ID OBP2A_HUMAN Reviewed; 170 AA. AC Q9NY56; Q5T8A3; Q9NY50; Q9NY53; Q9NY54; Q9NY55; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JAN-2024, entry version 152. DE RecName: Full=Odorant-binding protein 2a; DE AltName: Full=Odorant-binding protein IIa; DE Short=OBPIIa; DE Flags: Precursor; GN Name=OBP2A; 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 [GENOMIC DNA / MRNA] (ISOFORMS AA; AB; AD AND AG), RP TISSUE SPECIFICITY, AND VARIANT THR-159. RX PubMed=10607840; DOI=10.1093/hmg/9.2.289; RA Lacazette E., Gachon A.-M., Pitiot G.; RT "A novel human odorant-binding protein gene family resulting from genomic RT duplicons at 9q34: differential expression in the oral and genital RT spheres."; RL Hum. Mol. Genet. 9:289-301(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AA). 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 [4] RP FUNCTION, SUBUNIT, AND DISULFIDE BOND. RX PubMed=12044155; DOI=10.1021/bi015916c; RA Briand L., Eloit C., Nespoulous C., Bezirard V., Huet J.C., Henry C., RA Blon F., Trotier D., Pernollet J.C.; RT "Evidence of an odorant-binding protein in the human olfactory mucus: RT location, structural characterization, and odorant-binding properties."; RL Biochemistry 41:7241-7252(2002). RN [5] RP FUNCTION, AND MUTAGENESIS OF LYS-77; LYS-97 AND LYS-127. RX PubMed=16546182; DOI=10.1016/j.febslet.2006.03.017; RA Tcatchoff L., Nespoulous C., Pernollet J.C., Briand L.; RT "A single lysyl residue defines the binding specificity of a human odorant- RT binding protein for aldehydes."; RL FEBS Lett. 580:2102-2108(2006). RN [6] RP TISSUE SPECIFICITY. RX PubMed=27827363; DOI=10.1038/ncomms13267; RA Ekim Uestuenel B., Friedrich K., Maida A., Wang X., Krones-Herzig A., RA Seibert O., Sommerfeld A., Jones A., Sijmonsma T.P., Sticht C., Gretz N., RA Fleming T., Nawroth P.P., Stremmel W., Rose A.J., Berriel-Diaz M., RA Blueher M., Herzig S.; RT "Control of diabetic hyperglycaemia and insulin resistance through RT TSC22D4."; RL Nat. Commun. 7:13267-13267(2016). RN [7] {ECO:0007744|PDB:4RUN} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 23-169, DISULFIDE BONDS, AND RP SUBUNIT. RX PubMed=25810031; DOI=10.1002/prot.24797; RA Schiefner A., Freier R., Eichinger A., Skerra A.; RT "Crystal structure of the human odorant binding protein, OBPIIa."; RL Proteins 83:1180-1184(2015). CC -!- FUNCTION: Binds and transports small hydrophobic volatile molecules CC with a higher affinity for aldehydes and large fatty acids, including CC undecanal, palmitic acid, efficient aldehydes, benzenic aldehydes, CC heterocyclic aldehydes and aliphatic acids. CC {ECO:0000269|PubMed:12044155, ECO:0000269|PubMed:16546182}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12044155, CC ECO:0000269|PubMed:25810031}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Aa; CC IsoId=Q9NY56-1; Sequence=Displayed; CC Name=Ab; CC IsoId=Q9NY56-2; Sequence=VSP_003136; CC Name=Ad; CC IsoId=Q9NY56-3; Sequence=VSP_003135; CC Name=Ag; CC IsoId=Q9NY56-4; Sequence=VSP_003137; CC -!- TISSUE SPECIFICITY: Strongly expressed in the nasal structures, CC salivary and lachrymal glands, and lung (PubMed:10607840). Expressed in CC the liver (PubMed:27827363). {ECO:0000269|PubMed:10607840, CC ECO:0000269|PubMed:27827363}. CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ251021; CAB71318.1; -; mRNA. DR EMBL; AJ251022; CAB71319.1; -; mRNA. DR EMBL; AJ251023; CAB71320.1; -; mRNA. DR EMBL; AJ251024; CAB71321.1; -; mRNA. DR EMBL; AJ251029; CAB71326.1; -; Genomic_DNA. DR EMBL; AL161452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069563; AAH69563.1; -; mRNA. DR CCDS; CCDS6992.1; -. [Q9NY56-1] DR CCDS; CCDS78455.1; -. [Q9NY56-4] DR CCDS; CCDS78456.1; -. [Q9NY56-3] DR RefSeq; NP_001280118.1; NM_001293189.1. DR RefSeq; NP_001280122.1; NM_001293193.1. DR RefSeq; NP_055397.1; NM_014582.2. [Q9NY56-1] DR PDB; 4RUN; X-ray; 2.60 A; A/B=16-170. DR PDBsum; 4RUN; -. DR AlphaFoldDB; Q9NY56; -. DR SMR; Q9NY56; -. DR BioGRID; 119016; 13. DR IntAct; Q9NY56; 7. DR MINT; Q9NY56; -. DR DrugBank; DB00755; Tretinoin. DR SwissLipids; SLP:000001528; -. [Q9NY56-1] DR iPTMnet; Q9NY56; -. DR PhosphoSitePlus; Q9NY56; -. DR BioMuta; OBP2A; -. DR MassIVE; Q9NY56; -. DR PaxDb; 9606-ENSP00000441028; -. DR PeptideAtlas; Q9NY56; -. DR ProteomicsDB; 83174; -. [Q9NY56-1] DR ProteomicsDB; 83175; -. [Q9NY56-2] DR ProteomicsDB; 83176; -. [Q9NY56-3] DR ProteomicsDB; 83177; -. [Q9NY56-4] DR Antibodypedia; 56439; 85 antibodies from 13 providers. DR DNASU; 29991; -. DR Ensembl; ENST00000371776.6; ENSP00000360841.1; ENSG00000122136.14. [Q9NY56-1] DR Ensembl; ENST00000539850.1; ENSP00000441028.1; ENSG00000122136.14. [Q9NY56-1] DR GeneID; 29991; -. DR KEGG; hsa:29991; -. DR MANE-Select; ENST00000371776.6; ENSP00000360841.1; NM_014582.3; NP_055397.1. DR UCSC; uc004cgb.3; human. [Q9NY56-1] DR AGR; HGNC:23380; -. DR CTD; 29991; -. DR DisGeNET; 29991; -. DR GeneCards; OBP2A; -. DR HGNC; HGNC:23380; OBP2A. DR HPA; ENSG00000122136; Tissue enriched (fallopian). DR MIM; 164320; gene. DR neXtProt; NX_Q9NY56; -. DR OpenTargets; ENSG00000122136; -. DR PharmGKB; PA134915019; -. DR VEuPathDB; HostDB:ENSG00000122136; -. DR eggNOG; ENOG502S22P; Eukaryota. DR GeneTree; ENSGT01050000244868; -. DR HOGENOM; CLU_125034_0_0_1; -. DR InParanoid; Q9NY56; -. DR OMA; WYIKAMV; -. DR OrthoDB; 4660635at2759; -. DR PhylomeDB; Q9NY56; -. DR TreeFam; TF338197; -. DR PathwayCommons; Q9NY56; -. DR SignaLink; Q9NY56; -. DR BioGRID-ORCS; 29991; 31 hits in 1070 CRISPR screens. DR GeneWiki; OBP2A; -. DR GenomeRNAi; 29991; -. DR Pharos; Q9NY56; Tbio. DR PRO; PR:Q9NY56; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9NY56; Protein. DR Bgee; ENSG00000122136; Expressed in right uterine tube and 86 other cell types or tissues. DR ExpressionAtlas; Q9NY56; baseline and differential. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005549; F:odorant binding; IDA:UniProtKB. DR GO; GO:0036094; F:small molecule binding; IEA:InterPro. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007606; P:sensory perception of chemical stimulus; TAS:ProtInc. DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW. DR CDD; cd19414; lipocalin_1_3_4_13-like; 1. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR012674; Calycin. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom. DR InterPro; IPR002450; von_Ebner_gland. DR PANTHER; PTHR11430; LIPOCALIN; 1. DR PANTHER; PTHR11430:SF129; ODORANT-BINDING PROTEIN 2A-RELATED; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR01175; VNEBNERGLAND. DR SUPFAM; SSF50814; Lipocalins; 1. DR Genevisible; Q9NY56; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disulfide bond; Olfaction; KW Reference proteome; Secreted; Sensory transduction; Signal; Transport. FT SIGNAL 1..15 FT /evidence="ECO:0000255" FT CHAIN 16..170 FT /note="Odorant-binding protein 2a" FT /id="PRO_0000017937" FT DISULFID 74..166 FT /evidence="ECO:0000269|PubMed:12044155, FT ECO:0000269|PubMed:25810031, ECO:0007744|PDB:4RUN" FT VAR_SEQ 25..129 FT /note="ITGTWYVKAMVVDKDFPEDRRPRKVSPVKVTALGGGNLEATFTFMREDRCIQ FT KKILMRKTEEPGKFSAYGGRKLIYLQELPGTDDYVFYCKDQRRGGLRYMGKLV -> EG FT ESVHPEENPDAEDGGAWQIQRLWGQEAHIPAGAARDGRLRLLLQRPAPWGPALHGKACG FT ICSLQGRAAVPTLAHLATSPA (in isoform Ad)" FT /evidence="ECO:0000303|PubMed:10607840" FT /id="VSP_003135" FT VAR_SEQ 130..170 FT /note="GRNPNTNLEALEEFKKLVQHKGLSEEDIFMPLQTGSCVLEH -> ASAPCRA FT VPLSPRRLTWPPHLQVGILIPTWRPWKNLRNWCSTRDSRRRTFSCPCRREAAFSNTRQP FT PGLHLQSPPYHQTQSPDHLDLPSSHDPSLLPPT (in isoform Ag)" FT /evidence="ECO:0000303|PubMed:10607840" FT /id="VSP_003137" FT VAR_SEQ 131..170 FT /note="RNPNTNLEALEEFKKLVQHKGLSEEDIFMPLQTGSCVLEH -> PCRCPHVG FT SPGHLTCR (in isoform Ab)" FT /evidence="ECO:0000303|PubMed:10607840" FT /id="VSP_003136" FT VARIANT 61 FT /note="N -> K (in dbSNP:rs3180357)" FT /id="VAR_034354" FT VARIANT 130 FT /note="G -> A (in dbSNP:rs55695858)" FT /id="VAR_061359" FT VARIANT 133 FT /note="P -> S (in dbSNP:rs3178137)" FT /id="VAR_061360" FT VARIANT 159 FT /note="M -> T (in dbSNP:rs2853652)" FT /evidence="ECO:0000269|PubMed:10607840" FT /id="VAR_050176" FT MUTAGEN 77 FT /note="K->A: No effect on binding affinity for undecanal, FT palmitic acid, efficient aldehydes, benzenic aldehydes, FT heterocyclic aldehydes or aliphatic acids." FT /evidence="ECO:0000269|PubMed:16546182" FT MUTAGEN 97 FT /note="K->A: No effect on binding affinity for undecanal, FT palmitic acid, efficient aldehydes, benzenic aldehydes, FT heterocyclic aldehydes or aliphatic acids." FT /evidence="ECO:0000269|PubMed:16546182" FT MUTAGEN 127 FT /note="K->A: Decreases binding affinity for undecanal, FT efficient aldehydes and aliphatic acids from 9- to FT 12-carbons long. No effect on binding affinity of benzenic FT or heterocyclic aldehydes." FT /evidence="ECO:0000269|PubMed:16546182" FT CONFLICT 90 FT /note="F -> Y (in Ref. 1; CAB71326)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="H -> R (in Ref. 1; CAB71320)" FT /evidence="ECO:0000305" FT STRAND 27..36 FT /evidence="ECO:0007829|PDB:4RUN" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 62..70 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 73..82 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:4RUN" FT TURN 93..96 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 110..118 FT /evidence="ECO:0007829|PDB:4RUN" FT STRAND 121..133 FT /evidence="ECO:0007829|PDB:4RUN" FT HELIX 137..149 FT /evidence="ECO:0007829|PDB:4RUN" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:4RUN" SQ SEQUENCE 170 AA; 19318 MW; 391F55E2E3629E75 CRC64; MKTLFLGVTL GLAAALSFTL EEEDITGTWY VKAMVVDKDF PEDRRPRKVS PVKVTALGGG NLEATFTFMR EDRCIQKKIL MRKTEEPGKF SAYGGRKLIY LQELPGTDDY VFYCKDQRRG GLRYMGKLVG RNPNTNLEAL EEFKKLVQHK GLSEEDIFMP LQTGSCVLEH //