ID A0A1V4KKN8_PATFA Unreviewed; 503 AA.
AC A0A1V4KKN8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Bactericidal permeability-increasing protein {ECO:0000256|ARBA:ARBA00017827, ECO:0000256|RuleBase:RU369039};
DE Short=BPI {ECO:0000256|RuleBase:RU369039};
GN Name=BPI {ECO:0000313|EMBL:OPJ85022.1};
GN ORFNames=AV530_018062 {ECO:0000313|EMBL:OPJ85022.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ85022.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ85022.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ85022.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ85022.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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:0000256|RuleBase:RU369039}.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked.
CC {ECO:0000256|ARBA:ARBA00025943, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ85022.1}.
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DR EMBL; LSYS01002950; OPJ85022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KKN8; -.
DR STRING; 372326.A0A1V4KKN8; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd00025; BPI1; 1.
DR CDD; cd00026; BPI2; 1.
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; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR10504; BACTERICIDAL PERMEABILITY-INCREASING BPI PROTEIN-RELATED; 1.
DR PANTHER; PTHR10504:SF84; BACTERICIDAL PERMEABILITY-INCREASING 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.
PE 3: Inferred from homology;
KW Antibiotic {ECO:0000256|ARBA:ARBA00023022, ECO:0000256|RuleBase:RU369039};
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529,
KW ECO:0000256|RuleBase:RU369039};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002417-50,
KW ECO:0000256|RuleBase:RU369039};
KW Glycoprotein {ECO:0000256|RuleBase:RU369039};
KW Immunity {ECO:0000256|ARBA:ARBA00022859, ECO:0000256|RuleBase:RU369039};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588,
KW ECO:0000256|RuleBase:RU369039};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Secreted {ECO:0000256|RuleBase:RU369039};
KW Signal {ECO:0000256|RuleBase:RU369039}.
FT DOMAIN 54..275
FT /note="Lipid-binding serum glycoprotein N-terminal"
FT /evidence="ECO:0000259|SMART:SM00328"
FT DOMAIN 290..493
FT /note="Lipid-binding serum glycoprotein C-terminal"
FT /evidence="ECO:0000259|SMART:SM00329"
FT DISULFID 178..217
FT /evidence="ECO:0000256|PIRSR:PIRSR002417-50"
SQ SEQUENCE 503 AA; 55120 MW; 3426F69AAF95CDD1 CRC64;
MMELLLDIKA VRKTVQQWHR RAARMRAQSL AVACGALALC LALTDATNPG FVVRITQAGL
DYAHQHGIAI LEKELARLKL PDISGDFRFL GKVYYQISNL DLRTFHLPHS RISLVPNVGL
QVSISNAFAE LNGNWRVKYG LIRSSGSFNL KVENIYIRID LRLGSDSSGK PTVDTSSCST
RISKVHVHFS GKLSLLYNLF KKAVESRLRK ALEGKVCDNV AKAVRNELQP YAQTLPVTAR
IDAMTGIDYA LVASPTATAR SLDTGLKGEF FSLAHRSTVP FPPLPLGLPP DHERMVYFGA
SSYFFNTASF AYHSAGALVF EISDTMIPGG ADFHLNTSTF SAFIPQLETM YPKLPMKFRL
STRSAPFLSI GPGGFSLQPV VDVQAFAVLP NATLAPLFLL SLTTNVSAVV DVTSGHIVGS
LTVGRIKLSL KRSDVGAFQV RMLQSIMNIV ASKILLPRLN ARLGEGFPLP LPDRIQLSNI
LVQFHKNFLL LGADVQFQPQ IGK
//