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Protein

Bactericidal permeability-increasing protein

Gene

BPI

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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-negative 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

Keywordsi

Molecular functionAntibiotic, Antimicrobial

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000101425.12
HGNCiHGNC:1095 BPI
MIMi109195 gene
neXtProtiNX_P17213

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Chemistry databases

DrugBankiDB04178 Di-Stearoyl-3-Sn-Phosphatidylcholine

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...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP17213
MaxQBiP17213
PaxDbiP17213
PeptideAtlasiP17213
PRIDEiP17213
ProteomicsDBi53463

PTM databases

iPTMnetiP17213
PhosphoSitePlusiP17213

Expressioni

Tissue specificityi

Restricted to cells of the myeloid series.

Gene expression databases

BgeeiENSG00000101425 Expressed in 126 organ(s), highest expression level in bone marrow
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

3D structure databases

ProteinModelPortaliP17213
SMRiP17213
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17213

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 42Central sheet, part 11 PublicationAdd BLAST11
Regioni41 – 224N-terminal barrel1 PublicationAdd BLAST184
Regioni226 – 290Central sheet, part 21 PublicationAdd BLAST65
Regioni240 – 245Cleavage sites for elastaseSequence analysis6
Regioni291 – 461C-terminal barrel1 PublicationAdd BLAST171
Regioni468 – 487Central sheet, part 31 PublicationAdd BLAST20

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
OMAiDHDRMVY
OrthoDBiEOG091G08NV
PhylomeDBiP17213
TreeFamiTF315617

Family and domain databases

InterProiView protein in InterPro
IPR017943 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
PANTHERiPTHR10504 PTHR10504, 1 hit
PTHR10504:SF84 PTHR10504:SF84, 1 hit
PfamiView protein in Pfam
PF01273 LBP_BPI_CETP, 1 hit
PF02886 LBP_BPI_CETP_C, 1 hit
PIRSFiPIRSF002417 Lipid_binding_protein, 1 hit
SMARTiView protein in SMART
SM00328 BPI1, 1 hit
SM00329 BPI2, 1 hit
SUPFAMiSSF55394 SSF55394, 2 hits
PROSITEiView protein in PROSITE
PS00400 LBP_BPI_CETP, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y738H0Y738_HUMAN
Bactericidal permeability-increasin...
BPI
286Annotation score:
A0A0D9SFX6A0A0D9SFX6_HUMAN
Bactericidal permeability-increasin...
BPI
55Annotation score:
A0A2R8YDF1A0A2R8YDF1_HUMAN
Bactericidal permeability-increasin...
BPI
261Annotation score:

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 dbSNP:rs5743497Ensembl.1
Natural variantiVAR_04972912A → V. Corresponds to variant dbSNP:rs5743498Ensembl.1
Natural variantiVAR_01840116A → V2 PublicationsCorresponds to variant dbSNP:rs1341023EnsemblClinVar.1
Natural variantiVAR_04973090R → C. Corresponds to variant dbSNP:rs5743500Ensembl.1
Natural variantiVAR_049732140E → Q. Corresponds to variant dbSNP:rs5743506Ensembl.1
Natural variantiVAR_018402196A → V. Corresponds to variant dbSNP:rs5743509EnsemblClinVar.1
Natural variantiVAR_018403216E → K3 PublicationsCorresponds to variant dbSNP:rs4358188EnsemblClinVar.1
Natural variantiVAR_049733280A → V. Corresponds to variant dbSNP:rs5741804Ensembl.1
Natural variantiVAR_049734377V → I. Corresponds to variant dbSNP:rs5743524Ensembl.1
Natural variantiVAR_049735404N → D2 PublicationsCorresponds to variant dbSNP:rs5741809Ensembl.1
Natural variantiVAR_049736451K → E. Corresponds to variant dbSNP:rs5743542Ensembl.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

Similar proteinsi

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

Chemistry databases

DrugBankiDB04178 Di-Stearoyl-3-Sn-Phosphatidylcholine

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
ProteomicsDBi53463

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi671
DisGeNETi671
EuPathDBiHostDB:ENSG00000101425.12
GeneCardsiBPI
H-InvDBiHIX0027669
HGNCiHGNC:1095 BPI
HPAiHPA061284
MIMi109195 gene
neXtProtiNX_P17213
OpenTargetsiENSG00000101425
PharmGKBiPA25403
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4160 Eukaryota
ENOG410Z88E LUCA
GeneTreeiENSGT00730000110583
HOVERGENiHBG002797
InParanoidiP17213
OMAiDHDRMVY
OrthoDBiEOG091G08NV
PhylomeDBiP17213
TreeFamiTF315617

Enzyme and pathway databases

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
PROiPR:P17213
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101425 Expressed in 126 organ(s), highest expression level in bone marrow
ExpressionAtlasiP17213 baseline and differential
GenevisibleiP17213 HS

Family and domain databases

InterProiView protein in InterPro
IPR017943 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
PANTHERiPTHR10504 PTHR10504, 1 hit
PTHR10504:SF84 PTHR10504:SF84, 1 hit
PfamiView protein in Pfam
PF01273 LBP_BPI_CETP, 1 hit
PF02886 LBP_BPI_CETP_C, 1 hit
PIRSFiPIRSF002417 Lipid_binding_protein, 1 hit
SMARTiView protein in SMART
SM00328 BPI1, 1 hit
SM00329 BPI2, 1 hit
SUPFAMiSSF55394 SSF55394, 2 hits
PROSITEiView protein in PROSITE
PS00400 LBP_BPI_CETP, 1 hit
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 historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: November 7, 2018
This is version 179 of the entry and version 4 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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