CGLR_TRICA
ID CGLR_TRICA Reviewed; 398 AA.
AC D6WI29;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Cyclic GMP-AMP synthase-like receptor {ECO:0000305};
DE Short=Tc-cGLR {ECO:0000303|PubMed:34261127};
DE Short=cGLR {ECO:0000303|PubMed:34261127};
DE EC=2.7.7.86 {ECO:0000269|PubMed:34261127};
GN ORFNames=TcasGA2_TC003965 {ECO:0000312|EMBL:EFA01049.1};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2;
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2;
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-398 IN COMPLEX WITH MANGANESE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=34261127; DOI=10.1038/s41586-021-03743-5;
RA Slavik K.M., Morehouse B.R., Ragucci A.E., Zhou W., Ai X., Chen Y., Li L.,
RA Wei Z., Baehre H., Koenig M., Seifert R., Lee A.S.Y., Cai H., Imler J.L.,
RA Kranzusch P.J.;
RT "cGAS-like receptors sense RNA and control 3'2'-cGAMP signaling in
RT Drosophila.";
RL Nature 597:109-113(2021).
CC -!- FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic
CC GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate
CC immunity (PubMed:34261127). Acts as a key sensor of double-stranded RNA
CC (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal
CC that triggers the immune responses (PubMed:34261127). Directly binds
CC dsRNA, activating the nucleotidyltransferase activity, leading to
CC synthesis of 2',3'-cGAMP, a second messenger that binds to and
CC activates Sting, thereby triggering the antiviral immune response via
CC activation of the NF-kappa-B transcription factor Rel (Relish) (By
CC similarity). {ECO:0000250|UniProtKB:A1ZA55,
CC ECO:0000269|PubMed:34261127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = 2',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:42064,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:143093; EC=2.7.7.86;
CC Evidence={ECO:0000269|PubMed:34261127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42065;
CC Evidence={ECO:0000269|PubMed:34261127};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:34261127};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:34261127};
CC -!- ACTIVITY REGULATION: The enzyme activity is specifically activated by
CC double-stranded RNA (dsRNA). {ECO:0000269|PubMed:34261127}.
CC -!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
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DR EMBL; KQ971334; EFA01049.1; -; Genomic_DNA.
DR RefSeq; XP_969398.1; XM_964305.3.
DR PDB; 7LT2; X-ray; 1.58 A; A=1-398.
DR PDBsum; 7LT2; -.
DR SMR; D6WI29; -.
DR EnsemblMetazoa; TC003965_001; TC003965_001; TC003965.
DR GeneID; 657875; -.
DR KEGG; tca:657875; -.
DR eggNOG; ENOG502S61H; Eukaryota.
DR HOGENOM; CLU_053219_0_0_1; -.
DR InParanoid; D6WI29; -.
DR OMA; DGHYINR; -.
DR OrthoDB; 759341at2759; -.
DR PhylomeDB; D6WI29; -.
DR Proteomes; UP000007266; Linkage group 3.
DR GO; GO:0140700; F:3',2'-cyclic GMP-AMP synthase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:1902615; P:immune response involved in response to exogenous dsRNA; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR024810; Mab-21_dom.
DR Pfam; PF03281; Mab-21; 1.
DR SMART; SM01265; Mab-21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; GTP-binding; Immunity;
KW Innate immunity; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..398
FT /note="Cyclic GMP-AMP synthase-like receptor"
FT /id="PRO_0000454448"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 69..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 240..247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 244..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 277..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8N884"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:34261127,
FT ECO:0007744|PDB:7LT2"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:34261127,
FT ECO:0007744|PDB:7LT2"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:34261127,
FT ECO:0007744|PDB:7LT2"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 17..41
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:7LT2"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:7LT2"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 187..199
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:7LT2"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:7LT2"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 300..317
FT /evidence="ECO:0007829|PDB:7LT2"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 336..353
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:7LT2"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:7LT2"
SQ SEQUENCE 398 AA; 46190 MW; 0B8219E6FE5FB256 CRC64;
MENILNDINK RFISLPEEDV RGNKQILESV LRTFVEQMKT QDPLFKALFR RVFYGGSFYD
GLKVGKPEEF DLDILLHIPI YAQPVLNESN VPGFVWLKLN NLDGWLRQPE GRVYKDFRKK
FLADNDFLDT GKTLRWMESL VQKTLNTLPW VNNATCELTN EFGTFHINWW KGGPAMTLGI
SHSSGEKIMD VDLVACFVFS GDKWPINGYR SNPFPSTKPE FFIVPKKPQG PVNPQGRYWS
LSFQEQERVL IDNKNRLKPA VKLIKKLKEK THPNIASYYI KTVFLHIIEQ KDQSFWNKSL
REVFMTTLRE YNEFIADQSI PYYWCRKNNL IGHLAPITLN NISNRIGYII KDIENNPENI
AKHLLTKEEY TKYIQGEDVM AEALPALPAS QTSSCVII
