BPI_RAT
ID BPI_RAT Reviewed; 482 AA.
AC Q6AXU0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Bactericidal permeability-increasing protein;
DE Short=BPI;
DE Flags: Precursor;
GN Name=Bpi;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. {ECO:0000250}.
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 -!- 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; BC079318; AAH79318.1; -; mRNA.
DR RefSeq; NP_001004079.1; NM_001004079.1.
DR AlphaFoldDB; Q6AXU0; -.
DR SMR; Q6AXU0; -.
DR STRING; 10116.ENSRNOP00000049523; -.
DR GlyGen; Q6AXU0; 2 sites.
DR PaxDb; Q6AXU0; -.
DR GeneID; 296321; -.
DR KEGG; rno:296321; -.
DR CTD; 671; -.
DR RGD; 1303179; Bpi.
DR VEuPathDB; HostDB:ENSRNOG00000034195; -.
DR eggNOG; KOG4160; Eukaryota.
DR HOGENOM; CLU_028970_3_2_1; -.
DR InParanoid; Q6AXU0; -.
DR OMA; VGWLIRL; -.
DR OrthoDB; 1242894at2759; -.
DR PhylomeDB; Q6AXU0; -.
DR TreeFam; TF315617; -.
DR Reactome; R-RNO-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6803157; Antimicrobial peptides.
DR PRO; PR:Q6AXU0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000034195; Expressed in testis and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; TAS:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:RGD.
DR GO; GO:0042742; P:defense response to bacterium; IDA:RGD.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:0043031; P:negative regulation of macrophage activation; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
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; 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.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..482
FT /note="Bactericidal permeability-increasing protein"
FT /id="PRO_0000358333"
FT REGION 28..38
FT /note="Central sheet, part 1"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 37..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:0000250"
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 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 DISULFID 161..201
FT /evidence="ECO:0000250"
SQ SEQUENCE 482 AA; 53752 MW; 269591C4C2F5A6D1 CRC64;
MAWGPDNVRK WSSLALLAIV GTALTAATDP GFVARISQKG LDFVCQESMV ELQKELLAIS
IPDFSGDFKI KHLGKGTYEF YSMAVEGFHI PDPQIKLLPS DGLQLSITSA SIKISGRWKY
RKNILKASGN FQLSIQGVSI IADLILGNDP SGRITITCST CDSHINSVRI KVSGSMLGWL
IQLFHRKIET SLKKTIYKKI CKIVRNSVSA KLQPYVKTLP VVAKVDDITS IDYSLLAPPM
TTDKFLEGQL RGEFFWRGHH GPFPAVPPVM NILPNNNYMV CMGISDYFFN TAEFAYQESE
TLKITLRDQL LAKDARYHLN TDFLKTFLPE VAKKFPSMGL QLLISAPLFA HLNIQPSGLS
LSPNLETRAF VVLPNSSLIP LFLLGMKTNA SLEVNAMKNR LIGEMKLGRL LLELKQSNFG
SFKVELLEDV INYLMSTMVL PKINEKLRRG FPLPLPAGIQ LINSILYSSQ NFLLLEADLH
RT
