[11]	"The BPI/LBP family of proteins: a structural analysis of conserved regions." Beamer L.J., Carroll S.F., Eisenberg D. Protein Sci. 7:906-914(1998) [PubMed: 9568897] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M35533 mRNA. Translation: AAA59493.1. X98657 , X98658, X98659, X98660, X98661, X98662, X98663, X98664, X98665, X98666, X98667, X98668 Genomic DNA. Translation: CAA67226.1. AF013512 , AF013500, AF013501, AF013502, AF013503, AF013504, AF013505, AF013506, AF013507, AF013508, AF013509, AF013510, AF013511 Genomic DNA. Translation: AAC39547.1. AF105067 mRNA. Translation: AAD21962.1. AK313625 mRNA. Translation: BAG36385.1. AL080249 Genomic DNA. Translation: CAC10462.1. CH471077 Genomic DNA. Translation: EAW76034.1. L42172 Genomic DNA. Translation: AAA66446.1.
IPI	IPI00032311.
PIR	A35843. A54136.
RefSeq	NP_004130.2. NM_004139.2.
UniGene	Hs.154078.
3D structure databases
ProteinModelPortal	P18428.
SMR	P18428. Positions 26-479.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-90N.
IntAct	P18428. 13 interactions.
STRING	P18428.
Protein family/group databases
TCDB	1.C.40.1.2. bactericidal permeability increasing protein (BPIP) family.
Polymorphism databases
DMDM	116242615.
Proteomic databases
PeptideAtlas	P18428.
PRIDE	P18428.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217407; ENSP00000217407; ENSG00000129988.
GeneID	3929.
KEGG	hsa:3929.
UCSC	uc002xic.1. human.
Organism-specific databases
CTD	3929.
GeneCards	GC20P036974.
H-InvDB	HIX0015804.
HGNC	HGNC:6517. LBP.
HPA	CAB025905. HPA001508.
MIM	151990. gene.
neXtProt	NX_P18428.
PharmGKB	PA30303.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13159.
HOGENOM	HBG278860.
HOVERGEN	HBG002797.
InParanoid	P18428.
OMA	RNHRSPV.
OrthoDB	EOG4JDH6R.
PhylomeDB	P18428.
Enzyme and pathway databases
Pathway_Interaction_DB	il6_7pathway. IL6-mediated signaling events.
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P18428.
Bgee	P18428.
CleanEx	HS_LBP.
Genevestigator	P18428.
GermOnline	ENSG00000129988. Homo sapiens.
Family and domain databases
InterPro	IPR017943. Bactericidal_perm-incr_a/b_dom. IPR001124. Lipid-bd_serum_glycop_C. IPR017954. Lipid-bd_serum_glycop_CS. IPR017942. Lipid-bd_serum_glycop_N. [Graphical view]
KO	K05399.
Pfam	PF01273. LBP_BPI_CETP. 1 hit. PF02886. LBP_BPI_CETP_C. 1 hit. [Graphical view]
SMART	SM00328. BPI1. 1 hit. SM00329. BPI2. 1 hit. [Graphical view]
SUPFAM	SSF55394. Bactericidal_perm-incr_a/b_dom. 2 hits.
PROSITE	PS00400. LBP_BPI_CETP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	15427.
SOURCE	Search...

Entry information

Entry name

LBP_HUMAN

Accession

Primary (citable) accession number: P18428
Secondary accession number(s): B2R938 , O43438, Q92672, Q9H403, Q9UD66

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.