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ORCO_DROME
ID   ORCO_DROME              Reviewed;         486 AA.
AC   Q9VNB5; A8JQT8; Q672R0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Odorant receptor coreceptor;
DE   AltName: Full=Odorant receptor 83b;
GN   Name=Orco; Synonyms=A45, Or83b; ORFNames=CG10609;
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND VARIANT ILE-143.
RC   STRAIN=Oregon-R; TISSUE=Antenna, and Maxillary palp;
RX   PubMed=15339651; DOI=10.1016/j.neuron.2004.08.019;
RA   Larsson M.C., Domingos A.I., Jones W.D., Chiappe M.E., Amrein H.,
RA   Vosshall L.B.;
RT   "Or83b encodes a broadly expressed odorant receptor essential for
RT   Drosophila olfaction.";
RL   Neuron 43:703-714(2004).
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   TISSUE SPECIFICITY.
RX   PubMed=10089887; DOI=10.1016/s0092-8674(00)80582-6;
RA   Vosshall L.B., Amrein H., Morozov P.S., Rzhetsky A., Axel R.;
RT   "A spatial map of olfactory receptor expression in the Drosophila
RT   antenna.";
RL   Cell 96:725-736(1999).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=10943836; DOI=10.1016/s0092-8674(00)00021-0;
RA   Vosshall L.B., Wong A.M., Axel R.;
RT   "An olfactory sensory map in the fly brain.";
RL   Cell 102:147-159(2000).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH OR22A.
RX   PubMed=15592462; DOI=10.1038/nn1371;
RA   Neuhaus E.M., Gisselmann G., Zhang W., Dooley R., Stortkuhl K., Hatt H.;
RT   "Odorant receptor heterodimerization in the olfactory system of Drosophila
RT   melanogaster.";
RL   Nat. Neurosci. 8:15-17(2005).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH ORS, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16402857; DOI=10.1371/journal.pbio.0040020;
RA   Benton R., Sachse S., Michnick S.W., Vosshall L.B.;
RT   "Atypical membrane topology and heteromeric function of Drosophila odorant
RT   receptors in vivo.";
RL   PLoS Biol. 4:E20-E20(2006).
RN   [8]
RP   TOPOLOGY, GLYCOSYLATION AT ASN-169, AND MUTAGENESIS OF ASN-169.
RX   PubMed=18005664; DOI=10.1016/j.febslet.2007.11.007;
RA   Lundin C., Kaell L., Kreher S.A., Kapp K., Sonnhammer E.L., Carlson J.R.,
RA   von Heijne G., Nilsson I.;
RT   "Membrane topology of the Drosophila OR83b odorant receptor.";
RL   FEBS Lett. 581:5601-5604(2007).
RN   [9]
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   [10]
RP   FUNCTION, AND INTERACTION WITH OR47A.
RX   PubMed=18408712; DOI=10.1038/nature06850;
RA   Sato K., Pellegrino M., Nakagawa T., Nakagawa T., Vosshall L.B.,
RA   Touhara K.;
RT   "Insect olfactory receptors are heteromeric ligand-gated ion channels.";
RL   Nature 452:1002-1006(2008).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH OR22A AND OR47A.
RX   PubMed=18408711; DOI=10.1038/nature06861;
RA   Wicher D., Schaefer R., Bauernfeind R., Stensmyr M.C., Heller R.,
RA   Heinemann S.H., Hansson B.S.;
RT   "Drosophila odorant receptors are both ligand-gated and cyclic-nucleotide-
RT   activated cation channels.";
RL   Nature 452:1007-1011(2008).
RN   [12]
RP   INTERACTION WITH ORCO, AND FUNCTION.
RX   PubMed=20147286; DOI=10.1074/jbc.m109.058321;
RA   Nichols A.S., Luetje C.W.;
RT   "Transmembrane segment 3 of Drosophila melanogaster odorant receptor
RT   subunit 85b contributes to ligand-receptor interactions.";
RL   J. Biol. Chem. 285:11854-11862(2010).
RN   [13]
RP   INTERACTION WITH OR35A AND OR67A, AND FUNCTION.
RX   PubMed=21677030; DOI=10.1093/chemse/bjr053;
RA   Nichols A.S., Chen S., Luetje C.W.;
RT   "Subunit contributions to insect olfactory receptor function: channel block
RT   and odorant recognition.";
RL   Chem. Senses 36:781-790(2011).
RN   [14]
RP   INTERACTION WITH OR59B, AND FUNCTION.
RX   PubMed=21937991; DOI=10.1038/nature10438;
RA   Pellegrino M., Steinbach N., Stensmyr M.C., Hansson B.S., Vosshall L.B.;
RT   "A natural polymorphism alters odour and DEET sensitivity in an insect
RT   odorant receptor.";
RL   Nature 478:511-514(2011).
CC   -!- FUNCTION: Odorant coreceptor which complexes with conventional odorant
CC       receptors (ORs) to form odorant-sensing units, providing sensitive and
CC       prolonged odorant signaling and calcium permeability. Orco is a
CC       universal and integral part of the functional odorant receptor,
CC       involved in the dendritic localization of other olfactory receptors.
CC       Expression of Orco alone leads to formation of rapid and transient ion
CC       channels not directly responding to odorants, but directly activated by
CC       intracellular cAMP or cGMP. Snmp, Or67d and lush act in concert to
CC       capture fatty-acid-derived male pheromone 11-cis vaccenyl acetate (cVA)
CC       molecules on the surface of Or67d expressing olfactory dendrites and
CC       facilitate their transfer to the odorant-receptor Orco complex.
CC       {ECO:0000269|PubMed:15339651, ECO:0000269|PubMed:15592462,
CC       ECO:0000269|PubMed:16402857, ECO:0000269|PubMed:17943085,
CC       ECO:0000269|PubMed:18408711, ECO:0000269|PubMed:18408712,
CC       ECO:0000269|PubMed:20147286, ECO:0000269|PubMed:21677030,
CC       ECO:0000269|PubMed:21937991}.
CC   -!- SUBUNIT: Heterodimer with conventional odorant receptors (ORs).
CC       Complexes exist early in the endomembrane system in olfactory sensory
CC       neurons (OSNs), coupling these complexes to the conserved ciliary
CC       trafficking pathway.
CC   -!- INTERACTION:
CC       Q9VNB5; P81917: Or43a; NbExp=2; IntAct=EBI-15562228, EBI-15562282;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16402857};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16402857}.
CC   -!- TISSUE SPECIFICITY: Expression is restricted to olfactory sensory
CC       neurons (OSNs). Coexpressed with Snmp in a lateral-distal population of
CC       OSNs. Expressed in the embryonic antennal-maxillary complex, in all 21
CC       OSNs of the larval dorsal organ, in the pupal antennal OSNs, in all 120
CC       adult maxillary palp neurons and in approximately 70-80% of adult
CC       antennal OSNs, where expression is highest at the dorsal-medial edge.
CC       Localized to OSN cell bodies and to the distal portion of ciliated OSN
CC       dendrites. {ECO:0000269|PubMed:10089887, ECO:0000269|PubMed:10943836,
CC       ECO:0000269|PubMed:15339651, ECO:0000269|PubMed:16402857,
CC       ECO:0000269|PubMed:17943085}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout all developmental stages.
CC       First expressed at embryonic stage 15. Pupal expression first occurs 80
CC       hours after puparium formation. {ECO:0000269|PubMed:15339651}.
CC   -!- MISCELLANEOUS: The atypical heteromeric and topological design of the
CC       odorant receptors appears to be an insect-specific solution for odor
CC       recognition, making the OR/Orco complex an attractive target for the
CC       development of highly selective insect repellents to disrupt olfactory-
CC       mediated host-seeking behaviors of insect disease vectors. Odor-evoked
CC       OR currents are independent of known G-protein-coupled second messenger
CC       pathways. The homomeric Orco channel is thought to be a cyclic-
CC       nucleotide-gated ion channel that depolarizes the olfactory receptor
CC       neuron.
CC   -!- SIMILARITY: Belongs to the insect chemoreceptor superfamily.
CC       Heteromeric odorant receptor channel (TC 1.A.69) family. Orco
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY567998; AAT71306.1; -; mRNA.
DR   EMBL; AE014297; AAF52031.2; -; Genomic_DNA.
DR   EMBL; AE014297; ABW08603.1; -; Genomic_DNA.
DR   RefSeq; NP_001097687.1; NM_001104217.2.
DR   RefSeq; NP_524235.2; NM_079511.5.
DR   AlphaFoldDB; Q9VNB5; -.
DR   SMR; Q9VNB5; -.
DR   BioGRID; 65859; 71.
DR   DIP; DIP-29174N; -.
DR   IntAct; Q9VNB5; 2.
DR   STRING; 7227.FBpp0112105; -.
DR   TCDB; 1.A.69.1.1; the heteromeric odorant receptor channel (horc) family.
DR   GlyGen; Q9VNB5; 2 sites.
DR   iPTMnet; Q9VNB5; -.
DR   PaxDb; Q9VNB5; -.
DR   DNASU; 40650; -.
DR   EnsemblMetazoa; FBtr0078794; FBpp0078438; FBgn0037324.
DR   EnsemblMetazoa; FBtr0113193; FBpp0112105; FBgn0037324.
DR   GeneID; 40650; -.
DR   KEGG; dme:Dmel_CG10609; -.
DR   UCSC; CG10609-RB; d. melanogaster.
DR   CTD; 40650; -.
DR   FlyBase; FBgn0037324; Orco.
DR   VEuPathDB; VectorBase:FBgn0037324; -.
DR   eggNOG; ENOG502QR02; Eukaryota.
DR   HOGENOM; CLU_045605_0_0_1; -.
DR   InParanoid; Q9VNB5; -.
DR   OMA; QIYYVLF; -.
DR   OrthoDB; 588157at2759; -.
DR   PhylomeDB; Q9VNB5; -.
DR   BioGRID-ORCS; 40650; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Orco; fly.
DR   GenomeRNAi; 40650; -.
DR   PRO; PR:Q9VNB5; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037324; Expressed in antenna and 5 other tissues.
DR   ExpressionAtlas; Q9VNB5; baseline and differential.
DR   Genevisible; Q9VNB5; DM.
DR   GO; GO:0005929; C:cilium; IDA:FlyBase.
DR   GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR   GO; GO:0032590; C:dendrite membrane; ISS:FlyBase.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0015278; F:calcium-release channel activity; IDA:FlyBase.
DR   GO; GO:0005516; F:calmodulin binding; IMP:FlyBase.
DR   GO; GO:0005549; F:odorant binding; IPI:FlyBase.
DR   GO; GO:0004984; F:olfactory receptor activity; IDA:FlyBase.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR   GO; GO:0050911; P:detection of chemical stimulus involved in sensory perception of smell; IMP:FlyBase.
DR   GO; GO:0042048; P:olfactory behavior; IMP:FlyBase.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
DR   GO; GO:0019236; P:response to pheromone; IMP:FlyBase.
DR   GO; GO:0007608; P:sensory perception of smell; IDA:FlyBase.
DR   InterPro; IPR004117; 7tm6_olfct_rcpt.
DR   PANTHER; PTHR21137; PTHR21137; 1.
DR   Pfam; PF02949; 7tm_6; 1.
PE   1: Evidence at protein level;
KW   Behavior; Cell membrane; Glycoprotein; Membrane; Olfaction; Receptor;
KW   Reference proteome; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..486
FT                   /note="Odorant receptor coreceptor"
FT                   /id="PRO_0000174272"
FT   TOPO_DOM        1..47
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   TRANSMEM        48..68
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   TRANSMEM        76..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   TRANSMEM        136..156
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   TRANSMEM        192..212
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   TRANSMEM        352..372
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        373..390
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   TRANSMEM        391..411
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        412..462
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   TRANSMEM        463..483
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        484..486
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16402857"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18005664"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         143
FT                   /note="T -> I (in strain: Oregon-R)"
FT                   /evidence="ECO:0000269|PubMed:15339651"
FT   MUTAGEN         169
FT                   /note="N->NQ: Destroys glycosylation site."
FT                   /evidence="ECO:0000269|PubMed:18005664"
SQ   SEQUENCE   486 AA;  54413 MW;  8DD0ACDC3091B5D6 CRC64;
     MTTSMQPSKY TGLVADLMPN IRAMKYSGLF MHNFTGGSAF MKKVYSSVHL VFLLMQFTFI
     LVNMALNAEE VNELSGNTIT TLFFTHCITK FIYLAVNQKN FYRTLNIWNQ VNTHPLFAES
     DARYHSIALA KMRKLFFLVM LTTVASATAW TTITFFGDSV KMVVDHETNS SIPVEIPRLP
     IKSFYPWNAS HGMFYMISFA FQIYYVLFSM IHSNLCDVMF CSWLIFACEQ LQHLKGIMKP
     LMELSASLDT YRPNSAALFR SLSANSKSEL IHNEEKDPGT DMDMSGIYSS KADWGAQFRA
     PSTLQSFGGN GGGGNGLVNG ANPNGLTKKQ EMMVRSAIKY WVERHKHVVR LVAAIGDTYG
     AALLLHMLTS TIKLTLLAYQ ATKINGVNVY AFTVVGYLGY ALAQVFHFCI FGNRLIEESS
     SVMEAAYSCH WYDGSEEAKT FVQIVCQQCQ KAMSISGAKF FTVSLDLFAS VLGAVVTYFM
     VLVQLK
 
 
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