OBP2A_HUMAN
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 03-AUG-2022, entry version 145.
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), AND
RP 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] {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: Probably binds and transports small hydrophobic volatile
CC molecules with a higher affinity for aldehydes and large fatty acids.
CC {ECO:0000269|PubMed:12044155}.
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.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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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 STRING; 9606.ENSP00000441028; -.
DR DrugBank; DB00755; Tretinoin.
DR SwissLipids; SLP:000001528; -. [Q9NY56-1]
DR iPTMnet; Q9NY56; -.
DR PhosphoSitePlus; Q9NY56; -.
DR BioMuta; OBP2A; -.
DR MassIVE; Q9NY56; -.
DR PaxDb; Q9NY56; -.
DR PeptideAtlas; Q9NY56; -.
DR PRIDE; Q9NY56; -.
DR ProteomicsDB; 83174; -. [Q9NY56-1]
DR ProteomicsDB; 83175; -. [Q9NY56-2]
DR ProteomicsDB; 83177; -. [Q9NY56-4]
DR Antibodypedia; 56439; 71 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 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; TENCIPE; -.
DR OrthoDB; 1450978at2759; -.
DR PhylomeDB; Q9NY56; -.
DR TreeFam; TF338197; -.
DR PathwayCommons; Q9NY56; -.
DR SignaLink; Q9NY56; -.
DR BioGRID-ORCS; 29991; 24 hits in 995 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 tissues.
DR ExpressionAtlas; Q9NY56; baseline and differential.
DR Genevisible; Q9NY56; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005549; F:odorant binding; NAS:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
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 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; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01175; VNEBNERGLAND.
DR SUPFAM; SSF50814; SSF50814; 1.
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 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
