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BPIA2_HUMAN
ID   BPIA2_HUMAN             Reviewed;         249 AA.
AC   Q96DR5; Q9BQQ0;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=BPI fold-containing family A member 2;
DE   AltName: Full=Parotid secretory protein;
DE            Short=PSP;
DE   AltName: Full=Short palate, lung and nasal epithelium carcinoma-associated protein 2;
DE   Flags: Precursor;
GN   Name=BPIFA2; Synonyms=C20orf70, SPLUNC2; ORFNames=UNQ510/PRO1025;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Parotid gland;
RA   Venkatesh S.G., Geetha C., Gorr S.-U.;
RT   "A member of the PSP/plunc family of BPI proteins is expressed in the human
RT   parotid gland.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11971875; DOI=10.1093/hmg/11.8.937;
RA   Bingle C.D., Craven C.J.;
RT   "PLUNC: a novel family of candidate host defence proteins expressed in the
RT   upper airways and nasopharynx.";
RL   Hum. Mol. Genet. 11:937-943(2002).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124 AND ASN-132.
RC   TISSUE=Saliva;
RX   PubMed=16740002; DOI=10.1021/pr050492k;
RA   Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT   "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT   capture and mass spectrometry.";
RL   J. Proteome Res. 5:1493-1503(2006).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=24581853; DOI=10.1016/j.archoralbio.2013.12.005;
RA   Prokopovic V., Popovic M., Andjelkovic U., Marsavelski A., Raskovic B.,
RA   Gavrovic-Jankulovic M., Polovic N.;
RT   "Isolation, biochemical characterization and anti-bacterial activity of
RT   BPIFA2 protein.";
RL   Arch. Oral Biol. 59:302-309(2014).
CC   -!- FUNCTION: Has strong antibacterial activity against P. aeruginosa.
CC       {ECO:0000269|PubMed:24581853}.
CC   -!- INTERACTION:
CC       Q96DR5; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-10284754, EBI-741181;
CC       Q96DR5; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-10284754, EBI-11522760;
CC       Q96DR5; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-10284754, EBI-1054315;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in submandibular gland. Secreted into
CC       saliva. {ECO:0000269|PubMed:11971875, ECO:0000269|PubMed:24581853}.
CC   -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. Plunc family.
CC       {ECO:0000305}.
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DR   EMBL; AF432917; AAL28113.1; -; mRNA.
DR   EMBL; AY359055; AAQ89414.1; -; mRNA.
DR   EMBL; AL121901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC065726; AAH65726.1; -; mRNA.
DR   CCDS; CCDS13214.1; -.
DR   RefSeq; NP_001306093.1; NM_001319164.1.
DR   RefSeq; NP_542141.1; NM_080574.3.
DR   AlphaFoldDB; Q96DR5; -.
DR   SMR; Q96DR5; -.
DR   BioGRID; 126647; 30.
DR   IntAct; Q96DR5; 10.
DR   STRING; 9606.ENSP00000253362; -.
DR   GlyGen; Q96DR5; 2 sites.
DR   iPTMnet; Q96DR5; -.
DR   BioMuta; BPIFA2; -.
DR   DMDM; 34395850; -.
DR   MassIVE; Q96DR5; -.
DR   PaxDb; Q96DR5; -.
DR   PeptideAtlas; Q96DR5; -.
DR   PRIDE; Q96DR5; -.
DR   ProteomicsDB; 76306; -.
DR   Antibodypedia; 25522; 197 antibodies from 24 providers.
DR   DNASU; 140683; -.
DR   Ensembl; ENST00000253362.6; ENSP00000253362.2; ENSG00000131050.11.
DR   Ensembl; ENST00000354932.6; ENSP00000347012.5; ENSG00000131050.11.
DR   GeneID; 140683; -.
DR   KEGG; hsa:140683; -.
DR   MANE-Select; ENST00000354932.6; ENSP00000347012.5; NM_080574.4; NP_542141.1.
DR   UCSC; uc002wyo.2; human.
DR   CTD; 140683; -.
DR   DisGeNET; 140683; -.
DR   GeneCards; BPIFA2; -.
DR   HGNC; HGNC:16203; BPIFA2.
DR   HPA; ENSG00000131050; Tissue enriched (salivary).
DR   neXtProt; NX_Q96DR5; -.
DR   OpenTargets; ENSG00000131050; -.
DR   PharmGKB; PA25781; -.
DR   VEuPathDB; HostDB:ENSG00000131050; -.
DR   eggNOG; ENOG502TE6F; Eukaryota.
DR   GeneTree; ENSGT01020000230460; -.
DR   HOGENOM; CLU_097590_0_0_1; -.
DR   InParanoid; Q96DR5; -.
DR   OMA; QNELCPR; -.
DR   OrthoDB; 1389938at2759; -.
DR   PhylomeDB; Q96DR5; -.
DR   TreeFam; TF337052; -.
DR   PathwayCommons; Q96DR5; -.
DR   Reactome; R-HSA-6803157; Antimicrobial peptides.
DR   SignaLink; Q96DR5; -.
DR   BioGRID-ORCS; 140683; 10 hits in 1069 CRISPR screens.
DR   ChiTaRS; BPIFA2; human.
DR   GenomeRNAi; 140683; -.
DR   Pharos; Q96DR5; Tbio.
DR   PRO; PR:Q96DR5; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q96DR5; protein.
DR   Bgee; ENSG00000131050; Expressed in parotid gland and 55 other tissues.
DR   Genevisible; Q96DR5; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR   InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR   Pfam; PF01273; LBP_BPI_CETP; 1.
DR   SUPFAM; SSF55394; SSF55394; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..249
FT                   /note="BPI fold-containing family A member 2"
FT                   /id="PRO_0000017184"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002"
FT   DISULFID        174..217
FT                   /evidence="ECO:0000250"
FT   VARIANT         43
FT                   /note="G -> R (in dbSNP:rs6059139)"
FT                   /id="VAR_049751"
FT   VARIANT         113
FT                   /note="K -> E (in dbSNP:rs17304572)"
FT                   /id="VAR_049752"
FT   VARIANT         221
FT                   /note="R -> C (in dbSNP:rs6120140)"
FT                   /id="VAR_049753"
FT   CONFLICT        172
FT                   /note="G -> R (in Ref. 1; AAL28113)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  27011 MW;  E64E0794A1B4DB7D CRC64;
     MLQLWKLVLL CGVLTGTSES LLDNLGNDLS NVVDKLEPVL HEGLETVDNT LKGILEKLKV
     DLGVLQKSSA WQLAKQKAQE AEKLLNNVIS KLLPTNTDIF GLKISNSLIL DVKAEPIDDG
     KGLNLSFPVT ANVTVAGPII GQIINLKASL DLLTAVTIET DPQTHQPVAV LGECASDPTS
     ISLSLLDKHS QIINKFVNSV INTLKSTVSS LLQKEICPLI RIFIHSLDVN VIQQVVDNPQ
     HKTQLQTLI
 
 
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