BPI_BOVIN
ID BPI_BOVIN Reviewed; 482 AA.
AC P17453; Q3T0P4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Bactericidal permeability-increasing protein;
DE Short=BPI;
DE Flags: Precursor;
GN Name=BPI;
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 [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=2349103; DOI=10.1093/nar/18.10.3052;
RA Leong S.R., Camerato T.;
RT "Nucleotide sequence of the bovine bactericidal permeability increasing
RT protein (BPI).";
RL Nucleic Acids Res. 18:3052-3052(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The cytotoxic action of BPI is limited to many species of
CC Gram-negative bacteria; this specificity may be explained by a strong
CC affinity of the very basic N-terminal half for the negatively charged
CC lipopolysaccharides that are unique to the Gram-negative bacterial
CC outer envelope.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P17213}.
CC Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}.
CC Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
CC granules. {ECO:0000250|UniProtKB:P17213}.
CC -!- TISSUE SPECIFICITY: Restricted to cells of the myeloid series.
CC -!- DOMAIN: The N-terminal region may be exposed to the interior of the
CC granule, whereas the C-terminal portion may be embedded in the
CC membrane. During phagocytosis and degranulation, proteases may be
CC released and activated and cleave BPI at the junction of the N- and C-
CC terminal portions of the molecule, providing controlled release of the
CC N-terminal antibacterial fragment when bacteria are ingested (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The N- and C-terminal barrels adopt an identical fold despite
CC having only 13% of conserved residues. {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; X52563; CAA36797.1; -; mRNA.
DR EMBL; BC102310; AAI02311.1; -; mRNA.
DR PIR; S10180; S10180.
DR RefSeq; NP_776320.1; NM_173895.2.
DR AlphaFoldDB; P17453; -.
DR SMR; P17453; -.
DR STRING; 9913.ENSBTAP00000018669; -.
DR PaxDb; P17453; -.
DR PeptideAtlas; P17453; -.
DR PRIDE; P17453; -.
DR Ensembl; ENSBTAT00000018669; ENSBTAP00000018669; ENSBTAG00000014046.
DR GeneID; 280734; -.
DR KEGG; bta:280734; -.
DR CTD; 671; -.
DR VEuPathDB; HostDB:ENSBTAG00000014046; -.
DR VGNC; VGNC:97246; BPI.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230353; -.
DR HOGENOM; CLU_028970_3_2_1; -.
DR InParanoid; P17453; -.
DR OMA; VGWLIRL; -.
DR OrthoDB; 1242894at2759; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000014046; Expressed in ascending colon and 82 other tissues.
DR ExpressionAtlas; P17453; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative 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:0032715; P:negative regulation of interleukin-6 production; IBA:GO_Central.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IBA:GO_Central.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IBA:GO_Central.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IBA:GO_Central.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR030181; BPI.
DR InterPro; IPR030675; BPI/LBP.
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; PTHR10504; 1.
DR PANTHER; PTHR10504:SF84; PTHR10504:SF84; 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; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT CHAIN 27..482
FT /note="Bactericidal permeability-increasing protein"
FT /id="PRO_0000017153"
FT REGION 27..36
FT /note="Central sheet, part 1"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 36..219
FT /note="N-terminal barrel"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 221..285
FT /note="Central sheet, part 2"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 235..240
FT /note="Cleavage sites for elastase"
FT /evidence="ECO:0000255"
FT REGION 286..456
FT /note="C-terminal barrel"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 463..482
FT /note="Central sheet, part 3"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..201
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="S -> G (in Ref. 1; CAA36797)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="G -> S (in Ref. 1; CAA36797)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="H -> Q (in Ref. 1; CAA36797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 53442 MW; D2240AD128C58AE5 CRC64;
MARGPDTARR WATLVVLAAL STAVTTTNPG IVARITQKGL DYACQQGVLT LQKELEKITI
PNFSGNFKIK YLGKGQYSFF SMVIQGFNLP NSQIRPLPDK GLDLSIRDAS IKIRGKWKAR
KNFIKLGGNF DLSVEGISIL AGLNLGYDPA SGHSTVTCSS CSSGINTVRI HISGSSLGWL
IQLFRKRIES LLQKSMTRKI CEVVTSTVSS KLQPYFQTLP VTTKLDKVAG VDYSLVAPPR
ATANNLDWLL KGEFFSLAHR SPPPFAPPAL AFPSDHDRMV YLGISEYFFN TAGFVYQKAG
ALNLTLRDDM IPKESKFRLT TKFFGILIPQ VAKMFPDMQM QLFIWASLPP KLTMKPSGLD
LIFVLDTQAF AILPNSSLDP LFLLEMNLNL SVVVGAKSDR LIGELRLDKL LLELKHSDIG
PFSVESLQSV INYVMPTIVL PVINKKLQKG FPLPLPAYIE LFNLTLQPYQ DFLLFGADVH
YS
