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Bactericidal permeability-increasing protein (BPI) (Fragment)

 BPI_RABIT               Reviewed;         445 AA.
Q28739;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
18-JUL-2018, entry version 81.
RecName: Full=Bactericidal permeability-increasing protein;
Short=BPI;
Flags: Fragment;
Name=BPI;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New Zealand white; TISSUE=Bone marrow;
Weiss J., Weinrauch Y., Levy O., Flynn S.;
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: The cytotoxic action of BPI is limited to many species
of Gram-negative bacteria; this specificity may be explained by a
strong affinity of the very basic N-terminal half for the
negatively charged lipopolysaccharides that are unique to the
Gram-negative bacterial outer envelope. {ECO:0000250}.
-!- SUBUNIT: Monomer. Homodimer; disulfide-linked (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P17213}.
Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}.
Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
granules. {ECO:0000250|UniProtKB:P17213}.
-!- TISSUE SPECIFICITY: Restricted to cells of the myeloid series.
-!- DOMAIN: The N-terminal region may be exposed to the interior of
the granule, whereas the C-terminal portion may be embedded in the
membrane. During phagocytosis and degranulation, proteases may be
released and activated and cleave BPI at the junction of the
N- and C-terminal portions of the molecule, providing controlled
release of the N-terminal antibacterial fragment when bacteria are
ingested (By similarity). {ECO:0000250}.
-!- DOMAIN: The N- and C-terminal barrels adopt an identical fold
despite having only 13% of conserved residues.
{ECO:0000250|UniProtKB:P17213}.
-!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
family. {ECO:0000305}.
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EMBL; U61270; AAB03812.1; -; mRNA.
UniGene; Ocu.2111; -.
ProteinModelPortal; Q28739; -.
SMR; Q28739; -.
STRING; 9986.ENSOCUP00000011699; -.
PRIDE; Q28739; -.
eggNOG; KOG4160; Eukaryota.
eggNOG; ENOG410Z88E; LUCA.
HOGENOM; HOG000231250; -.
HOVERGEN; HBG002797; -.
InParanoid; Q28739; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
GO; GO:0006955; P:immune response; IEA:InterPro.
InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
InterPro; IPR030181; BPI.
InterPro; IPR030675; BPI/LBP.
InterPro; IPR032942; BPI/LBP/Plunc.
InterPro; IPR001124; Lipid-bd_serum_glycop_C.
InterPro; IPR017942; Lipid-bd_serum_glycop_N.
PANTHER; PTHR10504; PTHR10504; 1.
PANTHER; PTHR10504:SF84; PTHR10504:SF84; 1.
Pfam; PF01273; LBP_BPI_CETP; 1.
Pfam; PF02886; LBP_BPI_CETP_C; 1.
PIRSF; PIRSF002417; Lipid_binding_protein; 1.
SMART; SM00328; BPI1; 1.
SMART; SM00329; BPI2; 1.
SUPFAM; SSF55394; SSF55394; 2.
2: Evidence at transcript level;
Antibiotic; Antimicrobial; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Reference proteome; Secreted.
CHAIN <1 445 Bactericidal permeability-increasing
protein.
/FTId=PRO_0000089157.
REGION 184 248 Central sheet, part 2.
{ECO:0000250|UniProtKB:P17213}.
REGION 198 203 Cleavage sites for elastase.
{ECO:0000255}.
REGION 249 419 C-terminal barrel.
{ECO:0000250|UniProtKB:P17213}.
REGION 426 445 Central sheet, part 3.
{ECO:0000250|UniProtKB:P17213}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 125 164 {ECO:0000250}.
NON_TER 1 1
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


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