ID   BPI_RABIT               Reviewed;         445 AA.
AC   Q28739;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Bactericidal permeability-increasing protein;
DE            Short=BPI;
DE   Flags: Fragment;
GN   Name=BPI;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Bone marrow;
RA   Weiss J., Weinrauch Y., Levy O., Flynn S.;
RL   Submitted (JUN-1996) 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. {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   -!- 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}.
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; U61270; AAB03812.1; -; mRNA.
DR   AlphaFoldDB; Q28739; -.
DR   SMR; Q28739; -.
DR   STRING; 9986.ENSOCUP00000011699; -.
DR   PRIDE; Q28739; -.
DR   eggNOG; KOG4160; Eukaryota.
DR   InParanoid; Q28739; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
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.
FT   CHAIN           <1..445
FT                   /note="Bactericidal permeability-increasing protein"
FT                   /id="PRO_0000089157"
FT   REGION          184..248
FT                   /note="Central sheet, part 2"
FT                   /evidence="ECO:0000250|UniProtKB:P17213"
FT   REGION          198..203
FT                   /note="Cleavage sites for elastase"
FT                   /evidence="ECO:0000255"
FT   REGION          249..419
FT                   /note="C-terminal barrel"
FT                   /evidence="ECO:0000250|UniProtKB:P17213"
FT   REGION          426..445
FT                   /note="Central sheet, part 3"
FT                   /evidence="ECO:0000250|UniProtKB:P17213"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..164
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   445 AA;  48837 MW;  209AE0894FEDACFC CRC64;
     QKGLDYACQQ GVAVLQKELE KIRIPDVSGK FKLRPFGKGH YNFHSLVVRS FQLPNPQIRL
     QPNVGLRVSI SNANVRIGGR WKARKGFIKV RGKFDLSVEG VSISADLKLG SVPASGRATV
     TCSSCSSNIN RARLRSQASW GGWLKLFHKR IESSLRNTMN SKICQVLTSS VSSKLQPYVE
     TLPLKERLDS VAGIDYSLVA PPRATADSLD MQLKGEFYNV ARPSPPPFMP PPMAIPSLHD
     RMIYLAISDY LFNTAALVYQ QAGAFGLTLR DDMIPKESKS RLTTKFLGKA LPQVAKMFPN
     MNVQLTLSVS SPPHLTTRPT GIALTAAVDL QAFAILPNSS LASLFLLGLK LNTSAKIGTK
     ADKLVGELTL GRLILELKHS NIGSFPVQLL QALMDYVLSA VVLPKVNEKL QRGLPLPMPR
     KVQLYDLVLQ PHQDFLLLGA NVQHG