ID A0A1D5PT25_CHICK Unreviewed; 469 AA.
AC A0A1D5PT25;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Bactericidal permeability-increasing protein {ECO:0000256|RuleBase:RU369039};
DE Short=BPI {ECO:0000256|RuleBase:RU369039};
GN Name=BPIFCB {ECO:0000313|Ensembl:ENSGALP00010021628.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010021628.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010021628.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010021628.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU369039}.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked.
CC {ECO:0000256|RuleBase:RU369039}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU369039}.
CC -!- DOMAIN: The N- and C-terminal barrels adopt an identical fold despite
CC having only 13% of conserved residues. {ECO:0000256|RuleBase:RU369039}.
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.
CC {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 RefSeq; XP_004937862.1; XM_004937805.2.
DR AlphaFoldDB; A0A1D5PT25; -.
DR SMR; A0A1D5PT25; -.
DR STRING; 9031.ENSGALP00000056066; -.
DR Ensembl; ENSGALT00010037288.1; ENSGALP00010021628.1; ENSGALG00010015515.1.
DR GeneID; 771461; -.
DR KEGG; gga:771461; -.
DR CTD; 771461; -.
DR VEuPathDB; HostDB:geneid_771461; -.
DR GeneTree; ENSGT01100000263545; -.
DR InParanoid; A0A1D5PT25; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000039479; Expressed in testis and 4 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:UniProtKB-UniRule.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
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; BACTERICIDAL PERMEABILITY-INCREASING BPI PROTEIN-RELATED; 1.
DR PANTHER; PTHR10504:SF17; BPI FOLD-CONTAINING FAMILY C PROTEIN; 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; Bactericidal permeability-increasing protein, BPI; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Secreted {ECO:0000256|RuleBase:RU369039};
KW Signal {ECO:0000256|RuleBase:RU369039}.
FT DOMAIN 27..247
FT /note="Lipid-binding serum glycoprotein N-terminal"
FT /evidence="ECO:0000259|SMART:SM00328"
FT DOMAIN 262..463
FT /note="Lipid-binding serum glycoprotein C-terminal"
FT /evidence="ECO:0000259|SMART:SM00329"
SQ SEQUENCE 469 AA; 52310 MW; 06378BD452FF8380 CRC64;
MVKICCSLLL LSLLSVQLKA NPGLKVRITQ KALEYAKKVG VEILKKNMEK EQFPDLIGYE
RFGLGNVHYN ISRIRVTAVE FPNVSISLIP RSGVKLVIRN ASLTIDMNWN IRTWMFKDGG
RSTVHISKVF VTATFSTPLD SIGHTSVSLS SCHTTSGDTD IKVNGKSGFL HDFFIKYLKK
PIHRSLATNS CPNIRSGIQM IAKDFQSLNV PVRIDDLAEI DYSLNSLEVF RPYIDMDLKG
IVYPAGNYTG PPYVATPFAI PDQNDSMLYL AFSEYFFQTS LFSYYTAGAF NITIAKETCR
YLNISTEMFG SIIPEIAKYP IIPYPVMMKL TATEIPLVSL QQDSFTLEIR ESMEVFAVLP
DSTTQSLFTV NVAANTSIAL NVFDQKLTGS LCLNRLQFSL AHSNVGSFEI SFLENILSYI
LQTEVIPSAN AKLSKGFPLP NLANIILTRP HITIAQGYVL ISTDAHYKH
//
