TTLL9_CAEEL
ID TTLL9_CAEEL Reviewed; 417 AA.
AC Q564U4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable tubulin polyglutamylase ttll-9 {ECO:0000305};
DE EC=6.-.-.- {ECO:0000250|UniProtKB:A2APC3};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0000312|WormBase:F25C8.5};
GN Name=ttll-9 {ECO:0000312|WormBase:F25C8.5};
GN ORFNames=F25C8.5 {ECO:0000312|WormBase:F25C8.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=20519502; DOI=10.1074/jbc.c110.128280;
RA Kimura Y., Kurabe N., Ikegami K., Tsutsumi K., Konishi Y., Kaplan O.I.,
RA Kunitomo H., Iino Y., Blacque O.E., Setou M.;
RT "Identification of tubulin deglutamylase among Caenorhabditis elegans and
RT mammalian cytosolic carboxypeptidases (CCPs).";
RL J. Biol. Chem. 285:22936-22941(2010).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=23000142; DOI=10.1016/j.devcel.2012.08.010;
RA Ghosh-Roy A., Goncharov A., Jin Y., Chisholm A.D.;
RT "Kinesin-13 and tubulin posttranslational modifications regulate
RT microtubule growth in axon regeneration.";
RL Dev. Cell 23:716-728(2012).
RN [4] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=27635036; DOI=10.1242/bio.017442;
RA Chawla D.G., Shah R.V., Barth Z.K., Lee J.D., Badecker K.E., Naik A.,
RA Brewster M.M., Salmon T.P., Peel N.;
RT "Caenorhabditis elegans glutamylating enzymes function redundantly in male
RT mating.";
RL Biol. Open 5:1290-1298(2016).
CC -!- FUNCTION: Polyglutamylase that forms polyglutamate side chains on
CC tubulin (By similarity). Acts when complexed with other proteins
CC (Probable). Appears to be dispensable for polar spindle formation in
CC dividing embryonic cells, for cilia-dependent osmotic avoidance and for
CC male mating behavior (PubMed:27635036). Probably by regulating
CC microtubule stability via the glutamylation of tubulin, regulates PLM
CC axon developmental growth (PubMed:23000142).
CC {ECO:0000250|UniProtKB:A2APC3, ECO:0000269|PubMed:23000142,
CC ECO:0000269|PubMed:27635036, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in head sensory neurons.
CC {ECO:0000269|PubMed:20519502}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults.
CC {ECO:0000269|PubMed:27635036}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CAI79169.1; -; Genomic_DNA.
DR RefSeq; NP_001023841.1; NM_001028670.1.
DR AlphaFoldDB; Q564U4; -.
DR SMR; Q564U4; -.
DR STRING; 6239.F25C8.5; -.
DR PaxDb; Q564U4; -.
DR EnsemblMetazoa; F25C8.5.1; F25C8.5.1; WBGene00044187.
DR GeneID; 3564837; -.
DR KEGG; cel:CELE_F25C8.5; -.
DR UCSC; F25C8.5; c. elegans.
DR CTD; 3564837; -.
DR WormBase; F25C8.5; CE38330; WBGene00044187; ttll-9.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000159879; -.
DR HOGENOM; CLU_010131_0_1_1; -.
DR InParanoid; Q564U4; -.
DR OMA; LIWANGP; -.
DR OrthoDB; 584228at2759; -.
DR PhylomeDB; Q564U4; -.
DR Reactome; R-CEL-8955332; Carboxyterminal post-translational modifications of tubulin.
DR PRO; PR:Q564U4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00044187; Expressed in larva.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0018095; P:protein polyglutamylation; IBA:GO_Central.
DR GO; GO:0019098; P:reproductive behavior; IEA:UniProt.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027751; TTLL9.
DR PANTHER; PTHR12241:SF39; PTHR12241:SF39; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..417
FT /note="Probable tubulin polyglutamylase ttll-9"
FT /id="PRO_0000447856"
FT DOMAIN 23..372
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT BINDING 188..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ SEQUENCE 417 AA; 48465 MW; D6D05A22AB9B9BF9 CRC64;
MSSISNELSV TSSQNVISNS KEQRKKKILF KCALTNTISD VLTNREGWAQ TQGDDWQFFW
VTREWMTTCY DKHKFSEKQM ICHFRNDFEL TRKDFLIKNY KKARKAKEKS GIDVVSEFNF
LPSSYVLPTE YHLFVEEFRK YPNDTIWIMK PVAGAQGKGI FLFRKLKHVQ EWKKKDSSGS
EALPYVVQCY VHNPYLVGGK KFDVRIYVLV TSFRPLNAWV HREGFARFSH SRYSTDSVDD
AFVHLTNVAV AKTAADYDPE RGLKWSLPKL FRFFKSVHGQ SKLSKTMNDL TNVIIESLKS
VQNLIIQDNH CFELYGYDIL FDENLKPWLL EVNASPSLTA SSQEDFELKY RILNHMIDVL
DIEKKLIGNE NEVGGFDLLI KNSKPVELCK VDFHTQPFFG TQFNLRLGDY VEATPMP
