ID G1QYI0_NOMLE Unreviewed; 507 AA.
AC G1QYI0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 3.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Bactericidal permeability-increasing protein {ECO:0000256|RuleBase:RU369039};
DE Short=BPI {ECO:0000256|RuleBase:RU369039};
GN Name=BPIFC {ECO:0000313|Ensembl:ENSNLEP00000006001.3};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000006001.3, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000006001.3, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000006001.3}
RP IDENTIFICATION.
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 EMBL; ADFV01177895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01177896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01177897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003258177.1; XM_003258129.1.
DR AlphaFoldDB; G1QYI0; -.
DR STRING; 61853.ENSNLEP00000006001; -.
DR Ensembl; ENSNLET00000006312.3; ENSNLEP00000006001.3; ENSNLEG00000004931.3.
DR GeneID; 100596469; -.
DR KEGG; nle:100596469; -.
DR CTD; 254240; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01100000263545; -.
DR HOGENOM; CLU_028970_3_0_1; -.
DR InParanoid; G1QYI0; -.
DR OMA; TEPPMIN; -.
DR OrthoDB; 4081151at2759; -.
DR TreeFam; TF315617; -.
DR Proteomes; UP000001073; Chromosome 7b.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
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|PIRSR:PIRSR002417-50,
KW 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:UP000001073};
KW Secreted {ECO:0000256|RuleBase:RU369039};
KW Signal {ECO:0000256|RuleBase:RU369039, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..507
FT /note="Bactericidal permeability-increasing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014120212"
FT DOMAIN 33..257
FT /note="Lipid-binding serum glycoprotein N-terminal"
FT /evidence="ECO:0000259|SMART:SM00328"
FT DOMAIN 272..474
FT /note="Lipid-binding serum glycoprotein C-terminal"
FT /evidence="ECO:0000259|SMART:SM00329"
FT DISULFID 161..200
FT /evidence="ECO:0000256|PIRSR:PIRSR002417-50"
SQ SEQUENCE 507 AA; 56324 MW; 1473F5CB773A0F66 CRC64;
MCTKTIPVLW GCFLLWSLYV SSSQTIYPGI KARITQRALD YGVQAGMKMI EQMLKEKNLP
DLSGSESLEF LKVDYVNYNF SNIKISAFSF PNTSLAFVPG VGIKTLTNHG TANISTDWGF
ESPLFQDTGG ADLFLSGVYF TGIIILTRND FGHPTLKLQD CYAQLSHAHI SFSGELSVLY
NSFAEPMEKP ILKNLNEMLC PIIASEVKAL NANLSTLEVL TKIDNYTLLD YSLISSPEIT
ENYLDLNLKG LFYPLENLTD PPFSPVPFVL PERSNSMLYI GIAEYFFKSA SFAYFTAGAF
NITLSTKEIS NHFVQNSQGL GNVLSRIAEI YILSQPFMVR IMATEPPMIN LQPGNFTLDV
PASIMMLTQP KNSTVETIVS MDFVASTSVG LVILGQRLVC SLSLNRFRLA LPESNRSNIE
ILRFENILSS ILHFGVLPLA NAKLQQGFPL PNPHKISFVN SDIEVLEGFL LISTDLKYET
SSKQQPSFHG WEGLNLISGQ WRGKSAP
//
