BPIB4_MOUSE
ID BPIB4_MOUSE Reviewed; 617 AA.
AC A2BGH0; Q3UPM5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=BPI fold-containing family B member 4;
DE AltName: Full=Long palate, lung and nasal epithelium carcinoma-associated protein 4 {ECO:0000303|PubMed:14739326};
DE Flags: Precursor;
GN Name=Bpifb4; Synonyms=Gm1006 {ECO:0000312|MGI:MGI:2685852}, Lplunc4;
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] {ECO:0000305, ECO:0000312|EMBL:BAE25370.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25370.1};
RC TISSUE=Ovary {ECO:0000312|EMBL:BAE25370.1};
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 [2]
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAI47611.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis {ECO:0000312|EMBL:AAI47611.1};
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 [4] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=14739326; DOI=10.1110/ps.03332704;
RA Bingle C.D., LeClair E.E., Havard S., Bingle L., Gillingham P.,
RA Craven C.J.;
RT "Phylogenetic and evolutionary analysis of the PLUNC gene family.";
RL Protein Sci. 13:422-430(2004).
CC -!- FUNCTION: May have the capacity to recognize and bind specific classes
CC of odorants. May act as a carrier molecule, transporting odorants
CC across the mucus layer to access receptor sites. May serve as a primary
CC defense mechanism by recognizing and removing potentially harmful
CC odorants or pathogenic microorganisms from the mucosa or clearing
CC excess odorant from mucus to enable new odorant stimuli to be received
CC (By similarity). {ECO:0000250|UniProtKB:Q05701}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P59827}.
CC Cytoplasm {ECO:0000250|UniProtKB:P59827}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2BGH0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=A2BGH0-2; Sequence=VSP_052985, VSP_052986;
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000255}.
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DR EMBL; AK143420; BAE25370.1; -; mRNA.
DR EMBL; BX470156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147610; AAI47611.1; -; mRNA.
DR EMBL; BC147625; AAI47626.1; -; mRNA.
DR CCDS; CCDS16922.2; -. [A2BGH0-1]
DR RefSeq; NP_001030047.2; NM_001034875.3. [A2BGH0-1]
DR RefSeq; XP_006499887.1; XM_006499824.1. [A2BGH0-1]
DR AlphaFoldDB; A2BGH0; -.
DR SMR; A2BGH0; -.
DR STRING; 10090.ENSMUSP00000105379; -.
DR GlyGen; A2BGH0; 1 site.
DR PhosphoSitePlus; A2BGH0; -.
DR PaxDb; A2BGH0; -.
DR PRIDE; A2BGH0; -.
DR ProteomicsDB; 265454; -. [A2BGH0-1]
DR ProteomicsDB; 265455; -. [A2BGH0-2]
DR Antibodypedia; 25501; 12 antibodies from 8 providers.
DR Ensembl; ENSMUST00000099181; ENSMUSP00000096786; ENSMUSG00000074665. [A2BGH0-2]
DR Ensembl; ENSMUST00000109757; ENSMUSP00000105379; ENSMUSG00000074665. [A2BGH0-1]
DR Ensembl; ENSMUST00000109759; ENSMUSP00000105381; ENSMUSG00000074665. [A2BGH0-1]
DR GeneID; 381399; -.
DR KEGG; mmu:381399; -.
DR UCSC; uc008niq.1; mouse. [A2BGH0-2]
DR UCSC; uc012cgs.1; mouse. [A2BGH0-1]
DR CTD; 149954; -.
DR MGI; MGI:2685852; Bpifb4.
DR VEuPathDB; HostDB:ENSMUSG00000074665; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230460; -.
DR HOGENOM; CLU_031635_0_0_1; -.
DR InParanoid; A2BGH0; -.
DR OMA; DLAFMPT; -.
DR OrthoDB; 1099604at2759; -.
DR PhylomeDB; A2BGH0; -.
DR TreeFam; TF315617; -.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 381399; 3 hits in 73 CRISPR screens.
DR PRO; PR:A2BGH0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2BGH0; protein.
DR Bgee; ENSMUSG00000074665; Expressed in ovary and 6 other tissues.
DR ExpressionAtlas; A2BGH0; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..617
FT /note="BPI fold-containing family B member 4"
FT /id="PRO_0000355589"
FT REGION 117..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 297..334
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052985"
FT VAR_SEQ 215..228
FT /note="GEGGILSTVQGITG -> MAAVASSSLLTACR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052986"
SQ SEQUENCE 617 AA; 65723 MW; 7601EB15E01F73C1 CRC64;
MWTAWCVAAL SVAAVCGIRQ DTTTVLRVTK DVLGNAISGT IQKSDAFRSA LREVPVGVGG
VPYNDFHVRE PPPKYTNGRQ LGGNYKYGHI KANDNRAQLG GKYRYGEILD SDGSLRDLRH
EDYRPPDSAY HRGSGRYRSA ADSSSVGRLY RRELRPGEIP AGVATGALGP GGLLGTGGML
ANEGILAGQG GLLGGGGLLG DGGLLGGGGV LGVLGEGGIL STVQGITGLR IVELTLPRVS
VRLLPGVGVY LSLYTRVAIN GRSLIGFLDI AVEVNITAKV RLTMDRTGYP RLVIERCDTL
LGGIKVKLLR GLLPNLVDNL VNRVLANVLP DLLCPIVDVV LGLVNDQLGL VDSLVPLGIL
GSVQYTFSSL PLVTGEFLEL DLNTLVGEAG GDLIDYPLGR PAILPRPQMP ELPPMGDNTN
SQLAISANFL SSVLTMLQKQ GAMDIDITDG MFEDLPPLTT STLGALIPKV FQQYPESRPL
TIRIQVPNPP TVTLQKDKAL VKVFATSEVV VSQPNDVETT ICLIDVDTDL LASFSVEGDK
LMIDAKLDKT SLNLRTSNVG NFDVFILEML VEKIFDLAFM PAMNAILGSG VPLPKILNID
FSNADIDVLE DLLVLST
