BPIB3_RAT
ID BPIB3_RAT Reviewed; 473 AA.
AC Q05701;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=BPI fold-containing family B member 3 {ECO:0000305};
DE AltName: Full=Ligand-binding protein RYA3;
DE AltName: Full=Long palate, lung and nasal epithelium carcinoma-associated protein 3;
DE Flags: Precursor;
GN Name=Bpifb3 {ECO:0000312|RGD:1565613}; Synonyms=Lplunc3, Rya3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer; TISSUE=Olfactory epithelium;
RX PubMed=1915264; DOI=10.1002/j.1460-2075.1991.tb07830.x;
RA Dear T.N., Boehm T., Keverne E.B., Rabbitts T.H.;
RT "Novel genes for potential ligand-binding proteins in subregions of the
RT olfactory mucosa.";
RL EMBO J. 10:2813-2819(1991).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in olfactory mucosa but
CC undetectable in thymus, kidney, lung, brain, spleen and liver.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; X60658; CAA43065.1; -; mRNA.
DR RefSeq; XP_006235414.1; XM_006235352.3.
DR AlphaFoldDB; Q05701; -.
DR SMR; Q05701; -.
DR STRING; 10116.ENSRNOP00000052216; -.
DR GlyGen; Q05701; 1 site.
DR PaxDb; Q05701; -.
DR PRIDE; Q05701; -.
DR GeneID; 499924; -.
DR UCSC; RGD:1565613; rat.
DR CTD; 359710; -.
DR RGD; 1565613; Bpifb3.
DR eggNOG; KOG4160; Eukaryota.
DR HOGENOM; CLU_031635_1_0_1; -.
DR InParanoid; Q05701; -.
DR OrthoDB; 1099604at2759; -.
DR PhylomeDB; Q05701; -.
DR TreeFam; TF315617; -.
DR PRO; PR:Q05701; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0005549; F:odorant binding; NAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR032951; BPIFB3.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR46019:SF5; PTHR46019:SF5; 1.
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 Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..473
FT /note="BPI fold-containing family B member 3"
FT /id="PRO_0000017172"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..196
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 49949 MW; BB6957AFD62A26B9 CRC64;
MMPGVYALLL LWGLATPCLG LLETVGTLAR IDKDELGKAI QNSLVGGPIL QNVLGTVTSV
NQGLLGAGGL LGGGGLLSYG GLFSLVEELS GLKIEELTLP TVSIKLLPGV GVQLSLHTKV
SLHGSGPLVG LLQLAAEVNV SSKVALGMSP RGTPILILKR CNTLLGHISL TSGLLPTPIF
GLVEQTLCKV LPGLLCPVVD SVLSVVNELL GATLSLVPLG PLGSVEFTLA TLPLISNQYI
ELDINPIVKS IAGDVIDFPK PRLPVKMPPK EDHTSQVTVP LYLFNTVFGL LQTNGALDLD
ITPEMVPRNI PLTTTDLAAL APEALGKLPP GQHLLLSLRV MKSPMILLQN KKVTVSIPVT
IHVLSSVPQG TPVALFQMNG VMTLNAHLVP STTKLHISLS LERLTVQLAS SFSQPFDASR
LEEWLSDVVR AAYMQKLNEH LEVGIPLPKI LNVNFANSVV DVIENAVVLT VAP