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Database: UniProt
Entry: D2A1R3_TRICA
LinkDB: D2A1R3_TRICA
Original site: D2A1R3_TRICA 
ID   D2A1R3_TRICA            Unreviewed;      1086 AA.
AC   D2A1R3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   Name=AUGUSTUS-3.0.2_07759 {ECO:0000313|EMBL:EFA02113.2};
GN   ORFNames=TcasGA2_TC007759 {ECO:0000313|EMBL:EFA02113.2};
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:EFA02113.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA02113.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02113.2,
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:EFA02113.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02113.2,
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=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000798,
CC         ECO:0000256|PIRNR:PIRNR009376};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR   EMBL; KQ971338; EFA02113.2; -; Genomic_DNA.
DR   AlphaFoldDB; D2A1R3; -.
DR   STRING; 7070.D2A1R3; -.
DR   EnsemblMetazoa; TC007759_001; TC007759_001; TC007759.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_000690_2_0_1; -.
DR   InParanoid; D2A1R3; -.
DR   OMA; VRHPHRE; -.
DR   Proteomes; UP000007266; Linkage group 4.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd01254; PH_PLD; 1.
DR   CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR   CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR   CDD; cd06895; PX_PLD; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   Pfam; PF00787; PX; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50035; PLD; 2.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          95..214
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          477..504
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          899..926
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1086 AA;  123749 MW;  16E2DFCABD50E418 CRC64;
     MSTENIIRME EEESGECNNE LSLTRPSLGG SEYDDELGIP ESLIIVDVGD GPVVIEHSDE
     EIEDDVFDGL PFSSIHKPPI KFKSFRRNVF IPSLDISVTI KDYERNLTTH MLNPNLYTIS
     LVHGTFNWQI KKRYKQIQHL HQQLILFRAG LNIPFPSKTH KRKRKSFKMN ILVPYEKLCD
     RIKQLENYLN NLLSINIYRN HPATIEFLEV SHLSFVQGLG IKGKEGVVKK RTGSTQPGQA
     GCNCCGLIRC MFCIRCQHLC KDILCARWNE RWFFIKDTCF GYINPDDGMI KCVILFDQGF
     EVASGLYSIG LQTGFQIQTL SRQIAFKCWT RRKSREWVEA LKEVASGTAR EFTQANQHRS
     FAPLRTTIAA CWFVDGASYM SAVADAIENA KEEVFITDWW LSPEIYMKRP AISGDYWRLD
     KLLQRKAASG VRIFVLLYKE VELALGLNSY YSKQTLAELS ENIKVLRHPD HARVGVFLWA
     HHEKMVVVDQ SYAFVGGIDL CYGRWDDAKH RLTDLGSITP SIDVSTLKKK TSSVPGGDAI
     YPIPIPIYKQ TPIPVVTEPE APEPCPLPQL EPGDTLLIPT VKLKCNTPDM ERKNVIDTIK
     NTVKTKGKDL ISLVYTPHED SVEKTEEEKK PQTQDEFLET LNGSSKLWVG KDYVNFIVKD
     FNNLDSPFDD FIDRVTTPRM PWHDVGVCVQ GAAARDVSRH FIQRWNATKL EKAKSNKCYP
     YLLPKSYDDF KTLPIVFPNE VSNVSCQVLR SVSTWSCGFL EPDTVEQSIH EAYIDTINKA
     QHYIYIENQF FISLPYTNPN TRNQIAEALY KRIVRAFKAK EVFRVFVVMP LLPGFEGEVG
     GPTGTSLHAI THWNYCSISQ GKDAILSRLQ EAGIEDPSDF ISFYGLRNHA TLNCEPITEL
     IYVHSKLMIV DDKTVICGSA NINDRSLIGK RDSEIAVLIE DEAFDDGVMN GKKFPCGKFA
     GGLRKYLFKE HLGLLGKEHE MIDFDITDPI SDYFYKEVWY KTASLNTEFY EKVFHCIPTD
     RVKNFADLKK NQEEKPLYSN EISRAEKMLE SIQGHLVLLP LHFLSQESLT PAASSVEGMM
     PTSLWT
//
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