OB69A_DROME
ID OB69A_DROME Reviewed; 148 AA.
AC P54191; Q9VTX0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=General odorant-binding protein 69a;
DE AltName: Full=Odorant-binding protein 69a;
DE AltName: Full=Pheromone-binding protein-related protein 1;
DE Short=PBPRP-1;
DE Flags: Precursor;
GN Name=Obp69a; Synonyms=Pbprp1; ORFNames=CG10436;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Antenna;
RX PubMed=7545907; DOI=10.1016/0896-6273(94)90150-3;
RA Pikielny C.W., Hasan G., Rouyer F., Rosbash M.;
RT "Members of a family of Drosophila putative odorant-binding proteins are
RT expressed in different subsets of olfactory hairs.";
RL Neuron 12:35-49(1994).
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY
RP CIS-VACCENYL ACETATE, AND DISRUPTION PHENOTYPE.
RX PubMed=29630598; DOI=10.1371/journal.pgen.1007328;
RA Bentzur A., Shmueli A., Omesi L., Ryvkin J., Knapp J.M., Parnas M.,
RA Davis F.P., Shohat-Ophir G.;
RT "Odorant binding protein 69a connects social interaction to modulation of
RT social responsiveness in Drosophila.";
RL PLoS Genet. 14:E1007328-E1007328(2018).
CC -!- FUNCTION: Odorant-binding protein required for olfactory behavior and
CC activity of pheromone-sensitive neurons in response to the male-
CC specific pheromone cis-vaccenyl acetate (cVA). Modulates social
CC responsivity differently in males and females, regulating male
CC aggression and female receptivity respectively.
CC {ECO:0000269|PubMed:29630598}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29630598}.
CC Note=Secreted in the lumen of olfactory hairs.
CC {ECO:0000269|PubMed:29630598}.
CC -!- TISSUE SPECIFICITY: Expressed in the antenna, mostly on the anterior
CC surface of the third antennal segment (PubMed:7545907,
CC PubMed:29630598). Expressed in auxilary cells and the third antennal
CC segment and exported to the sensillar lymph (at protein level)
CC (PubMed:29630598). {ECO:0000269|PubMed:29630598,
CC ECO:0000269|PubMed:7545907}.
CC -!- INDUCTION: Expression is inversely regulated in male and female in
CC response to the male-specific pheromone cis-vaccenyl acetate (cVA) and
CC is dependent on the active neurotransmission of cVA-sensitive neurons
CC to second order olfactory neurons. {ECO:0000269|PubMed:29630598}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in males results in
CC reduction of aggressive display. RNAi-mediated knockdown in females
CC results in a significant reduction in sexual receptivity after exposure
CC to the male-specific pheromone cis-vaccenyl acetate (cVA).
CC {ECO:0000269|PubMed:29630598}.
CC -!- SIMILARITY: Belongs to the PBP/GOBP family. {ECO:0000305}.
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DR EMBL; U05980; AAC46474.1; -; mRNA.
DR EMBL; AE014296; AAF49925.1; -; Genomic_DNA.
DR RefSeq; NP_524039.2; NM_079315.2.
DR AlphaFoldDB; P54191; -.
DR SMR; P54191; -.
DR BioGRID; 64763; 1.
DR DIP; DIP-18244N; -.
DR STRING; 7227.FBpp0075687; -.
DR PaxDb; P54191; -.
DR EnsemblMetazoa; FBtr0075955; FBpp0075687; FBgn0011279.
DR GeneID; 39411; -.
DR KEGG; dme:Dmel_CG10436; -.
DR CTD; 39411; -.
DR FlyBase; FBgn0011279; Obp69a.
DR VEuPathDB; VectorBase:FBgn0011279; -.
DR eggNOG; ENOG502S7DV; Eukaryota.
DR HOGENOM; CLU_107288_1_2_1; -.
DR InParanoid; P54191; -.
DR OMA; CMFDMFG; -.
DR OrthoDB; 1145531at2759; -.
DR PhylomeDB; P54191; -.
DR BioGRID-ORCS; 39411; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39411; -.
DR PRO; PR:P54191; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011279; Expressed in head capsule and 10 other tissues.
DR Genevisible; P54191; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005549; F:odorant binding; ISS:FlyBase.
DR GO; GO:0008145; F:phenylalkylamine binding; ISS:FlyBase.
DR GO; GO:0005550; F:pheromone binding; ISS:FlyBase.
DR GO; GO:0007619; P:courtship behavior; IMP:UniProtKB.
DR GO; GO:0042048; P:olfactory behavior; IMP:UniProtKB.
DR GO; GO:0019236; P:response to pheromone; IMP:UniProtKB.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; ISS:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:UniProtKB.
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 Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..148
FT /note="General odorant-binding protein 69a"
FT /id="PRO_0000012586"
FT DISULFID 42..74
FT /evidence="ECO:0000250"
FT DISULFID 70..121
FT /evidence="ECO:0000250"
FT DISULFID 112..130
FT /evidence="ECO:0000250"
FT CONFLICT 102
FT /note="H -> Y (in Ref. 1; AAC46474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16726 MW; EB8D417130226A5E CRC64;
MVARHFSFFL ALLILYDLIP SNQGVEINPT IIKQVRKLRM RCLNQTGASV DVIDKSVKNR
ILPTDPEIKC FLYCMFDMFG LIDSQNIMHL EALLEVLPEE IHKTINGLVS SCGTQKGKDG
CDTAYETVKC YIAVNGKFIW EEIIVLLG
