OB76A_DROME
ID OB76A_DROME Reviewed; 153 AA.
AC O02372; E1JI39; Q29QG4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=General odorant-binding protein lush;
DE Flags: Precursor;
GN Name=lush; Synonyms=Obp76a, Obp76c; ORFNames=CG8807;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=9755202; DOI=10.1093/genetics/150.2.711;
RA Kim M.-S., Repp A., Smith D.P.;
RT "LUSH odorant-binding protein mediates chemosensory responses to alcohols
RT in Drosophila melanogaster.";
RL Genetics 150:711-721(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=11238251; DOI=10.1093/chemse/26.2.195;
RA Kim M.-S., Smith D.P.;
RT "The invertebrate odorant-binding protein LUSH is required for normal
RT olfactory behavior in Drosophila.";
RL Chem. Senses 26:195-199(2001).
RN [6]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11729153; DOI=10.1093/genetics/159.3.1059;
RA Galindo K., Smith D.P.;
RT "A large family of divergent Drosophila odorant-binding proteins expressed
RT in gustatory and olfactory sensilla.";
RL Genetics 159:1059-1072(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11754509; DOI=10.1002/jemt.1179;
RA Shanbhag S.R., Hekmat-Scafe D., Kim M.-S., Park S.-K., Carlson J.R.,
RA Pikielny C., Smith D.P., Steinbrecht R.A.;
RT "Expression mosaic of odorant-binding proteins in Drosophila olfactory
RT organs.";
RL Microsc. Res. Tech. 55:297-306(2001).
RN [8]
RP FUNCTION.
RX PubMed=14759510; DOI=10.1016/s0014-5793(03)01521-7;
RA Zhou J.-J., Zhang G.-A., Huang W., Birkett M.A., Field L.M., Pickett J.A.,
RA Pelosi P.;
RT "Revisiting the odorant-binding protein LUSH of Drosophila melanogaster:
RT evidence for odour recognition and discrimination.";
RL FEBS Lett. 558:23-26(2004).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15664171; DOI=10.1016/j.neuron.2004.12.031;
RA Xu P., Atkinson R., Jones D.N.M., Smith D.P.;
RT "Drosophila OBP LUSH is required for activity of pheromone-sensitive
RT neurons.";
RL Neuron 45:193-200(2005).
RN [10]
RP FUNCTION.
RX PubMed=16928861; DOI=10.1523/jneurosci.0876-06.2006;
RA Ha T.S., Smith D.P.;
RT "A pheromone receptor mediates 11-cis-vaccenyl acetate-induced responses in
RT Drosophila.";
RL J. Neurosci. 26:8727-8733(2006).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17943085; DOI=10.1038/nature06328;
RA Benton R., Vannice K.S., Vosshall L.B.;
RT "An essential role for a CD36-related receptor in pheromone detection in
RT Drosophila.";
RL Nature 450:289-293(2007).
RN [12] {ECO:0007744|PDB:1OOF, ECO:0007744|PDB:1OOG, ECO:0007744|PDB:1OOH, ECO:0007744|PDB:1OOI}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 30-153 OF APOPROTEIN AND
RP COMPLEXES WITH ETHANOL; BUTAN-1-OL AND PROPAN-1-OL.
RX PubMed=12881720; DOI=10.1038/nsb960;
RA Kruse S.W., Zhao R., Smith D.P., Jones D.N.M.;
RT "Structure of a specific alcohol-binding site defined by the odorant
RT binding protein LUSH from Drosophila melanogaster.";
RL Nat. Struct. Biol. 10:694-700(2003).
CC -!- FUNCTION: Odorant-binding protein required for olfactory behavior and
CC for activity of pheromone-sensitive neurons. Binds to alcohols and
CC mediates avoidance behavior to high concentrations of alcohols, the
CC alcohol-binding possibly resulting in activation of receptors on T2B
CC neurons, the activation of these receptors inhibiting these neurons.
CC Acts in concert with Snmp and lush to capture cVA molecules on the
CC surface of Or67d expressing olfactory dendrites and facilitate their
CC transfer to the odorant-receptor Orco complex. Required for cVA
CC response, probably by binding to VA. May act by serving as an adapter
CC that bridges the presence of gaseous pheromone molecules, cVA, to
CC activation of specific neuronal receptors expressed on T1 olfactory
CC neurons, possibly via a specific conformational change induced by cVA
CC that in turn activates T1 receptors. T1 neurons are excited by the
CC pheromone VA, while T2 neurons are inhibited by alcohols. Also binds to
CC phthalates. {ECO:0000269|PubMed:11238251, ECO:0000269|PubMed:14759510,
CC ECO:0000269|PubMed:15664171, ECO:0000269|PubMed:16928861,
CC ECO:0000269|PubMed:17943085, ECO:0000269|PubMed:9755202}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9755202}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in chemosensory system in
CC both males and females. Expressed in a subset of trichoid chemosensory
CC sensilla located on the ventral-lateral surface of the third antennal
CC segment. Secreted from non-neuronal support cells into the sensillum
CC lymph that bathes the olfactory neurons within these sensilla.
CC {ECO:0000269|PubMed:11729153, ECO:0000269|PubMed:11754509,
CC ECO:0000269|PubMed:15664171, ECO:0000269|PubMed:17943085,
CC ECO:0000269|PubMed:9755202}.
CC -!- SIMILARITY: Belongs to the PBP/GOBP family. {ECO:0000305}.
CC -!- CAUTION: According to some authors (PubMed:14759510) it does not bind
CC to ethanol. They suggest that the avoidance triggered by high
CC concentration of alcohols may be due to impurities, such as phthalates
CC or structurally related compounds, present as contaminants in the
CC ethanol used. They conclude that it may be directly and strictly
CC required for the perception of an odorant, rather than being involved
CC only in modulating the response to ethanol.
CC {ECO:0000305|PubMed:14759510}.
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DR EMBL; AF001621; AAB58940.1; -; mRNA.
DR EMBL; AE014296; AAF49136.1; -; Genomic_DNA.
DR EMBL; AE014296; ACZ94739.1; -; Genomic_DNA.
DR EMBL; BT024426; ABC86488.1; -; mRNA.
DR RefSeq; NP_001163468.1; NM_001169997.1.
DR RefSeq; NP_524162.1; NM_079438.3.
DR PDB; 1OOF; X-ray; 1.49 A; A/B=30-153.
DR PDB; 1OOG; X-ray; 1.45 A; A/B=30-153.
DR PDB; 1OOH; X-ray; 1.25 A; A/B=30-153.
DR PDB; 1OOI; X-ray; 2.04 A; X=30-153.
DR PDB; 1T14; X-ray; 1.86 A; A/B=30-153.
DR PDB; 2GTE; X-ray; 1.40 A; A/B=30-153.
DR PDB; 2QDI; X-ray; 2.00 A; A/B=30-153.
DR PDB; 3B6X; X-ray; 2.00 A; A/B=30-153.
DR PDB; 3B7A; X-ray; 1.90 A; A/B=30-153.
DR PDB; 3B86; X-ray; 2.00 A; A/B=30-153.
DR PDB; 3B87; X-ray; 2.00 A; A/B=30-153.
DR PDB; 3B88; X-ray; 2.00 A; A/B=30-153.
DR PDBsum; 1OOF; -.
DR PDBsum; 1OOG; -.
DR PDBsum; 1OOH; -.
DR PDBsum; 1OOI; -.
DR PDBsum; 1T14; -.
DR PDBsum; 2GTE; -.
DR PDBsum; 2QDI; -.
DR PDBsum; 3B6X; -.
DR PDBsum; 3B7A; -.
DR PDBsum; 3B86; -.
DR PDBsum; 3B87; -.
DR PDBsum; 3B88; -.
DR AlphaFoldDB; O02372; -.
DR SMR; O02372; -.
DR BioGRID; 65406; 4.
DR IntAct; O02372; 1.
DR STRING; 7227.FBpp0074737; -.
DR PaxDb; O02372; -.
DR DNASU; 40136; -.
DR EnsemblMetazoa; FBtr0074969; FBpp0074737; FBgn0020277.
DR EnsemblMetazoa; FBtr0301489; FBpp0290704; FBgn0020277.
DR GeneID; 40136; -.
DR KEGG; dme:Dmel_CG8807; -.
DR UCSC; CG8807-RA; d. melanogaster.
DR CTD; 40136; -.
DR FlyBase; FBgn0020277; lush.
DR VEuPathDB; VectorBase:FBgn0020277; -.
DR eggNOG; ENOG502SA47; Eukaryota.
DR GeneTree; ENSGT00940000176403; -.
DR HOGENOM; CLU_107288_0_0_1; -.
DR InParanoid; O02372; -.
DR OMA; LLCYTKC; -.
DR OrthoDB; 1461377at2759; -.
DR PhylomeDB; O02372; -.
DR BioGRID-ORCS; 40136; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; O02372; -.
DR GenomeRNAi; 40136; -.
DR PRO; PR:O02372; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0020277; Expressed in head capsule and 5 other tissues.
DR ExpressionAtlas; O02372; baseline and differential.
DR Genevisible; O02372; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0035275; F:dibutyl phthalate binding; IDA:FlyBase.
DR GO; GO:0035274; F:diphenyl phthalate binding; IDA:FlyBase.
DR GO; GO:0005549; F:odorant binding; TAS:FlyBase.
DR GO; GO:0005550; F:pheromone binding; IEA:UniProtKB-KW.
DR GO; GO:0007619; P:courtship behavior; IMP:FlyBase.
DR GO; GO:0042048; P:olfactory behavior; IDA:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; TAS:FlyBase.
DR GO; GO:0019236; P:response to pheromone; IDA:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR Gene3D; 1.10.238.20; -; 1.
DR InterPro; IPR006170; PBP/GOBP.
DR InterPro; IPR036728; PBP_GOBP_sf.
DR Pfam; PF01395; PBP_GOBP; 1.
DR SMART; SM00708; PhBP; 1.
DR SUPFAM; SSF47565; SSF47565; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Behavior; Disulfide bond; Olfaction; Pheromone response;
KW Pheromone-binding; Reference proteome; Secreted; Sensory transduction;
KW Signal; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..153
FT /note="General odorant-binding protein lush"
FT /id="PRO_0000012577"
FT BINDING 81
FT /ligand="1-propanol"
FT /ligand_id="ChEBI:CHEBI:28831"
FT /evidence="ECO:0000269|PubMed:12881720,
FT ECO:0007744|PDB:1OOG"
FT BINDING 81
FT /ligand="butan-1-ol"
FT /ligand_id="ChEBI:CHEBI:28885"
FT /evidence="ECO:0000269|PubMed:12881720,
FT ECO:0007744|PDB:1OOH"
FT BINDING 81
FT /ligand="ethanol"
FT /ligand_id="ChEBI:CHEBI:16236"
FT /evidence="ECO:0000269|PubMed:12881720,
FT ECO:0007744|PDB:1OOF"
FT BINDING 86
FT /ligand="1-propanol"
FT /ligand_id="ChEBI:CHEBI:28831"
FT /evidence="ECO:0000269|PubMed:12881720,
FT ECO:0007744|PDB:1OOG"
FT BINDING 86
FT /ligand="butan-1-ol"
FT /ligand_id="ChEBI:CHEBI:28885"
FT /evidence="ECO:0000269|PubMed:12881720,
FT ECO:0007744|PDB:1OOH"
FT BINDING 86
FT /ligand="ethanol"
FT /ligand_id="ChEBI:CHEBI:16236"
FT /evidence="ECO:0000269|PubMed:12881720,
FT ECO:0007744|PDB:1OOF"
FT DISULFID 46..79
FT /evidence="ECO:0000250"
FT DISULFID 75..132
FT /evidence="ECO:0000250"
FT DISULFID 121..141
FT /evidence="ECO:0000250"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1OOH"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:1OOH"
SQ SEQUENCE 153 AA; 17437 MW; 60EBED58C2B06178 CRC64;
MKHWKRRSSA VFAIVLQVLV LLLPDPAVAM TMEQFLTSLD MIRSGCAPKF KLKTEDLDRL
RVGDFNFPPS QDLMCYTKCV SLMAGTVNKK GEFNAPKALA QLPHLVPPEM MEMSRKSVEA
CRDTHKQFKE SCERVYQTAK CFSENADGQF MWP
