BPIB2_MOUSE
ID BPIB2_MOUSE Reviewed; 462 AA.
AC Q8C1E1; Q3TUY4; Q8BVZ0; Q8C1E2; Q9D713; Q9D744;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=BPI fold-containing family B member 2;
DE AltName: Full=Bactericidal/permeability-increasing protein-like 1;
DE Flags: Precursor;
GN Name=Bpifb2; Synonyms=Bpil1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; AK009619; BAB26395.1; -; mRNA.
DR EMBL; AK009754; BAB26479.1; -; mRNA.
DR EMBL; AK028156; BAC25783.1; -; mRNA.
DR EMBL; AK028158; BAC25784.1; -; mRNA.
DR EMBL; AK075874; BAC36021.1; -; mRNA.
DR EMBL; AK160516; BAE35837.1; -; mRNA.
DR CCDS; CCDS16919.1; -.
DR RefSeq; NP_079907.2; NM_025631.3.
DR RefSeq; XP_017174674.1; XM_017319185.1.
DR AlphaFoldDB; Q8C1E1; -.
DR SMR; Q8C1E1; -.
DR STRING; 10090.ENSMUSP00000028983; -.
DR GlyGen; Q8C1E1; 3 sites.
DR PhosphoSitePlus; Q8C1E1; -.
DR PaxDb; Q8C1E1; -.
DR PRIDE; Q8C1E1; -.
DR ProteomicsDB; 273795; -.
DR Antibodypedia; 25479; 120 antibodies from 25 providers.
DR DNASU; 66557; -.
DR Ensembl; ENSMUST00000028983; ENSMUSP00000028983; ENSMUSG00000027481.
DR GeneID; 66557; -.
DR KEGG; mmu:66557; -.
DR UCSC; uc008nin.2; mouse.
DR CTD; 80341; -.
DR MGI; MGI:1913807; Bpifb2.
DR VEuPathDB; HostDB:ENSMUSG00000027481; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230460; -.
DR HOGENOM; CLU_597102_0_0_1; -.
DR InParanoid; Q8C1E1; -.
DR OMA; VVNLHYV; -.
DR OrthoDB; 931398at2759; -.
DR PhylomeDB; Q8C1E1; -.
DR TreeFam; TF315617; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 66557; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8C1E1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C1E1; protein.
DR Bgee; ENSMUSG00000027481; Expressed in peripheral lymph node and 9 other tissues.
DR ExpressionAtlas; Q8C1E1; baseline and differential.
DR Genevisible; Q8C1E1; MM.
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; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..462
FT /note="BPI fold-containing family B member 2"
FT /id="PRO_0000017165"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4F0"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4F0"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..177
FT /evidence="ECO:0000250"
FT CONFLICT 73
FT /note="Q -> H (in Ref. 1; BAC25783)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="P -> T (in Ref. 1; BAC25783)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> A (in Ref. 1; BAC25783)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="I -> L (in Ref. 1; BAB26479)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="P -> L (in Ref. 1; BAB26395)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="T -> P (in Ref. 1; BAC36021)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="L -> V (in Ref. 1; BAC36021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 49521 MW; 5D4F6D1F2AD57F45 CRC64;
MARACSLGLL LLLLLLLRTV VTVSLPVIVV RLNKAALDYV SDIGKAPLQR ALQVTISDFM
DPSGEVLQST RVQILDAHVP FFYLKFIAGF GVHLSAAANF TIKVFSVPEP MELVLPVDLL
ADVHVARDSI GTLVLSVPAC SSIFSPAGML DGSISTSQEL LDRVQEHIKA DLNNKLCLHV
YGLVQDLNVH LGTLIGLSPV GPESQIRYSI TSMPTITSNY ISLDIGAILS LLGKPILLPM
HGAHPFVLPW PLGDAGAMAT VGLSQHLFDC ALLMLQKAGS LNLEITGQLN SKNNPLNTSV
LGQLIPEVAH LFPEPTPLVL KVQLGATPVV TLHTSNSTLQ LQPLVEVFAA PSNLALQFLF
SLDVMVNLDL QLSVSKAKLR GSTSLLGGFQ LSVATSNVGS VDMDQVLTLI STVFQKPLLD
HLNALLGMGV VLPRVHNLHY VHSEVLVREG YVVVSSGLAY QH
