ID D2A2A1_TRICA Unreviewed; 1400 AA.
AC D2A2A1;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN Name=GLEAN_07814 {ECO:0000313|EMBL:EFA02161.2};
GN ORFNames=TcasGA2_TC007814 {ECO:0000313|EMBL:EFA02161.2};
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 {ECO:0000313|EMBL:EFA02161.2, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA02161.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02161.2,
RC ECO:0000313|Proteomes:UP000007266};
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] {ECO:0000313|EMBL:EFA02161.2, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02161.2,
RC ECO:0000313|Proteomes:UP000007266};
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).
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:0000256|ARBA:ARBA00001593};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; KQ971338; EFA02161.2; -; Genomic_DNA.
DR RefSeq; XP_008191695.1; XM_008193473.2.
DR RefSeq; XP_015834366.1; XM_015978880.1.
DR STRING; 7070.D2A2A1; -.
DR EnsemblMetazoa; TC007814_001; TC007814_001; TC007814.
DR GeneID; 663450; -.
DR KEGG; tca:663450; -.
DR eggNOG; KOG3618; Eukaryota.
DR HOGENOM; CLU_001072_12_1_1; -.
DR InParanoid; D2A2A1; -.
DR OMA; FTAMPPG; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000007266; Linkage group 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
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:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF8; ADENYLATE CYCLASE TYPE 9; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 944..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 970..989
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1010..1029
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1041..1058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1070..1091
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..468
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1206..1346
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 159882 MW; 14C5883A0B8FEA6A CRC64;
MTEKRPSSVS YKSEQPSDDE NAQLSLDPQT QLYLAHLSQQ NGCWGRFFPI PFERAAQKSW
WDPTFDSEIL EEQYRRSSNP HSRFKFRYAL WYMLLISSSW LVYFLVTGLV SETHHWPMLC
TVLGTLILSV TTVLFLTYTD IYNNHMLLMS LIVAFVLCVI SLSFVVLVPM KTDPLSFPIT
SDISPVGHFS ICIEILMLIY TLIPLKLYMS ITIGFLYSAA FETLTISLQN QSLEASTITV
RLLSHFCIHV IGLHILIMTN VRMRNTFMKV GQSLLVRRQL ESEKKLKENM IHSLMPSSVA
EWLLSEEETF TRSDQRNSDP ETNDIRSLFR PFNMNRMENV SILFADIVGF TKMASKKSAE
ELVEILNNLF QRFDHLCKFH NCEKISTLGD CYYCVSGCPE PRHDHAKCCV EMGLSMIQAI
KQFDQEKNEG VNMRVGVHTG TVLCGIVGTR RFKFDVWSND VTLANRMEST GKPGMVHVSE
KTCEFLQDMY LLEEGEPVLG MKTYFILGRT GDKTPSYSGS FRAEGRQKYT NSLQLFVSPP
TSSPSMSPQS RPRVLSCDTT HIKATHNPNM LSPDVCKIKA SSLPSILDSE NEQDGGDICK
ETSDCDNIKT PTSTASSGKY SVKLKNWKMP KFLRKNDGKP ELDIEVPANS EDRISGGYQQ
VPTIIETSNV SNGKKKDSFI SVTDVDDDNK RSSIFLDDPK DTIDVKSYIS QSRSDIGQYD
YSPGDLNQFM RTGSYRSQYG RSPNEFSFLQ RAGSNRSRRG RSPNFDVFPG ERQRSTTVCV
GNLERPKMSL EVPGRLTNIS VLDDHFSVYS RKDSGIRSNS RRSSIQQLEQ ATHPNSEHRV
SGYYTSSQST VTSPQYNVRM PGVFKDKFGT CIQNLRKQSD RQLIKCVQEN SKSRGSYFIK
PPLRRLTLFF KDKQMEQDYR TNVHSLFEKA DSILTLADSK FNTYFDVCVS SLVFAIVSIS
LWLLYGHTTL WLVMSGVFVA IQACGWALCS RKVVECSDRC LRCVSRFYRW NMFGAVLVSL
PLVTVLINFC TKVFTTSETS NYLYTYLLFV GVIHFCNFTQ LNCWMKNCLA VAFTLIFIPL
FLNGTCSNFF VEKSERTELN PIVAILDDRN RTEVKSLSLE HYSFLYKSEI LMDLFLLLVL
VWLLNREFEI GYRLSFHANY VSNRDKINVQ NLKTQADYLI YNIVPEHVAE QLKKNAKYSE
NFKDVGIIFA SIVNFNEMYD ESYLGGKEYL RVLNELIADF DELLDRPEFA SVEKIKTIGS
TFMAASGLNS TTRRNQKDPN EHLYALMDFA LEMQNVITDF NRDLLEFNLI LRIGYNFGEV
TAAVIGNTKL YYDIWGDAVN IASRMDSTGV NGCIQIGENC LQVLETRYVF RPRGSVYVKG
KDNMSVYLLE RKKTDDEIEA
//
