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Protein

Bactericidal permeability-increasing protein

Gene

BPI

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.2 Publications

GO - Molecular functioni

  • lipopolysaccharide binding Source: BHF-UCL

GO - Biological processi

  • defense response to Gram-negative bacterium Source: InterPro
  • immune response Source: Ensembl
  • negative regulation of interleukin-6 production Source: BHF-UCL
  • negative regulation of interleukin-8 production Source: BHF-UCL
  • negative regulation of macrophage activation Source: BHF-UCL
  • negative regulation of tumor necrosis factor production Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101425-MONOMER.
ReactomeiR-HSA-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6803157. Antimicrobial peptides.

Protein family/group databases

TCDBi1.C.40.1.1. the bactericidal permeability increasing protein (bpip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Bactericidal permeability-increasing protein
Short name:
BPI
Alternative name(s):
CAP 57
Gene namesi
Name:BPI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:1095. BPI.

Subcellular locationi

  • Secreted 1 Publication
  • Cytoplasmic granule membrane 1 Publication

  • Note: Membrane-associated in polymorphonuclear Leukocytes (PMN) granules.1 Publication

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: InterPro
  • integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49S → C: No impairment of secretion and increased propensity for dimer formation. 1 Publication1
Mutagenesisi163C → A: No impairment of secretion and/or biological activity. Loss of dimer formation. 1 Publication1
Mutagenesisi166C → S: Poorly secreted. Loss of LPS-binding and biological activity. 1 Publication1
Mutagenesisi206C → A: Not secreted. 1 Publication1

Organism-specific databases

DisGeNETi671.
OpenTargetsiENSG00000101425.
PharmGKBiPA25403.

Polymorphism and mutation databases

BioMutaiBPI.
DMDMi215274242.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 314 PublicationsAdd BLAST31
ChainiPRO_000001715432 – 487Bactericidal permeability-increasing proteinAdd BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi166 ↔ 2061 Publication
Glycosylationi380N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP17213.
MaxQBiP17213.
PaxDbiP17213.
PeptideAtlasiP17213.
PRIDEiP17213.

PTM databases

iPTMnetiP17213.
PhosphoSitePlusiP17213.

Expressioni

Tissue specificityi

Restricted to cells of the myeloid series.

Gene expression databases

BgeeiENSG00000101425.
ExpressionAtlasiP17213. baseline and differential.
GenevisibleiP17213. HS.

Organism-specific databases

HPAiHPA061284.

Interactioni

Subunit structurei

Monomer. Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000262865.

Structurei

Secondary structure

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 41Combined sources7
Helixi42 – 60Combined sources19
Beta strandi68 – 71Combined sources4
Beta strandi75 – 79Combined sources5
Beta strandi81 – 93Combined sources13
Beta strandi97 – 102Combined sources6
Turni103 – 105Combined sources3
Beta strandi106 – 126Combined sources21
Beta strandi129 – 153Combined sources25
Turni154 – 157Combined sources4
Beta strandi158 – 169Combined sources12
Beta strandi172 – 176Combined sources5
Helixi180 – 182Combined sources3
Helixi183 – 192Combined sources10
Helixi194 – 215Combined sources22
Helixi217 – 221Combined sources5
Beta strandi226 – 229Combined sources4
Beta strandi231 – 233Combined sources3
Beta strandi235 – 237Combined sources3
Beta strandi240 – 242Combined sources3
Beta strandi248 – 255Combined sources8
Beta strandi258 – 260Combined sources3
Beta strandi282 – 290Combined sources9
Helixi291 – 303Combined sources13
Beta strandi307 – 312Combined sources6
Helixi313 – 315Combined sources3
Helixi326 – 330Combined sources5
Beta strandi333 – 335Combined sources3
Helixi336 – 339Combined sources4
Beta strandi344 – 350Combined sources7
Beta strandi356 – 360Combined sources5
Beta strandi363 – 367Combined sources5
Beta strandi369 – 377Combined sources9
Beta strandi383 – 392Combined sources10
Beta strandi395 – 401Combined sources7
Beta strandi403 – 412Combined sources10
Beta strandi416 – 424Combined sources9
Helixi429 – 432Combined sources4
Helixi433 – 443Combined sources11
Helixi445 – 454Combined sources10
Beta strandi464 – 474Combined sources11
Beta strandi477 – 486Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BP1X-ray2.40A32-487[»]
1EWFX-ray1.70A32-487[»]
ProteinModelPortaliP17213.
SMRiP17213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17213.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 193N-terminal barrel1 PublicationAdd BLAST184
Regioni194 – 359Central sheet1 PublicationAdd BLAST166
Regioni240 – 245Cleavage sites for elastaseSequence analysis6
Regioni260 – 430C-terminal barrel1 PublicationAdd BLAST171

Domaini

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.1 Publication
The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4160. Eukaryota.
ENOG410Z88E. LUCA.
GeneTreeiENSGT00730000110583.
HOVERGENiHBG002797.
InParanoidiP17213.
OMAiELKHSDV.
OrthoDBiEOG091G08NV.
PhylomeDBiP17213.
TreeFamiTF315617.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR030181. BPI.
IPR030675. BPI/LBP.
IPR032942. BPI/LBP/Plunc.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504. PTHR10504. 1 hit.
PTHR10504:SF84. PTHR10504:SF84. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002417. Lipid_binding_protein. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRENMARGPC NAPRWASLMV LVAIGTAVTA AVNPGVVVRI SQKGLDYASQ
60 70 80 90 100
QGTAALQKEL KRIKIPDYSD SFKIKHLGKG HYSFYSMDIR EFQLPSSQIS
110 120 130 140 150
MVPNVGLKFS ISNANIKISG KWKAQKRFLK MSGNFDLSIE GMSISADLKL
160 170 180 190 200
GSNPTSGKPT ITCSSCSSHI NSVHVHISKS KVGWLIQLFH KKIESALRNK
210 220 230 240 250
MNSQVCEKVT NSVSSELQPY FQTLPVMTKI DSVAGINYGL VAPPATTAET
260 270 280 290 300
LDVQMKGEFY SENHHNPPPF APPVMEFPAA HDRMVYLGLS DYFFNTAGLV
310 320 330 340 350
YQEAGVLKMT LRDDMIPKES KFRLTTKFFG TFLPEVAKKF PNMKIQIHVS
360 370 380 390 400
ASTPPHLSVQ PTGLTFYPAV DVQAFAVLPN SSLASLFLIG MHTTGSMEVS
410 420 430 440 450
AESNRLVGEL KLDRLLLELK HSNIGPFPVE LLQDIMNYIV PILVLPRVNE
460 470 480
KLQKGFPLPT PARVQLYNVV LQPHQNFLLF GADVVYK
Length:487
Mass (Da):53,900
Last modified:November 25, 2008 - v4
Checksum:i30BC73B1B465B62D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5M → L in AAH40955 (PubMed:15489334).Curated1
Sequence conflicti53T → R AA sequence (PubMed:1937776).Curated1
Sequence conflicti355P → S in AAG42844 (Ref. 7) Curated1
Sequence conflicti375F → L (PubMed:7517398).Curated1
Sequence conflicti411K → R in AAG42844 (Ref. 7) Curated1
Sequence conflicti433Q → L in BAG37729 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04972812A → T.Corresponds to variant rs5743497dbSNPEnsembl.1
Natural variantiVAR_04972912A → V.Corresponds to variant rs5743498dbSNPEnsembl.1
Natural variantiVAR_01840116A → V.2 PublicationsCorresponds to variant rs1341023dbSNPEnsembl.1
Natural variantiVAR_04973090R → C.Corresponds to variant rs5743500dbSNPEnsembl.1
Natural variantiVAR_049732140E → Q.Corresponds to variant rs5743506dbSNPEnsembl.1
Natural variantiVAR_018402196A → V.Corresponds to variant rs5743509dbSNPEnsembl.1
Natural variantiVAR_018403216E → K.3 PublicationsCorresponds to variant rs4358188dbSNPEnsembl.1
Natural variantiVAR_049733280A → V.Corresponds to variant rs5741804dbSNPEnsembl.1
Natural variantiVAR_049734377V → I.Corresponds to variant rs5743524dbSNPEnsembl.1
Natural variantiVAR_049735404N → D.2 PublicationsCorresponds to variant rs5741809dbSNPEnsembl.1
Natural variantiVAR_049736451K → E.Corresponds to variant rs5743542dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04739 mRNA. Translation: AAA51841.1.
DQ414688 mRNA. Translation: ABD66755.1.
AK315328 mRNA. Translation: BAG37729.1.
AL359555 Genomic DNA. No translation available.
AL391095 Genomic DNA. No translation available.
AL499625 Genomic DNA. No translation available.
AL583962 Genomic DNA. No translation available.
BC040955 mRNA. Translation: AAH40955.1.
AF322588 mRNA. Translation: AAG42844.1.
CCDSiCCDS13303.1.
PIRiA33850. A30909.
RefSeqiNP_001716.2. NM_001725.2.
UniGeneiHs.529019.

Genome annotation databases

EnsembliENST00000262865; ENSP00000262865; ENSG00000101425.
GeneIDi671.
KEGGihsa:671.
UCSCiuc002xib.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04739 mRNA. Translation: AAA51841.1.
DQ414688 mRNA. Translation: ABD66755.1.
AK315328 mRNA. Translation: BAG37729.1.
AL359555 Genomic DNA. No translation available.
AL391095 Genomic DNA. No translation available.
AL499625 Genomic DNA. No translation available.
AL583962 Genomic DNA. No translation available.
BC040955 mRNA. Translation: AAH40955.1.
AF322588 mRNA. Translation: AAG42844.1.
CCDSiCCDS13303.1.
PIRiA33850. A30909.
RefSeqiNP_001716.2. NM_001725.2.
UniGeneiHs.529019.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BP1X-ray2.40A32-487[»]
1EWFX-ray1.70A32-487[»]
ProteinModelPortaliP17213.
SMRiP17213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000262865.

Protein family/group databases

TCDBi1.C.40.1.1. the bactericidal permeability increasing protein (bpip) family.

PTM databases

iPTMnetiP17213.
PhosphoSitePlusiP17213.

Polymorphism and mutation databases

BioMutaiBPI.
DMDMi215274242.

Proteomic databases

EPDiP17213.
MaxQBiP17213.
PaxDbiP17213.
PeptideAtlasiP17213.
PRIDEiP17213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262865; ENSP00000262865; ENSG00000101425.
GeneIDi671.
KEGGihsa:671.
UCSCiuc002xib.3. human.

Organism-specific databases

CTDi671.
DisGeNETi671.
GeneCardsiBPI.
H-InvDBHIX0027669.
HGNCiHGNC:1095. BPI.
HPAiHPA061284.
MIMi109195. gene.
neXtProtiNX_P17213.
OpenTargetsiENSG00000101425.
PharmGKBiPA25403.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4160. Eukaryota.
ENOG410Z88E. LUCA.
GeneTreeiENSGT00730000110583.
HOVERGENiHBG002797.
InParanoidiP17213.
OMAiELKHSDV.
OrthoDBiEOG091G08NV.
PhylomeDBiP17213.
TreeFamiTF315617.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101425-MONOMER.
ReactomeiR-HSA-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6803157. Antimicrobial peptides.

Miscellaneous databases

ChiTaRSiBPI. human.
EvolutionaryTraceiP17213.
GenomeRNAii671.
PROiP17213.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101425.
ExpressionAtlasiP17213. baseline and differential.
GenevisibleiP17213. HS.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR030181. BPI.
IPR030675. BPI/LBP.
IPR032942. BPI/LBP/Plunc.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504. PTHR10504. 1 hit.
PTHR10504:SF84. PTHR10504:SF84. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002417. Lipid_binding_protein. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBPI_HUMAN
AccessioniPrimary (citable) accession number: P17213
Secondary accession number(s): B2RCY2
, Q1ZZU8, Q5JRW0, Q8IW58, Q9BYZ9, Q9H1L2, Q9H1M8, Q9H203, Q9UCT4, Q9UD65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 165 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.