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P17213 (BPI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bactericidal permeability-increasing protein

Short name=BPI
Alternative name(s):
CAP 57
Gene names
Name:BPI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8

Subunit structure

Monomer. Homodimer; disulfide-linked. Ref.11

Subcellular location

Secreted. Cytoplasmic granule membrane. Note: Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. Ref.1 Ref.11

Tissue specificity

Restricted to cells of the myeloid series.

Domain

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. Ref.1

Sequence similarities

Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.1 Ref.8 Ref.9 Ref.10
Chain32 – 487456Bactericidal permeability-increasing protein
PRO_0000017154

Regions

Region240 – 2456Cleavage sites for elastase Potential

Amino acid modifications

Glycosylation3801N-linked (GlcNAc...) Potential
Disulfide bond166 ↔ 206

Natural variations

Natural variant121A → T.
Corresponds to variant rs5743497 [ dbSNP | Ensembl ].
VAR_049728
Natural variant121A → V.
Corresponds to variant rs5743498 [ dbSNP | Ensembl ].
VAR_049729
Natural variant161A → V. Ref.1 Ref.3
Corresponds to variant rs1341023 [ dbSNP | Ensembl ].
VAR_018401
Natural variant901R → C.
Corresponds to variant rs5743500 [ dbSNP | Ensembl ].
VAR_049730
Natural variant1401E → Q.
Corresponds to variant rs5743506 [ dbSNP | Ensembl ].
VAR_049732
Natural variant1961A → V.
Corresponds to variant rs5743509 [ dbSNP | Ensembl ].
VAR_018402
Natural variant2161E → K. Ref.1 Ref.6 Ref.7
Corresponds to variant rs4358188 [ dbSNP | Ensembl ].
VAR_018403
Natural variant2801A → V.
Corresponds to variant rs5741804 [ dbSNP | Ensembl ].
VAR_049733
Natural variant3771V → I.
Corresponds to variant rs5743524 [ dbSNP | Ensembl ].
VAR_049734
Natural variant4041N → D. Ref.4 Ref.7
Corresponds to variant rs5741809 [ dbSNP | Ensembl ].
VAR_049735
Natural variant4511K → E.
Corresponds to variant rs5743542 [ dbSNP | Ensembl ].
VAR_049736

Experimental info

Mutagenesis491S → C: No impairment of secretion and increased propensity for dimer formation. Ref.11
Mutagenesis1631C → A: No impairment of secretion and/or biological activity. Loss of dimer formation. Ref.11
Mutagenesis1661C → S: Poorly secreted. Loss of LPS-binding and biological activity. Ref.11
Mutagenesis2061C → A: Not secreted. Ref.11
Sequence conflict51M → L in AAH40955. Ref.6
Sequence conflict531T → R AA sequence Ref.8
Sequence conflict3551P → S in AAG42844. Ref.7
Sequence conflict3751F → L Ref.2
Sequence conflict4111K → R in AAG42844. Ref.7
Sequence conflict4331Q → L in BAG37729. Ref.4

Secondary structure

........................................................................... 487
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17213 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 30BC73B1B465B62D

FASTA48753,900
        10         20         30         40         50         60 
MRENMARGPC NAPRWASLMV LVAIGTAVTA AVNPGVVVRI SQKGLDYASQ QGTAALQKEL 

        70         80         90        100        110        120 
KRIKIPDYSD SFKIKHLGKG HYSFYSMDIR EFQLPSSQIS MVPNVGLKFS ISNANIKISG 

       130        140        150        160        170        180 
KWKAQKRFLK MSGNFDLSIE GMSISADLKL GSNPTSGKPT ITCSSCSSHI NSVHVHISKS 

       190        200        210        220        230        240 
KVGWLIQLFH KKIESALRNK MNSQVCEKVT NSVSSELQPY FQTLPVMTKI DSVAGINYGL 

       250        260        270        280        290        300 
VAPPATTAET LDVQMKGEFY SENHHNPPPF APPVMEFPAA HDRMVYLGLS DYFFNTAGLV 

       310        320        330        340        350        360 
YQEAGVLKMT LRDDMIPKES KFRLTTKFFG TFLPEVAKKF PNMKIQIHVS ASTPPHLSVQ 

       370        380        390        400        410        420 
PTGLTFYPAV DVQAFAVLPN SSLASLFLIG MHTTGSMEVS AESNRLVGEL KLDRLLLELK 

       430        440        450        460        470        480 
HSNIGPFPVE LLQDIMNYIV PILVLPRVNE KLQKGFPLPT PARVQLYNVV LQPHQNFLLF 


GADVVYK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations."
Gray P.W., Flaggs G., Leong S.R., Gumina R.J., Weiss J., Ooi C.E., Elsbach P.
J. Biol. Chem. 264:9505-9509(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-68, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, VARIANTS VAL-16 AND LYS-216.
[2]"Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-binding protein. LPS binding properties and effects on LPS-mediated cell activation."
Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L., Lane J.C., Leong S.R., Thornton M.B., Miller K.L., Scott R.W.
J. Biol. Chem. 269:17411-17416(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"cDNA cloning and sequence analysis of human bactericidal/permeability protein."
Ma H., Cao X., Sun Y., Lei W.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-16.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-404.
Tissue: Fetal heart.
[5]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-216.
Tissue: Leukocyte.
[7]"Cloning of cDNA of human bactericidal/permeability-increasing protein."
Xu J., Wang H.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-487, VARIANTS LYS-216 AND ASP-404.
[8]"Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa."
Wasiluk K.R., Skubitz K.M., Gray B.H.
Infect. Immun. 59:4193-4200(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-53, FUNCTION.
Tissue: Leukocyte.
[9]"Antibiotic proteins of human polymorphonuclear leukocytes."
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F.
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-51.
[10]"A 25-kDa NH2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein."
Ooi C.E., Weiss J., Elsbach P., Frangione B., Mannion B.
J. Biol. Chem. 262:14891-14894(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-48.
[11]"Expression and characterization of cysteine-modified variants of an amino-terminal fragment of bactericidal/permeability-increasing protein."
Horwitz A.H., Leigh S.D., Abrahamson S., Gazzano-Santoro H., Liu P.-S., Williams R.E., Carroll S.F., Theofan G.
Protein Expr. Purif. 8:28-40(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-49; CYS-163; CYS-166 AND CYS-206.
[12]"Crystal structure of human BPI and two bound phospholipids at 2.4-A resolution."
Beamer L.J., Carroll S.F., Eisenberg D.
Science 276:1861-1864(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 32-487.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA30909. A33850.
RefSeqNP_001716.2. NM_001725.2.
UniGeneHs.529019.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BP1X-ray2.40A32-487[»]
1EWFX-ray1.70A32-483[»]
ProteinModelPortalP17213.
SMRP17213. Positions 32-487.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB1.C.40.1.1. the bactericidal permeability increasing protein (bpip) family.

PTM databases

PhosphoSiteP17213.

Polymorphism databases

DMDM215274242.

Proteomic databases

PaxDbP17213.
PRIDEP17213.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262865; ENSP00000262865; ENSG00000101425.
GeneID671.
KEGGhsa:671.
UCSCuc002xib.2. human.

Organism-specific databases

CTD671.
GeneCardsGC20P036888.
H-InvDBHIX0027669.
HGNCHGNC:1095. BPI.
MIM109195. gene.
neXtProtNX_P17213.
PharmGKBPA25403.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262970.
HOVERGENHBG002797.
InParanoidP17213.
OMACSSHINS.
PhylomeDBP17213.
TreeFamTF315617.

Gene expression databases

ArrayExpressP17213.
BgeeP17213.
GenevestigatorP17213.

Family and domain databases

InterProIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PfamPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
SMARTSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMSSF55394. SSF55394. 2 hits.
PROSITEPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBPI. human.
EvolutionaryTraceP17213.
GenomeRNAi671.
NextBio2748.
PROP17213.
SOURCESearch...

Entry information

Entry nameBPI_HUMAN
AccessionPrimary (citable) accession number: P17213
Secondary accession number(s): B2RCY2 expand/collapse secondary AC list , Q1ZZU8, Q5JRW0, Q8IW58, Q9BYZ9, Q9H1L2, Q9H1M8, Q9H203, Q9UCT4, Q9UD65
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: March 19, 2014
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM