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Bactericidal permeability-increasing protein (BPI)

 BPI_MOUSE               Reviewed;         483 AA.
Q67E05; A2AC63; Q5I5I4; Q8BSF3;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
07-NOV-2018, entry version 109.
RecName: Full=Bactericidal permeability-increasing protein;
Short=BPI;
Flags: Precursor;
Name=Bpi;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=15590754; DOI=10.1189/jlb.0304159;
Lennartsson A., Pieters K., Vidovic K., Gullberg U.;
"A murine antibacterial ortholog to human bactericidal/permeability-
increasing protein (BPI) is expressed in testis, epididymis, and bone
marrow.";
J. Leukoc. Biol. 77:369-377(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=16365446; DOI=10.4049/jimmunol.176.1.522;
Eckert M., Wittmann I., Roellinghoff M., Gessner A., Schnare M.;
"Endotoxin-induced expression of murine bactericidal
permeability/increasing protein is mediated exclusively by toll/IL-1
receptor domain-containing adaptor inducing IFN-beta-dependent
pathways.";
J. Immunol. 176:522-528(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Swiss Webster;
Bingle C.D., Craven J.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Epididymis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
{ECO:0000269|PubMed:15590754}.
-!- SUBUNIT: Monomer. Homodimer; disulfide-linked (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P17213}.
Cytoplasmic granule membrane {ECO:0000269|PubMed:15590754}.
Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
granules. {ECO:0000269|PubMed:15590754}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q67E05-1; Sequence=Displayed;
Name=2;
IsoId=Q67E05-2; Sequence=VSP_036070;
Name=3;
IsoId=Q67E05-3; Sequence=VSP_036069;
-!- TISSUE SPECIFICITY: Expressed in testis, epididymis, and bone
marrow, as well as in Sertoli and promyelocytic cell lines. Upon
stimulation with different TLR ligands, it is strongly expressed
in granulocytes and in bone marrow-derived dendritic cells.
{ECO:0000269|PubMed:15590754, ECO:0000269|PubMed:16365446}.
-!- INDUCTION: By lipopolysaccharide (LPS) through TRL4-TRIF-dependent
pathway. Expression in Sertoli and promyelocytic cells is enhanced
several-fold by all-trans retinoic acid.
{ECO:0000269|PubMed:15590754, ECO:0000269|PubMed:16365446}.
-!- 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 (By similarity). {ECO:0000250}.
-!- DOMAIN: The N- and C-terminal barrels adopt an identical fold
despite having only 13% of conserved residues.
{ECO:0000250|UniProtKB:P17213}.
-!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY853179; AAW50819.1; -; mRNA.
EMBL; AY648037; AAV65841.1; -; mRNA.
EMBL; AY363993; AAR13289.1; -; mRNA.
EMBL; AK033770; BAC28468.1; -; mRNA.
EMBL; AL663063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC118049; AAI18050.1; -; mRNA.
EMBL; BC118504; AAI18505.1; -; mRNA.
CCDS; CCDS16987.1; -. [Q67E05-3]
RefSeq; NP_808518.1; NM_177850.3. [Q67E05-3]
UniGene; Mm.260883; -.
ProteinModelPortal; Q67E05; -.
SMR; Q67E05; -.
STRING; 10090.ENSMUSP00000067837; -.
iPTMnet; Q67E05; -.
PhosphoSitePlus; Q67E05; -.
PaxDb; Q67E05; -.
PRIDE; Q67E05; -.
Ensembl; ENSMUST00000065039; ENSMUSP00000067837; ENSMUSG00000052922. [Q67E05-3]
Ensembl; ENSMUST00000109499; ENSMUSP00000105125; ENSMUSG00000052922. [Q67E05-1]
Ensembl; ENSMUST00000109500; ENSMUSP00000105126; ENSMUSG00000052922. [Q67E05-2]
GeneID; 329547; -.
KEGG; mmu:329547; -.
UCSC; uc008npw.1; mouse. [Q67E05-3]
UCSC; uc008npx.1; mouse. [Q67E05-1]
CTD; 671; -.
MGI; MGI:3045315; Bpi.
eggNOG; KOG4160; Eukaryota.
eggNOG; ENOG410Z88E; LUCA.
GeneTree; ENSGT00730000110583; -.
HOGENOM; HOG000231250; -.
HOVERGEN; HBG002797; -.
InParanoid; Q67E05; -.
OMA; DHDRMVY; -.
OrthoDB; EOG091G08NV; -.
TreeFam; TF315617; -.
Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6803157; Antimicrobial peptides.
PRO; PR:Q67E05; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000052922; Expressed in 5 organ(s), highest expression level in testis.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
GO; GO:0006955; P:immune response; ISO:MGI.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
GO; GO:0043031; P:negative regulation of macrophage activation; ISO:MGI.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
InterPro; IPR030181; BPI.
InterPro; IPR030675; BPI/LBP.
InterPro; IPR032942; BPI/LBP/Plunc.
InterPro; IPR001124; Lipid-bd_serum_glycop_C.
InterPro; IPR017942; Lipid-bd_serum_glycop_N.
PANTHER; PTHR10504; PTHR10504; 1.
PANTHER; PTHR10504:SF84; PTHR10504:SF84; 1.
Pfam; PF01273; LBP_BPI_CETP; 1.
Pfam; PF02886; LBP_BPI_CETP_C; 1.
PIRSF; PIRSF002417; Lipid_binding_protein; 1.
SMART; SM00328; BPI1; 1.
SMART; SM00329; BPI2; 1.
SUPFAM; SSF55394; SSF55394; 2.
1: Evidence at protein level;
Alternative splicing; Antibiotic; Antimicrobial; Complete proteome;
Disulfide bond; Glycoprotein; Membrane; Reference proteome; Secreted;
Signal.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 483 Bactericidal permeability-increasing
protein.
/FTId=PRO_0000358332.
REGION 28 38 Central sheet, part 1.
{ECO:0000250|UniProtKB:P17213}.
REGION 37 219 N-terminal barrel.
{ECO:0000250|UniProtKB:P17213}.
REGION 221 285 Central sheet, part 2.
{ECO:0000250|UniProtKB:P17213}.
REGION 235 240 Cleavage sites for elastase.
{ECO:0000250}.
REGION 286 457 C-terminal barrel.
{ECO:0000250|UniProtKB:P17213}.
REGION 464 483 Central sheet, part 3.
{ECO:0000250|UniProtKB:P17213}.
CARBOHYD 375 375 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 161 201 {ECO:0000250}.
VAR_SEQ 386 386 M -> MVRR (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_036069.
VAR_SEQ 409 409 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_036070.
SEQUENCE 483 AA; 53940 MW; 4AA2D48095C52B74 CRC64;
MTWAPDNVRK WSALLLLAII GTALTAATDP GFVAMISQKG LDFACQQGVV ELQKELQAIS
VPDFSGVFKI KHLGKGSYEF YSMAVDGFHI PNPKIEMLPS DGLRVFIKDA SIKINGKWMS
RKNFLKAGGN FELSIQGVSI STDLILGSDS SGHITTICSN CDSHIDSVHI KISGSMLGWL
IRLFHRKIET SLKNIIYKKI CKIVRDSVSS KLQPYLKTLS VITRVDDVTS VDYSLLAPLT
TTNQFLEGQL KGEFFWRGHR DPLPIHPPVM RFVPNGAYMV CMGISDYFFN TEVLAYQQSG
TLKMTLGGQL LSNNGRFQLN TDFLRTFLPK VAKMFPSMGV QLLISAPVPV HLSIQPSGLS
FNPKLETQAF VVLPNASLVP LFVLGMKTNA SLEVDAEENR LVGEMKLGSR WLLELKESKF
GPFKVEYLED VINYLVSTLV LPKINERLRR GFPLPLPAGI RFSHFTFYPY QNFLLLEADL
HLI


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