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Database: UniProt
Entry: A0A139WLU5_TRICA
LinkDB: A0A139WLU5_TRICA
Original site: A0A139WLU5_TRICA 
ID   A0A139WLU5_TRICA        Unreviewed;       831 AA.
AC   A0A139WLU5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   Name=AUGUSTUS-3.0.2_32341 {ECO:0000313|EMBL:KYB28876.1};
GN   ORFNames=TcasGA2_TC032341 {ECO:0000313|EMBL:KYB28876.1};
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 {ECO:0000313|EMBL:KYB28876.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB28876.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB28876.1,
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:KYB28876.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB28876.1,
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|RuleBase:RU363067};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000256|RuleBase:RU363067}.
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DR   EMBL; KQ971319; KYB28876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139WLU5; -.
DR   STRING; 7070.A0A139WLU5; -.
DR   EnsemblMetazoa; TC032341_003; TC032341_003; TC032341.
DR   InParanoid; A0A139WLU5; -.
DR   OMA; MHHLKYN; -.
DR   Proteomes; UP000007266; Linkage group 3.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR623088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN          21..342
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          336..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         97..101
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         138
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         246
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         297
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   831 AA;  93377 MW;  8257DEE6558B09F2 CRC64;
     MHKRRRKKLA TRSLSQDHAI LDDIHHGLVQ RILDRVGLWG FNAFTLETVA GGRALPVLCV
     HLFHWYGLLD YFQLDVVRVW KLFTLIEEGY HSTNPYHNSI HATDVTQAMH CFLQEEKIRK
     HLSELEIMAA LIGAVAHDLD HPGVNQHFLI STSNHLAILY QNTSVLENHH WRSAVGCLLE
     SGVAEQLLPH RSKLELQIRD LILATDINRQ NEFLTKFKAY LDEGSLDLTK TTDRHFILQI
     ALKCADISNP TRPWDISHKW SLKVCDEFFR QGEFERKLNL PVTSICDQQS TSVAKIQVGF
     FRYVVKPLFS EWHRFLKSTL STHMMEILEA NRKRWEKQES AEQAEETQTE LSDAEPDVSD
     DEEATKQSSE TPSIMDFIPP PRREIRRQSL AVPTLEHTLG VRRHSVPVNM EPSLPRTIYR
     RESLPTGRAA SSGRSPVSPV QNESRTSSGL REEDELMKFG SQSSIISSTS PHLSSGAEDQ
     PERPLSAENL LPEPSIASMT SSAAASRLSS VLQGNSVAPP SKCLTRQQTF PPPQPYVRMR
     YMSATVEMST CTETVHEGES RSNSSHGSHE NISNVPHYTI PAIAVLSPNN SRSPDFLIPE
     VPHKSSLAGK REQEANSDKE KVCKMVKLSD PGQRYEKENV DPRRLTTTSL ARRRGSAPVS
     LPLSGPDDSV SSAGGGLCLS ETQTLRRGSV PIEIAHYLYT ASDSYTDENL EQVINITPVE
     TTRSFWQYQR RGSAPIDLPP AGGERREQLT RHTSLNGKSG RRKKQLRRRS SGGPETVCLP
     ESSHSEGCSR LLLRRPENPD ALLARRRGSL PIEVLTVGHS GKNIQPVFFY C
//
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