ID I3L5U6_PIG Unreviewed; 586 AA.
AC I3L5U6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Lipopolysaccharide-binding protein {ECO:0000256|ARBA:ARBA00015119, ECO:0000256|RuleBase:RU369039};
DE Short=LBP {ECO:0000256|RuleBase:RU369039};
GN Name=LBP {ECO:0000313|Ensembl:ENSSSCP00000019396.3,
GN ECO:0000313|VGNC:VGNC:96403};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000019396.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000019396.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000019396.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000019396.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU369039}.
CC -!- SUBUNIT: When bound to LPS, interacts (via C-terminus) with soluble and
CC membrane-bound CD14. {ECO:0000256|ARBA:ARBA00011317,
CC ECO:0000256|RuleBase:RU369039}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU369039}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000256|ARBA:ARBA00007292}.
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DR AlphaFoldDB; I3L5U6; -.
DR SMR; I3L5U6; -.
DR STRING; 9823.ENSSSCP00000019396; -.
DR PaxDb; 9823-ENSSSCP00000019396; -.
DR PeptideAtlas; I3L5U6; -.
DR Ensembl; ENSSSCT00000032321.3; ENSSSCP00000019396.3; ENSSSCG00000028758.4.
DR VGNC; VGNC:96403; LBP.
DR GeneTree; ENSGT01100000263545; -.
DR HOGENOM; CLU_028970_3_2_1; -.
DR InParanoid; I3L5U6; -.
DR TreeFam; TF315617; -.
DR Reactome; R-SSC-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-SSC-166020; Transfer of LPS from LBP carrier to CD14.
DR Reactome; R-SSC-5686938; Regulation of TLR by endogenous ligand.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000028758; Expressed in right lobe of liver and 18 other cell types or tissues.
DR ExpressionAtlas; I3L5U6; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IBA:GO_Central.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IBA:GO_Central.
DR CDD; cd00025; BPI1; 1.
DR CDD; cd00026; BPI2; 1.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR032942; BPI/LBP/Plunc.
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; BACTERICIDAL PERMEABILITY-INCREASING BPI PROTEIN-RELATED; 1.
DR PANTHER; PTHR10504:SF66; LIPOPOLYSACCHARIDE-BINDING PROTEIN; 1.
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 permeability-increasing protein, BPI; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 1: Evidence at protein level;
KW Antibiotic {ECO:0000256|RuleBase:RU369039};
KW Antimicrobial {ECO:0000256|RuleBase:RU369039};
KW Disulfide bond {ECO:0000256|RuleBase:RU369039};
KW Glycoprotein {ECO:0000256|RuleBase:RU369039};
KW Immunity {ECO:0000256|RuleBase:RU369039};
KW Innate immunity {ECO:0000256|RuleBase:RU369039};
KW Proteomics identification {ECO:0007829|PeptideAtlas:I3L5U6};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Secreted {ECO:0000256|RuleBase:RU369039};
KW Signal {ECO:0000256|RuleBase:RU369039}.
FT DOMAIN 138..361
FT /note="Lipid-binding serum glycoprotein N-terminal"
FT /evidence="ECO:0000259|SMART:SM00328"
FT DOMAIN 376..579
FT /note="Lipid-binding serum glycoprotein C-terminal"
FT /evidence="ECO:0000259|SMART:SM00329"
FT REGION 58..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 64308 MW; CD98E0EF7BCCE28D CRC64;
MSVLYGRWSW SHPRRQSTAC RVLLALSFAV QAPHTRPVQT LEKNSQLSAR GKAFAAKVPV
TGPPFPDPGN PPHSGAAKPS GLSYLRELGP ACGCIGPDPA LWESMMGASA GALPSLLLGI
LLTSILGSLG ANPGLVARIT NKGLEYVARE GVATLQSKLH EVTLPDFNGD FKIKYMGRGH
YEFHSLDIHS CELLGSTLTP LPGQGLYLAI SDSSIRVKGK WKVRKGILKL DGSFDVKVKG
ITISVNLLLG SESSGRPTVA VSSCSSHIDD VETHMSGDLS WLLNLFHNQI ESRFRRTLES
KICEEIQDLV ASDLQPYLQT VPVTTEIDNL AGIDYSLVEA PRATAQMLDV MIKGEIFSLD
HRSPVGFLAP VMRLPEEHSR MVYFAVSDYV FKTASLVYNE AGFLNFSITD DLVPPTSNIR
LTTNSFRTFV PRLARLYPNM NLELRGAMVS APFLNFGSGN LSSTPQIEVE GFVLLPNSVR
EPVFRLGMAT NVSAALTFNT SKITGFLKPG KIQMELKESK VGIFNVELLE ALLNYYLLNN
LYPKVNDKLA EGFPLPLLNY IQLHDPVLQI HKDFLLLGTN IRYLRV
//
