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BPIA1_RAT
ID   BPIA1_RAT               Reviewed;         270 AA.
AC   Q8K4I4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-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   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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Nasal epithelium;
RX   PubMed=11821380; DOI=10.1074/jbc.m106208200;
RA   Sung Y.K., Moon C., Yoo J.-Y., Moon C., Pearse D., Pevsner J.,
RA   Ronnett G.V.;
RT   "Plunc, a member of the secretory gland protein family, is up-regulated in
RT   nasal respiratory epithelium after olfactory bulbectomy.";
RL   J. Biol. Chem. 277:12762-12769(2002).
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:0000269|PubMed:11821380}.
CC       Note=Apical side of airway epithelial cells. Detected in airway surface
CC       liquid, nasal mucus and sputum.
CC   -!- TISSUE SPECIFICITY: Detected in adult nasal epithelium, heart, lung,
CC       spleen, testis and salivary gland, and in embryonic nasal epithelium,
CC       lung, salivary gland and thymus. {ECO:0000269|PubMed:11821380}.
CC   -!- INDUCTION: After bulbectomy or lesion of the olfactory bulb.
CC       {ECO:0000269|PubMed:11821380}.
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; AF393750; AAM73687.1; -; mRNA.
DR   RefSeq; NP_742028.1; NM_172031.1.
DR   AlphaFoldDB; Q8K4I4; -.
DR   SMR; Q8K4I4; -.
DR   STRING; 10116.ENSRNOP00000018581; -.
DR   GlyGen; Q8K4I4; 1 site.
DR   PaxDb; Q8K4I4; -.
DR   Ensembl; ENSRNOT00000018581; ENSRNOP00000018581; ENSRNOG00000013859.
DR   GeneID; 246238; -.
DR   KEGG; rno:246238; -.
DR   UCSC; RGD:619818; rat.
DR   CTD; 51297; -.
DR   RGD; 619818; Bpifa1.
DR   eggNOG; ENOG502SR58; Eukaryota.
DR   GeneTree; ENSGT01020000230460; -.
DR   HOGENOM; CLU_095915_0_0_1; -.
DR   InParanoid; Q8K4I4; -.
DR   OMA; ANMLIHG; -.
DR   OrthoDB; 1275829at2759; -.
DR   PhylomeDB; Q8K4I4; -.
DR   TreeFam; TF337052; -.
DR   Reactome; R-RNO-6803157; Antimicrobial peptides.
DR   PRO; PR:Q8K4I4; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000013859; Expressed in lung and 4 other tissues.
DR   Genevisible; Q8K4I4; RN.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005902; C:microvillus; IDA:RGD.
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; ISO:RGD.
DR   GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR   GO; GO:0002395; P:immune response in nasopharyngeal-associated lymphoid tissue; ISO:RGD.
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..270
FT                   /note="BPI fold-containing family A member 1"
FT                   /id="PRO_0000017178"
FT   REGION          104..109
FT                   /note="Important for surfactant activity and antibacterial
FT                   properties"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP55"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        196..238
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP55"
SQ   SEQUENCE   270 AA;  27719 MW;  17B5EA3D4C845524 CRC64;
     MFLVGSLVVL CGLLAQSTAQ LAGLPLPLGQ GLPLPLGQGL PLPLGQGLPL AVSPALPSNP
     TDLLAGNFAN ALSGGLLSGG LLGILENIPL LDVIKSGGGS SNGLVGGLLG KLTSSVPLLN
     NILDIKITDP RLLELGLVQS PDGHRLYATI PLSLKLQVNM PVVGSFLQLA VKLNITAEIV
     AMKDNQGRIH LVLGDCTHSP GSLQITLLNG VTPVQSSLDS LTGILTKVLP ELIQGKVCPL
     INGILSGLDV TLVHNIAELL IHGIQFVIKV
 
 
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