IR21A_ANOGA
ID IR21A_ANOGA Reviewed; 975 AA.
AC A0A1S4GYH6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Ionotropic receptor 21a {ECO:0000303|PubMed:32029627};
DE Flags: Precursor;
GN Name=Ir21a {ECO:0000303|PubMed:32029627};
GN ORFNames=AGAP008511 {ECO:0000312|EMBL:AAAB01008964};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000312|EMBL:AAAB01008964};
RN [1] {ECO:0000312|EMBL:AAAB01008964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|EMBL:AAAB01008964};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=32029627; DOI=10.1126/science.aay9847;
RA Greppi C., Laursen W.J., Budelli G., Chang E.C., Daniels A.M.,
RA van Giesen L., Smidler A.L., Catteruccia F., Garrity P.A.;
RT "Mosquito heat seeking is driven by an ancestral cooling receptor.";
RL Science 367:681-684(2020).
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:32029627). Specifically, required
CC for thermosensing by the cooling cell (PubMed:32029627). Plays a role
CC in heat seeking and heat-stimulated blood feeding behavior
CC (PubMed:32029627). {ECO:0000269|PubMed:32029627}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:32029627}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In both female and male antenna, expressed
CC specifically in 3 sensory neurons of flagellomere 13 segment (at
CC protein level). {ECO:0000269|PubMed:32029627}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAAB01008964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1S4GYH6; -.
DR VEuPathDB; VectorBase:AGAP008511; -.
DR OMA; PPYIFRI; -.
DR OrthoDB; 460569at2759; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR GO; GO:0050961; P:detection of temperature stimulus involved in sensory perception; IMP:UniProtKB.
DR GO; GO:0040040; P:thermosensory behavior; IMP:UniProtKB.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001320; Iontro_rcpt.
DR Pfam; PF00060; Lig_chan; 1.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
PE 1: Evidence at protein level;
KW Behavior; Cell membrane; Cell projection; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..975
FT /note="Ionotropic receptor 21a"
FT /evidence="ECO:0000255"
FT /id="PRO_5010273893"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 757..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 763
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 975 AA; 109617 MW; A35F2AB36394FC1C CRC64;
MFKRIVLAVI NLVFLIVSTT AFASLHYPES FNQQLIRYKG RDSSNGYFEL ASEAYYTGTY
DLVEELNETA TCLRADCREQ SNSSPVVRDR RRVDPTFYGH PKTREQIWER NFAHVIEDNR
QTLSLVTLLN KIILKYLHSC IPIVLFDTYV ATTENYMLEA LFSDFPITYI TGRIGPNYTL
DNPGILEPTG PQCRSYIIFL ADVMMTRKVI GPQMNSYVVL IPRSSQWKLQ EFLAAKQSRD
IINLLVIGES YSVDKRINNE QPYVLYTHEL YIDGLGANRP QVLTSWIGNK FSRNNVNLFP
RKLRKGFSGH RFTVKAAHQP PFMIKRLSTD GVGNVNIRWE GLEMRLLRVM AQYLNFTYDI
IEPGRTELGP GDAVVEEIKR GQGDMGLAGI YVTIERNLAT EMSVSHSTDC AAFLTLMSSA
LPRYRAILGP FQWPVWVAVI LIYLLAIFPL AFSDKMTLRH LLGNWSEIEN MFWYVFGTFT
NSLTFQGENS WSNTRKTSTR MLIGIYWVFT IIITACYTGS IIAFITLPVE PERIDGIEQL
SRGFFRVGTL DRGGWERWFL NSSHKQTNKL LKDLRFVSSV DEGIRNVTEA FLISYAFIGS
KGELEFLIKS NLSHQFENKR YGLHVSRECF ALYGVSMVFP PNSVHRDPIN NAILYMQEAG
LIGKLNRDVT WETMKTKDGR RKEASVGEVL RSTAPSERGL TLADTEGMFL LMLFGYVVAL
GVLISEWVGG CTNKCREVLK ERAERLKAAA AEIAAAATAG SDNGSLPVSS PTSTNRNSPH
KRTGPNGVEN SLPASGNGSA TVRRIRLTGE DSENEPNEYD VPPDAASDGG SSLQRHSLSE
CLSEVSAHTM QDLYNGPDRR HSTIVFLDGQ LMSEEEAQRK VARSKSRHRH SLSSVLEREV
SQLFRFLGKE SPHSARADES SDAGGLVRRG AGRERKEMKV AVEINARATE EGQQGPGAAV
GRRSIEATFG EKLLH
