TRPA1_DROME
ID TRPA1_DROME Reviewed; 1197 AA.
AC Q7Z020; A8JNP0; Q9VSQ9;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Transient receptor potential cation channel subfamily A member 1;
DE Short=dTRPA1;
DE AltName: Full=Ankyrin-like with transmembrane domains protein 1;
DE Short=dANKTM1;
GN Name=TrpA1; Synonyms=Anktm1; ORFNames=CG5751;
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] (ISOFORM I), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12815418; DOI=10.1038/423822a;
RA Viswanath V., Story G.M., Peier A.M., Petrus M.J., Lee V.M., Hwang S.W.,
RA Patapoutian A., Jegla T.;
RT "Ion channels: opposite thermosensor in fruitfly and mouse.";
RL Nature 423:822-823(2003).
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, AND ALTERNATIVE SPLICING.
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, AND DISRUPTION PHENOTYPE.
RX PubMed=15681611; DOI=10.1101/gad.1278205;
RA Rosenzweig M., Brennan K.M., Tayler T.D., Phelps P.O., Patapoutian A.,
RA Garrity P.A.;
RT "The Drosophila ortholog of vertebrate TRPA1 regulates thermotaxis.";
RL Genes Dev. 19:419-424(2005).
CC -!- FUNCTION: Essential for thermotaxis by sensing environmental
CC temperature. Receptor-activated non-selective cation channel involved
CC in detection of sensations such as temperature. Involved in heat
CC nociception by being activated by warm temperature of about 24-29
CC degrees Celsius. {ECO:0000269|PubMed:12815418,
CC ECO:0000269|PubMed:15681611}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O75762}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12815418};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=I;
CC IsoId=Q7Z020-4; Sequence=Displayed;
CC Name=J;
CC IsoId=Q7Z020-5; Sequence=VSP_030263;
CC -!- DISRUPTION PHENOTYPE: Eliminates avoidance of elevated temperatures
CC along a thermal gradient. {ECO:0000269|PubMed:15681611}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The power behind pain
CC - Issue 82 of May 2007;
CC URL="https://web.expasy.org/spotlight/back_issues/082";
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DR EMBL; AY302598; AAP76197.1; -; mRNA.
DR EMBL; AE014296; AAF50356.5; -; Genomic_DNA.
DR EMBL; AE014296; ABW08500.4; -; Genomic_DNA.
DR RefSeq; NP_001097554.4; NM_001104084.4. [Q7Z020-5]
DR RefSeq; NP_648263.5; NM_140006.5. [Q7Z020-4]
DR AlphaFoldDB; Q7Z020; -.
DR SMR; Q7Z020; -.
DR BioGRID; 64420; 23.
DR IntAct; Q7Z020; 5.
DR STRING; 7227.FBpp0304207; -.
DR TCDB; 1.A.4.6.2; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q7Z020; 3 sites.
DR PaxDb; Q7Z020; -.
DR PRIDE; Q7Z020; -.
DR EnsemblMetazoa; FBtr0331825; FBpp0304209; FBgn0035934. [Q7Z020-4]
DR EnsemblMetazoa; FBtr0331826; FBpp0304210; FBgn0035934. [Q7Z020-5]
DR GeneID; 39015; -.
DR KEGG; dme:Dmel_CG5751; -.
DR CTD; 8989; -.
DR FlyBase; FBgn0035934; TrpA1.
DR VEuPathDB; VectorBase:FBgn0035934; -.
DR eggNOG; KOG0510; Eukaryota.
DR eggNOG; KOG1326; Eukaryota.
DR GeneTree; ENSGT00940000156118; -.
DR InParanoid; Q7Z020; -.
DR OMA; HWATEKN; -.
DR Reactome; R-DME-3295583; TRP channels.
DR BioGRID-ORCS; 39015; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39015; -.
DR PRO; PR:Q7Z020; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035934; Expressed in adult hindgut (Drosophila) and 6 other tissues.
DR ExpressionAtlas; Q7Z020; baseline and differential.
DR Genevisible; Q7Z020; DM.
DR GO; GO:0034703; C:cation channel complex; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IDA:FlyBase.
DR GO; GO:0005261; F:cation channel activity; IDA:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IDA:FlyBase.
DR GO; GO:0097604; F:temperature-gated cation channel activity; IDA:FlyBase.
DR GO; GO:0006816; P:calcium ion transport; IDA:FlyBase.
DR GO; GO:0006812; P:cation transport; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:FlyBase.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IMP:FlyBase.
DR GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; IMP:FlyBase.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IDA:FlyBase.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; IDA:FlyBase.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:FlyBase.
DR GO; GO:0046957; P:negative phototaxis; IMP:FlyBase.
DR GO; GO:0023041; P:neuronal signal transduction; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IDA:FlyBase.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR GO; GO:0010378; P:temperature compensation of the circadian clock; IMP:FlyBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 15.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 10.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; Repeat; Sensory transduction;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1197
FT /note="Transient receptor potential cation channel
FT subfamily A member 1"
FT /id="PRO_0000215373"
FT TOPO_DOM 1..753
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..774
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..827
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 828..848
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 849..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..889
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 911..932
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 933..953
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 954..968
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 969..989
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:O75762"
FT TOPO_DOM 990..1004
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1005..1025
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1026..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 89..118
FT /note="ANK 1"
FT REPEAT 122..151
FT /note="ANK 2"
FT REPEAT 155..184
FT /note="ANK 3"
FT REPEAT 190..219
FT /note="ANK 4"
FT REPEAT 224..253
FT /note="ANK 5"
FT REPEAT 265..294
FT /note="ANK 6"
FT REPEAT 298..327
FT /note="ANK 7"
FT REPEAT 336..365
FT /note="ANK 8"
FT REPEAT 369..398
FT /note="ANK 9"
FT REPEAT 443..472
FT /note="ANK 10"
FT REPEAT 476..505
FT /note="ANK 11"
FT REPEAT 512..541
FT /note="ANK 12"
FT REPEAT 544..574
FT /note="ANK 13"
FT REPEAT 578..607
FT /note="ANK 14"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 690..720
FT /note="AFLQCPFMFAKIDEKTGESITTASPIPLPAL -> WPYQKTPEQIEAKRKEF
FT NDPKWRPAPLAVV (in isoform J)"
FT /evidence="ECO:0000305"
FT /id="VSP_030263"
SQ SEQUENCE 1197 AA; 135158 MW; 0A0866232733B69B CRC64;
MTSGDKETPK REDFASALRF LMGGCAREPE MTAMAPLNLP KKWARILRMS STPKIPIVDY
LEAAESGNLD DFKRLFMADN SRIALKDAKG RTAAHQAAAR NRVNILRYIR DQNGDFNAKD
NAGNTPLHIA VESDAYDALD YLLSIPVDTG VLNEKKQAPV HLATELNKVK SLRVMGQYRN
VIDIQQGGEH GRTALHLAAI YDHEECARIL ITEFDACPRK PCNNGYYPIH EAAKNASSKT
MEVFFQWGEQ RGCTREEMIS FYDSEGNVPL HSAVHGGDIK AVELCLKSGA KISTQQHDLS
TPVHLACAQG AIDIVKLMFE MQPMEKRLCL SCTDVQKMTP LHCASMFDHP DIVSYLVAEG
ADINALDKEH RSPLLLAASR SGWKTVHLLI RLGACISVKD AAARNVLHFV IMNGGRLTDF
AEQVANCQTQ AQLKLLLNEK DSMGCSPLHY ASRDGHIRSL ENLIRLGACI NLKNNNNESP
LHFAARYGRY NTVRQLLDSE KGSFIINESD GAGMTPLHIS SQQGHTRVVQ LLLNRGALLH
RDHTGRNPLQ LAAMSGYTET IELLHSVHSH LLDQVDKDGN TALHLATMEN KPHAISVLMS
MGCKLVYNVL DMSAIDYAIY YKYPEAALAM VTHEERANEV MALRSDKHPC VTLALIASMP
KVFEAVQDKC ITKANCKKDS KSFYIKYSFA FLQCPFMFAK IDEKTGESIT TASPIPLPAL
NTMVTHGRVE LLAHPLSQKY LQMKWNSYGK YFHLANLLIY SIFLVFVTIY SSLMMNNIEL
KAGDNKTMSQ YCNMGWEQLT MNLSQNPSVA SQIRLDSCEE RINRTTAILF CAVVIVVYIL
LNSMRELIQI YQQKLHYILE TVNLISWVLY ISALVMVTPA FQPDGGINTI HYSAASIAVF
LSWFRLLLFL QRFDQVGIYV VMFLEILQTL IKVLMVFSIL IIAFGLAFYI LLSKIIDPQP
NHLSFSNIPM SLLRTFSMML GELDFVGTYV NTYYRDQLKV PMTSFLILSV FMILMPILLM
NLLIGLAVGD IESVRRNAQL KRLAMQVVLH TELERKLPHV WLQRVDKMEL IEYPNETKCK
LGFCDFILRK WFSNPFTEDS SMDVISFDNN DDYINAELER QRRKLRDISR MLEQQHHLVR
LIVQKMEIKT EADDVDEGIS PNELRSVVGL RSAGGNRWNS PRVRNKLRAA LSFNKSM
