TTL3B_DROME
ID TTL3B_DROME Reviewed; 756 AA.
AC Q9VM92; Q5BHY1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Tubulin glycylase 3B;
DE Short=dmTTLL3B;
DE EC=6.3.2.-;
GN Name=TTLL3B; ORFNames=CG11201;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
CC -!- FUNCTION: Essential glycylase which modifies both tubulin and non-
CC tubulin proteins, generating side chains of glycine on the gamma-
CC carboxyl groups of specific glutamate residues of target proteins.
CC Monoglycylates alpha-tubulin by adding a single glycine chain to
CC generate monoglycine side chains, but is not involved in elongation
CC step to generate polyglycine side chains on alpha-tubulin. Has the
CC ability to both mono- and polyglycylate non-tubulin proteins such as up
CC (Troponin T). Required for early steps of spermatogenesis.
CC {ECO:0000269|PubMed:19524510}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19524510}. Nucleus {ECO:0000269|PubMed:19524510}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014134; AAF52431.2; -; Genomic_DNA.
DR EMBL; BT021443; AAX33591.1; -; mRNA.
DR RefSeq; NP_609068.2; NM_135224.3.
DR AlphaFoldDB; Q9VM92; -.
DR SMR; Q9VM92; -.
DR BioGRID; 60098; 3.
DR IntAct; Q9VM92; 2.
DR STRING; 7227.FBpp0289333; -.
DR PaxDb; Q9VM92; -.
DR DNASU; 33946; -.
DR EnsemblMetazoa; FBtr0300056; FBpp0289333; FBgn0031853.
DR GeneID; 33946; -.
DR KEGG; dme:Dmel_CG11201; -.
DR UCSC; CG11201-RB; d. melanogaster.
DR CTD; 33946; -.
DR FlyBase; FBgn0031853; TTLL3B.
DR VEuPathDB; VectorBase:FBgn0031853; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000168830; -.
DR HOGENOM; CLU_010131_5_0_1; -.
DR InParanoid; Q9VM92; -.
DR OMA; RMAFIED; -.
DR OrthoDB; 143220at2759; -.
DR PhylomeDB; Q9VM92; -.
DR BioGRID-ORCS; 33946; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33946; -.
DR PRO; PR:Q9VM92; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031853; Expressed in testis and 7 other tissues.
DR Genevisible; Q9VM92; DM.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; IDA:UniProtKB.
DR GO; GO:0070737; F:protein-glycine ligase activity, elongating; IDA:UniProtKB.
DR GO; GO:0070736; F:protein-glycine ligase activity, initiating; IDA:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR GO; GO:0018094; P:protein polyglycylation; IDA:UniProtKB.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Differentiation; Ligase; Microtubule;
KW Nucleotide-binding; Nucleus; Reference proteome; Spermatogenesis.
FT CHAIN 1..756
FT /note="Tubulin glycylase 3B"
FT /id="PRO_0000381796"
FT DOMAIN 272..629
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ SEQUENCE 756 AA; 86109 MW; 62BD02138F624E27 CRC64;
MTTQNTTPAG FTGNRNRYYN PVSKIQSLIH NLDAELVQLC KQCSVQKPLT SLNNSTSLGS
HFSNFGALGG GSGSKTMGGS SSMGSNNFSP DSIGNLLARV RASTPLPRTV TSSPTAPEAQ
KRQMRNVYRT RVIDAYRNRR IFTVYGNYHT VRRALMRRGW LEKLPASRHA KLQSMSEDAL
LEHARRGNDY EAVVISKMIN HFPAFFIWQG KGQRDLCAEV RPFRNRVRRS QFLDFSTKVG
LVGCAEQERW YREDGVCGMS YPRFYRLGGN NLEERMAFIE DYQQTQARSL LLYVREHQPA
ELISENGTIF STTLDFALGK VKKMVRHAEH YSLDDARIKP PTPAEIVENQ TFMVQSTDVL
KSNAKFKVSE KVMAEYARLA GLYLDQIESL RPDYRWDGSR NLWILKPGYQ SRGIGIVIRS
SLDDILQWTS NNQNKKYIVQ KYIERPLLIY RTKFDIRQYM LLTITDTKVS IWTYRDCYLR
FSSQEFTMDD LRESIHLTNN SVQKRYKNKT NRDSRLPKNN MWSLDQFKNY LRIMGAPDGS
WSKTYNGFKQ NLVAVVMASL DETELLQNAF ELYGCDFMLD EHYNPILIEI NSTPDLSPST
EITARICPMV LKDCIRVVVD LPKNPTAATG LFELAFEVNY SINKGADGKP LELNGKQMTL
FENMPRMRNS PRTRLLRKIL NNVKTSTTKK VEKVVEAPAK NVKNPTAKIT KKKKLSASAG
SSTAASAQPS TQNLTTKLIL NPATRENLAL QYTAPK
