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Database: UniProt
Entry: D2A1M1_TRICA
LinkDB: D2A1M1_TRICA
Original site: D2A1M1_TRICA 
ID   D2A1M1_TRICA            Unreviewed;      1127 AA.
AC   D2A1M1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Disheveled-associated activator of morphogenesis 1-like Protein {ECO:0000313|EMBL:EFA01522.1};
GN   Name=AUGUSTUS-3.0.2_07082 {ECO:0000313|EMBL:EFA01522.1};
GN   ORFNames=TcasGA2_TC007082 {ECO:0000313|EMBL:EFA01522.1};
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:EFA01522.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA01522.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01522.1,
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:EFA01522.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01522.1,
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).
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DR   EMBL; KQ971338; EFA01522.1; -; Genomic_DNA.
DR   RefSeq; XP_008192803.1; XM_008194581.2.
DR   AlphaFoldDB; D2A1M1; -.
DR   STRING; 7070.D2A1M1; -.
DR   EnsemblMetazoa; TC007082_001; TC007082_001; TC007082.
DR   GeneID; 658864; -.
DR   eggNOG; KOG1922; Eukaryota.
DR   HOGENOM; CLU_002356_1_0_1; -.
DR   InParanoid; D2A1M1; -.
DR   OMA; HSERTRF; -.
DR   OrthoDB; 5485896at2759; -.
DR   PhylomeDB; D2A1M1; -.
DR   Proteomes; UP000007266; Linkage group 4.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45725:SF1; DELPHILIN; 1.
DR   PANTHER; PTHR45725; FORMIN HOMOLOGY 2 FAMILY MEMBER; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN          84..457
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          636..1037
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1065..1097
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          488..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1015..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1087..1127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..629
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1127 AA;  128400 MW;  772352ED2C261B89 CRC64;
     MCSKEQITEI MDKIHMGLPK CSVKLPAWEN ITNALPRFHI PAMPAVRSKR GWCGCLQDDE
     PPEITYCVVE NTGTLTLQAI TPTQPMPSQE ELDAKFAELV EELDLTAPNK AAMLSLPSQK
     KWQIYCSRKG GEDTVDQTHA PEHYIERLRT LATLQYPEAN TEEEVRTRTK QIDGLKTALR
     TSTHSFVIKF IELDGLSALL DCLERMDYFT AQSSIHTSII GCVKALMNNS TGRAHVLAHP
     TSINTIAQSL STENIKTKIA ALEILGAVCL VSGGHKKVLD AMLHYQKYAF ERTRFQGIIN
     DLDRSTGIYR DEVNLKTAIM SFVNAVLNYG QGQENLEFRL HLRYEFLMLG IQPIIDKLRS
     HENETLDRHL DFFEMVRNED EKELARKFEL EHVDTKSATA MFDLIRRKLS HTAAYPHLLS
     LLEHCLLLPL DYGSHPQHWL LFDRIVQQIV LQQDNDVKNP DVSPIDINVK EIVHLLAKEE
     ELTEARKKAE ELERENTDMS NKLAKKEQEL DQRTQEKEDI ESSLVRIKER LEKETAAHIE
     TQQRLNELEY RAADLDRQVS CERGERFRLE RLVSSGSIPD DAKVQGLKST VDVEYKSPPP
     PPPLAPPPPP PAPGPPPPPN APMAPPPEPF KVETVKKNIP QPANPLKSFN WSKLPETKLA
     GTIWSELDDT KLYNTMELDC IDKLFSAYQK NGVTNDGSIE DLRQMGKNRT KVLSVIDSRR
     AQNCTILLSK LKMSDEDITK AILSMDCKEQ LPIDMVEQLL KFTPSSEEAA LLEEHSDEID
     SLARADRFLY EISKVPHYEQ RLRSLHYKKR FQVTLNEIIP RITSVMEASR EVSRSRRLRR
     LLEIVLALGN YMNRGARGNA SGFRLASLNR LADTKSSAAK GTTLLHYLVQ IIEKKFKDIL
     RLDEDIPHVR VAAKVSLGEL SKDMAQLRLG LKDVAKEIEF HLSQSPLAND KFVPVMREFQ
     ATATCRLAEV EDQYQDMKTR FERAVRLFGE DPTNAQPDEF FGVFDAFLTS FTEARQDNEN
     MRRRQEEEEK RAKQEAELKK LTLERKHSRE GILSSINKSL SLKNGESAKG EFDDLISALR
     TGDVFGEDMA KFKRSRKSRV TGNSPPRRNS VNREDSRERI VSSGRRQ
//
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