ACXE_DROME
ID ACXE_DROME Reviewed; 1123 AA.
AC Q9VK50; F3YDG3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Adenylyl cyclase X E {ECO:0000312|FlyBase:FBgn0040506};
DE EC=4.6.1.1 {ECO:0000250|UniProtKB:P40146};
GN Name=ACXE {ECO:0000312|FlyBase:FBgn0040506};
GN ORFNames=CG17178 {ECO:0000312|FlyBase:FBgn0040506};
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, AND DISRUPTION PHENOTYPE.
RX PubMed=19046378; DOI=10.1111/j.1460-9568.2008.06507.x;
RA Ueno K., Kidokoro Y.;
RT "Adenylyl cyclase encoded by AC78C participates in sugar perception in
RT Drosophila melanogaster.";
RL Eur. J. Neurosci. 28:1956-1966(2008).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP in
CC response to G-protein signaling. {ECO:0000250|UniProtKB:P26769}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000250|UniProtKB:P40146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in labella.
CC {ECO:0000269|PubMed:19046378}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in sugar gustatory
CC neurons does not affect sucrose response.
CC {ECO:0000269|PubMed:19046378}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEB72004.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53229.3; -; Genomic_DNA.
DR EMBL; BT126324; AEB72004.1; ALT_INIT; mRNA.
DR RefSeq; NP_652601.3; NM_144344.3.
DR AlphaFoldDB; Q9VK50; -.
DR SMR; Q9VK50; -.
DR STRING; 7227.FBpp0302693; -.
DR PaxDb; Q9VK50; -.
DR EnsemblMetazoa; FBtr0310556; FBpp0302693; FBgn0040506.
DR GeneID; 53426; -.
DR KEGG; dme:Dmel_CG17178; -.
DR UCSC; CG17178-RA; d. melanogaster.
DR CTD; 53426; -.
DR FlyBase; FBgn0040506; ACXE.
DR VEuPathDB; VectorBase:FBgn0040506; -.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000168344; -.
DR HOGENOM; CLU_001072_2_5_1; -.
DR InParanoid; Q9VK50; -.
DR OMA; IIYMIYM; -.
DR OrthoDB; 363718at2759; -.
DR PhylomeDB; Q9VK50; -.
DR Reactome; R-DME-163615; PKA activation.
DR Reactome; R-DME-170660; Adenylate cyclase activating pathway.
DR Reactome; R-DME-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-DME-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-DME-5610787; Hedgehog 'off' state.
DR BioGRID-ORCS; 53426; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ACXE; fly.
DR GenomeRNAi; 53426; -.
DR PRO; PR:Q9VK50; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0040506; Expressed in embryonic/larval hemocyte (Drosophila) and 5 other tissues.
DR ExpressionAtlas; Q9VK50; baseline and differential.
DR Genevisible; Q9VK50; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; ISM:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006171; P:cAMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1123
FT /note="Adenylyl cyclase X E"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445434"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..73
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..137
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..196
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..608
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..719
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..772
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..1123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 346..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 903
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1014..1016
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1021..1025
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1061
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
SQ SEQUENCE 1123 AA; 128918 MW; D0DEC66707486D60 CRC64;
MPRSLGNCQL NYSKERMWEP GYLKAKCAEL RLESEFRLYR IRLWKSYLLT FFMLHIFVTS
VHCALLLATI ERRSIIYFDV ALSIGCALVL ILVLSVNFCD EFIAKHTWYM YASSIFASLT
LVFADLTESI YHTYAHSWIL GTFYDTYIIY MIYMFLPIHF ISGAVLLALL VSGLYILYFV
IFIAQGFAQF ASALFSVGGM SVDIVHYLCL NLVGIFYRVM NDTVVRSSFL DRHQYIKEKI
WLRNARLQEK QLLDSILPPQ ISLPLQKDIQ GRIVMAKQGI HSWTAMERTM AIQIHPDVSI
LYADVVNYTH LTTTLTVEML VKVLHDLYGR FDLAAYRYKV QRIKFLGDCY YCVAGLSDPD
PDHANNCVIL GLSMINHIME VRDIHGLDIN MRIGVHSGNL FAGVIGEAKL QFDIWGLDVT
IANVLESTGV PGCVHISGAT LNNLDVNRFD IEDGPEEARD HPLLKKYRIR SYIIRQDLHM
DDEDSDEFLG DLHSISLCNM GAQPRISDSA NQSLRALFHE ELREEFRKMP VSAFSPKRLL
GICRFNTGKE VPAHQNLNIC LTFTDPILER AYLKQTDYMY KYSIILSASV GCSLVYIELM
DTQMICSSCF VLPASVATIQ CILALIAWYK KYCWTRYGRN NVPHHYNGFS CFIFRIHDKI
LNSLPIRICI YLFLMISSFF VMCLIVMSCQ REEFEMAYIE ERLFHYEQEA HICFHPWVTT
NMLSLMICLT FTFAHIPIMV KTAVAILETL AYLLLIFFQF DFVFHHSVTT NPYFKSEYAH
ALLICITFLI MFVKERQIEF TNKVNFNWRV DLRKEENAAS LTNHSIIIIL NNILPSHIVD
VYLNSLAKHE LYFENYRMVS VMFAMLINFE MDLRSLRVLN EIIAEFDTLL LFYKEYYTVE
KIKIVGCTYM AACGLDLNFA GSTSTNRKES IPPTEFNEEQ SRRILFQQSN EDLDEVVFVM
TSYALDMMRT LAKSNEAYQS IAGDRNITDG TIAIGISSGE VMAGIVGASQ PHYDIWGNPV
NMASRMESTG LPGHIHVTEE TSEILQQFGI TCSYRGMTFV KGRGKIPTYL VGIDENLNFI
PQKATRFPSH QERSTVISLQ STYTHAENNN SIASTSRHTL QSL
