IR21A_DROME
ID IR21A_DROME Reviewed; 842 AA.
AC Q9VPI2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ionotropic receptor 21a {ECO:0000312|EMBL:AAF51569.2};
DE Flags: Precursor;
GN Name=Ir21a {ECO:0000312|FlyBase:FBgn0031209};
GN ORFNames=CG2657 {ECO:0000312|FlyBase:FBgn0031209};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=19135896; DOI=10.1016/j.cell.2008.12.001;
RA Benton R., Vannice K.S., Gomez-Diaz C., Vosshall L.B.;
RT "Variant ionotropic glutamate receptors as chemosensory receptors in
RT Drosophila.";
RL Cell 136:149-162(2009).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27126188; DOI=10.7554/elife.13254;
RA Ni L., Klein M., Svec K.V., Budelli G., Chang E.C., Ferrer A.J., Benton R.,
RA Samuel A.D., Garrity P.A.;
RT "The ionotropic receptors IR21a and IR25a mediate cool sensing in
RT Drosophila.";
RL Elife 5:0-0(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27656904; DOI=10.7554/elife.17879;
RA Knecht Z.A., Silbering A.F., Ni L., Klein M., Budelli G., Bell R.,
RA Abuin L., Ferrer A.J., Samuel A.D., Benton R., Garrity P.A.;
RT "Distinct combinations of variant ionotropic glutamate receptors mediate
RT thermosensation and hygrosensation in Drosophila.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Integral part of a neural sensory system in the antenna that
CC provides the neural basis for the response to environmental changes in
CC temperature (thermosensation) (PubMed:27126188, PubMed:27656904).
CC Together with Ir25a and Ir93a, mediates the response of the dorsal
CC organ cool cells, a trio of cool-responsive neurons, to cooling and is
CC required for cool avoidance behavior (PubMed:27126188,
CC PubMed:27656904). {ECO:0000269|PubMed:27126188,
CC ECO:0000269|PubMed:27656904}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal organ cool cells
CC (PubMed:27126188). In the antenna, expressed in approximately six
CC neurons in the arista as well as five to ten neurons near the third
CC chamber of the sacculus (PubMed:19135896).
CC {ECO:0000269|PubMed:19135896, ECO:0000269|PubMed:27126188}.
CC -!- DISRUPTION PHENOTYPE: Strong disruption of larval thermotaxis when
CC exposed to a thermal gradient ranging from 13.5 to 21.5 degrees Celsius
CC with mutants unable to navigate away from cooler temperatures and
CC toward warmer temperatures (PubMed:27126188). Reduced response of
CC dorsal organ cool cells to cooling (PubMed:27126188, PubMed:27656904).
CC No effect on humidity preference (PubMed:27656904).
CC {ECO:0000269|PubMed:27126188, ECO:0000269|PubMed:27656904}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; AE014134; AAF51569.2; -; Genomic_DNA.
DR RefSeq; NP_001097043.1; NM_001103573.2.
DR AlphaFoldDB; Q9VPI2; -.
DR STRING; 7227.FBpp0111921; -.
DR TCDB; 1.A.10.1.26; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q9VPI2; 8 sites.
DR PaxDb; Q9VPI2; -.
DR EnsemblMetazoa; FBtr0113008; FBpp0111921; FBgn0031209.
DR GeneID; 33157; -.
DR KEGG; dme:Dmel_CG2657; -.
DR UCSC; CG2657-RB; d. melanogaster.
DR CTD; 33157; -.
DR FlyBase; FBgn0031209; Ir21a.
DR VEuPathDB; VectorBase:FBgn0031209; -.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_012744_1_0_1; -.
DR InParanoid; Q9VPI2; -.
DR OMA; PPYIFRI; -.
DR OrthoDB; 460569at2759; -.
DR PhylomeDB; Q9VPI2; -.
DR Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR Reactome; R-DME-399710; Activation of AMPA receptors.
DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-DME-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 33157; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33157; -.
DR PRO; PR:Q9VPI2; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031209; Expressed in adult sense organ (Drosophila) and 10 other tissues.
DR Genevisible; Q9VPI2; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISM:FlyBase.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0050907; P:detection of chemical stimulus involved in sensory perception; IEP:FlyBase.
DR InterPro; IPR001320; Iontro_rcpt.
DR Pfam; PF00060; Lig_chan; 1.
PE 2: Evidence at transcript level;
KW Behavior; Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..842
FT /note="Ionotropic receptor 21a"
FT /id="PRO_5004338393"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 722..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 842 AA; 95565 MW; 19BA304DEE4F8B2C CRC64;
MSYYWVALVL FTAQAFSIEG DRSASYQEKC ISRRLINHYQ LNKEIFGVGM CDGNNENEFR
QKRRIVPTFQ GNPRPRGELL ASKFHVNSYN FEQTNSLVGL VNKIAQEYLN KCPPVIYYDS
FVEKSDGLIL ENLFKTIPIT FYHGEINADY EAKNKRFTSH IDCNCKSYIL FLSDPLMTRK
ILGPQTESRV VLVSRSTQWR LRDFLSSELS SNIVNLLVIG ESLMADPMRE RPYVLYTHKL
YADGLGSNTP VVLTSWIKGA LSRPHINLFP SKFQFGFAGH RFQISAANQP PFIFRIRTLD
SSGMGQLRWD GVEFRLLTMI SKRLNFSIDI TETPTRSNTR GVVDTIQEQI IERTVDIGMS
GIYITQERLM DSAMSVGHSP DCAAFITLAS KALPKYRAIM GPFQWPVWVA LICVYLGGIF
PIVFTDRLTL SHLMGNWGEV ENMFWYVFGM FTNAFSFTGK YSWSNTRKNS TRLLIGAYWL
FTIIITSCYT GSIIAFVTLP AFPDTVDSVL DLLGLFFRVG TLNNGGWETW FQNSTHIPTS
RLYKKMEFVG SVDEGIGNVT QSFFWNYAFL GSKAQLEYLV QSNFSDENIS RRSALHLSEE
CFALFQIGFL FPRESVYKIK IDSMILLAQQ SGLIAKINNE VSWVMQRSSS GRLLQASSSN
SLREIIQEER QLTTADTEGM FLLMALGYFL GATALVSEIV GGITNKCRQI IKRSRKSAAS
SWSSASSGSM LRTNAEQLSH DKRKANRREA AEVAQKMSFG MRELNLTRAT LREIYGSYGA
PETDHGQLDI VHTEFPNSSA KLNNIEDEES REALESLQRL DEFMDQMDND GNPSSHTFRI
DN
