BPI_MOUSE
ID BPI_MOUSE Reviewed; 483 AA.
AC Q67E05; A2AC63; Q5I5I4; Q8BSF3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Bactericidal permeability-increasing protein;
DE Short=BPI;
DE Flags: Precursor;
GN Name=Bpi;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=15590754; DOI=10.1189/jlb.0304159;
RA Lennartsson A., Pieters K., Vidovic K., Gullberg U.;
RT "A murine antibacterial ortholog to human bactericidal/permeability-
RT increasing protein (BPI) is expressed in testis, epididymis, and bone
RT marrow.";
RL J. Leukoc. Biol. 77:369-377(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=16365446; DOI=10.4049/jimmunol.176.1.522;
RA Eckert M., Wittmann I., Roellinghoff M., Gessner A., Schnare M.;
RT "Endotoxin-induced expression of murine bactericidal
RT permeability/increasing protein is mediated exclusively by toll/IL-1
RT receptor domain-containing adaptor inducing IFN-beta-dependent pathways.";
RL J. Immunol. 176:522-528(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Swiss Webster;
RA Bingle C.D., Craven J.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:15590754}.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P17213}.
CC Cytoplasmic granule membrane {ECO:0000269|PubMed:15590754}.
CC Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
CC granules. {ECO:0000269|PubMed:15590754}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q67E05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67E05-2; Sequence=VSP_036070;
CC Name=3;
CC IsoId=Q67E05-3; Sequence=VSP_036069;
CC -!- TISSUE SPECIFICITY: Expressed in testis, epididymis, and bone marrow,
CC as well as in Sertoli and promyelocytic cell lines. Upon stimulation
CC with different TLR ligands, it is strongly expressed in granulocytes
CC and in bone marrow-derived dendritic cells.
CC {ECO:0000269|PubMed:15590754, ECO:0000269|PubMed:16365446}.
CC -!- INDUCTION: By lipopolysaccharide (LPS) through TRL4-TRIF-dependent
CC pathway. Expression in Sertoli and promyelocytic cells is enhanced
CC several-fold by all-trans retinoic acid. {ECO:0000269|PubMed:15590754,
CC ECO:0000269|PubMed:16365446}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The N- and C-terminal barrels adopt an identical fold despite
CC having only 13% of conserved residues. {ECO:0000250|UniProtKB:P17213}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; AY853179; AAW50819.1; -; mRNA.
DR EMBL; AY648037; AAV65841.1; -; mRNA.
DR EMBL; AY363993; AAR13289.1; -; mRNA.
DR EMBL; AK033770; BAC28468.1; -; mRNA.
DR EMBL; AL663063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118049; AAI18050.1; -; mRNA.
DR EMBL; BC118504; AAI18505.1; -; mRNA.
DR CCDS; CCDS16987.1; -. [Q67E05-3]
DR CCDS; CCDS89574.1; -. [Q67E05-1]
DR RefSeq; NP_808518.1; NM_177850.3. [Q67E05-3]
DR AlphaFoldDB; Q67E05; -.
DR SMR; Q67E05; -.
DR STRING; 10090.ENSMUSP00000067837; -.
DR GlyGen; Q67E05; 2 sites.
DR iPTMnet; Q67E05; -.
DR PhosphoSitePlus; Q67E05; -.
DR PaxDb; Q67E05; -.
DR PRIDE; Q67E05; -.
DR ProteomicsDB; 281704; -. [Q67E05-1]
DR ProteomicsDB; 281705; -. [Q67E05-2]
DR ProteomicsDB; 281706; -. [Q67E05-3]
DR Antibodypedia; 26835; 355 antibodies from 31 providers.
DR DNASU; 329547; -.
DR Ensembl; ENSMUST00000065039; ENSMUSP00000067837; ENSMUSG00000052922. [Q67E05-3]
DR Ensembl; ENSMUST00000109499; ENSMUSP00000105125; ENSMUSG00000052922. [Q67E05-1]
DR Ensembl; ENSMUST00000109500; ENSMUSP00000105126; ENSMUSG00000052922. [Q67E05-2]
DR GeneID; 329547; -.
DR KEGG; mmu:329547; -.
DR UCSC; uc008npw.1; mouse. [Q67E05-3]
DR UCSC; uc008npx.1; mouse. [Q67E05-1]
DR CTD; 671; -.
DR MGI; MGI:3045315; Bpi.
DR VEuPathDB; HostDB:ENSMUSG00000052922; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230353; -.
DR HOGENOM; CLU_028970_3_2_1; -.
DR InParanoid; Q67E05; -.
DR OMA; VGWLIRL; -.
DR OrthoDB; 1242894at2759; -.
DR TreeFam; TF315617; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 329547; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q67E05; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q67E05; protein.
DR Bgee; ENSMUSG00000052922; Expressed in spermatocyte and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0006955; P:immune response; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0043031; P:negative regulation of macrophage activation; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR030181; BPI.
DR InterPro; IPR030675; BPI/LBP.
DR InterPro; IPR032942; BPI/LBP/Plunc.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR10504; PTHR10504; 1.
DR PANTHER; PTHR10504:SF84; PTHR10504:SF84; 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; SSF55394; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Antibiotic; Antimicrobial; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..483
FT /note="Bactericidal permeability-increasing protein"
FT /id="PRO_0000358332"
FT REGION 28..38
FT /note="Central sheet, part 1"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 37..219
FT /note="N-terminal barrel"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 221..285
FT /note="Central sheet, part 2"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 235..240
FT /note="Cleavage sites for elastase"
FT /evidence="ECO:0000250"
FT REGION 286..457
FT /note="C-terminal barrel"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT REGION 464..483
FT /note="Central sheet, part 3"
FT /evidence="ECO:0000250|UniProtKB:P17213"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..201
FT /evidence="ECO:0000250"
FT VAR_SEQ 386
FT /note="M -> MVRR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036069"
FT VAR_SEQ 409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036070"
SQ 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
