BPIA1_BOVIN
ID BPIA1_BOVIN Reviewed; 255 AA.
AC Q8SPU5; Q1RMN7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=BPI fold-containing family A member 1;
DE AltName: Full=Palate lung and nasal epithelium clone protein;
DE Flags: Precursor;
GN Name=BPIFA1; Synonyms=PLUNC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Tonsil;
RX PubMed=12427544; DOI=10.1016/s0167-4781(02)00508-0;
RA Wheeler T.T., Haigh B.J., McCracken J.Y., Wilkins R.J., Morris C.A.,
RA Grigor M.R.;
RT "The BSP30 salivary proteins from cattle, LUNX/PLUNC and von Ebner's minor
RT salivary gland protein are members of the PSP/LBP superfamily of
RT proteins.";
RL Biochim. Biophys. Acta 1579:92-100(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid-binding protein which shows high specificity for the
CC surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC). Plays a
CC role in the innate immune responses of the upper airways. Reduces the
CC surface tension in secretions from airway epithelia and inhibits the
CC formation of biofilm by pathogenic Gram-negative bacteria, such as
CC P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic
CC cleavage of SCNN1G, an event that is required for activation of the
CC epithelial sodium channel (ENaC), and thereby contributes to airway
CC surface liquid homeostasis and proper clearance of mucus. Plays a role
CC in the airway inflammatory response after exposure to irritants. May
CC attract macrophages and neutrophils. {ECO:0000250|UniProtKB:Q9NP55}.
CC -!- SUBUNIT: Monomer. Interacts (via N-terminus) with SCNN1B, a subunit of
CC the heterotrimeric epithelial sodium channel (ENaC); this inhibits
CC proteolytic activation of ENaC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Apical side of
CC airway epithelial cells. Detected in airway surface liquid, nasal mucus
CC and sputum (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in trachea, and at lower levels in nasal
CC epithelium. {ECO:0000269|PubMed:12427544}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. Plunc family.
CC {ECO:0000305}.
CC -!- CAUTION: Reported to bind to bacterial lipopolysaccharide (LPS) in
CC vitro. However, the in vivo significance of this is uncertain since
CC other studies indicate little or no specificity for LPS.
CC {ECO:0000250|UniProtKB:Q9NP55}.
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DR EMBL; AF488706; AAM00907.1; -; mRNA.
DR EMBL; BC114803; AAI14804.1; -; mRNA.
DR RefSeq; NP_776851.1; NM_174426.3.
DR AlphaFoldDB; Q8SPU5; -.
DR SMR; Q8SPU5; -.
DR STRING; 9913.ENSBTAP00000022728; -.
DR PaxDb; Q8SPU5; -.
DR Ensembl; ENSBTAT00000022728; ENSBTAP00000022728; ENSBTAG00000017098.
DR GeneID; 281989; -.
DR KEGG; bta:281989; -.
DR CTD; 51297; -.
DR VEuPathDB; HostDB:ENSBTAG00000017098; -.
DR VGNC; VGNC:26543; BPIFA1.
DR eggNOG; ENOG502SR58; Eukaryota.
DR GeneTree; ENSGT01020000230460; -.
DR HOGENOM; CLU_095915_0_0_1; -.
DR InParanoid; Q8SPU5; -.
DR OMA; ANMLIHG; -.
DR OrthoDB; 1275829at2759; -.
DR TreeFam; TF337052; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000017098; Expressed in olfactory segment of nasal mucosa and 35 other tissues.
DR ExpressionAtlas; Q8SPU5; baseline.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019731; P:antibacterial humoral response; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0002395; P:immune response in nasopharyngeal-associated lymphoid tissue; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
DR GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; ISS:UniProtKB.
DR GO; GO:0050828; P:regulation of liquid surface tension; ISS:UniProtKB.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISS:UniProtKB.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR034307; BPIFA1.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR47015:SF1; PTHR47015:SF1; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR SUPFAM; SSF55394; SSF55394; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Lipid-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..255
FT /note="BPI fold-containing family A member 1"
FT /id="PRO_0000017174"
FT REGION 87..92
FT /note="Important for surfactant activity and antibacterial
FT properties"
FT /evidence="ECO:0000250|UniProtKB:Q9NP55"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 179..223
FT /evidence="ECO:0000250|UniProtKB:Q9NP55"
SQ SEQUENCE 255 AA; 26576 MW; 02C02D565406F787 CRC64;
MFHIGSLVVL CGLLAPTTAL LEALPTPLGQ TLPLAVTPAL APSPPDLAGS LTGALSNGLL
SEGLLGILEN LPLLDILKTR GNAPSGLLGS LLGKVTSLTP LLNNIIELKI TNPQLLELGL
VQSPDGHRLY VTIPLGMILN VKTSLVGSLL KLAVKLNITV ELLAVTDEQK HVHLVVGNCT
HSPGSLQIFL LDGLGSLPIQ SFVDNLTGIL NDVLPGLVQG KVCPLVNAVL SRLDVTLVHS
IVNALIHGLQ FVIKV
