ID   D2A295_TRICA            Unreviewed;       401 AA.
AC   D2A295;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   02-SEP-2026, entry version 77.
DE   RecName: Full=Polyglutamylase complex subunit TTLL1 {ECO:0000256|ARBA:ARBA00074800};
DE   AltName: Full=Tubulin polyglutamylase TTLL1 {ECO:0000256|ARBA:ARBA00075351};
DE   AltName: Full=Tubulin polyglutamylase complex subunit 3 {ECO:0000256|ARBA:ARBA00083073};
DE   AltName: Full=Tubulin--tyrosine ligase-like protein 1 {ECO:0000256|ARBA:ARBA00080021};
GN   Name=AUGUSTUS-3.0.2_07682 {ECO:0000313|EMBL:EFA02053.1};
GN   ORFNames=TcasGA2_TC007682 {ECO:0000313|EMBL:EFA02053.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Neuropteroidea; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA02053.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA02053.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02053.1,
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:EFA02053.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02053.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-
CC         glutamate + ATP = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-
CC         [protein] + ADP + phosphate + H(+); Xref=Rhea:RHEA:60148, Rhea:RHEA-
CC         COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:143623, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00052959};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC         Evidence={ECO:0000256|ARBA:ARBA00052959};
CC   -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which
CC       contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. Interacts with PCM1,
CC       CSTPP1 and LRRC49. {ECO:0000256|ARBA:ARBA00062645}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000256|ARBA:ARBA00004120}.
CC   -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC       {ECO:0000256|ARBA:ARBA00006118}.
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DR   EMBL; KQ971338; EFA02053.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2A295; -.
DR   FunCoup; D2A295; 45.
DR   STRING; 7070.D2A295; -.
DR   KEGG; tca:663328; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_010131_0_0_1; -.
DR   InParanoid; D2A295; -.
DR   OMA; DWNFYWS; -.
DR   OrthoDB; 202825at2759; -.
DR   PhylomeDB; D2A295; -.
DR   Proteomes; UP000007266; Linkage Group LG4.
DR   GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IBA:GO_Central.
DR   GO; GO:0007288; P:sperm axoneme assembly; IBA:GO_Central.
DR   FunFam; 3.30.470.20:FF:000033; Probable tubulin polyglutamylase TTLL1; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241:SF31; POLYGLUTAMYLASE COMPLEX SUBUNIT TTLL1; 1.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PROSITE-
KW   ProRule:PRU00568}; Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
SQ   SEQUENCE   401 AA;  46599 MW;  21C44228076AC257 CRC64;
     MRITFCTDLD KSVVVANCEK RGWIQVGPED DWNIYWAGTQ TCRSLFSVDS GYRMHDNQLI
     NHFPNHYEIS RKDLLVKNIK RYRRDLEKEG NVLAERGDSK YLHLDFIPVT FVLPADYNMF
     VEEYRKAPQS TWIMKPCGRS QGSGIFLINK LSKLKRWSRE AKSPFQQQLT KESYVISKYI
     DNPLLIGGKK FDLRLYVLVT SFRPLKAYQF RLGFCRFCTV KYDSSVAELD NMYVHLTNVS
     VQKHGGEYNS LHGGKLSVQN LRLHLESTRG KQVTERLFDQ ISWLIIHSLK AVAPVIATDR
     HCFECYGYDI IIDNKLKPWL IEVNASPSLT STTANDRILK HKLMDNIFSI VVPPSGLPDV
     RWNKIPSQEA LGDFELLIDE DLIHLHETEN NSYLLKNNRW K
//