TTLL5_CAEEL
ID TTLL5_CAEEL Reviewed; 730 AA.
AC E9P886; O17720;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Tubulin polyglutamylase ttll-5 {ECO:0000305};
DE EC=6.-.-.- {ECO:0000250|UniProtKB:Q8CHB8};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000312|WormBase:C55A6.2b};
GN Name=ttll-5 {ECO:0000312|WormBase:C55A6.2b};
GN ORFNames=C55A6.2 {ECO:0000312|WormBase:C55A6.2b};
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 which preferentially modifies alpha-tubulin
CC (By similarity). Involved in the side-chain initiation step of the
CC polyglutamylation reaction rather than in the elongation step (By
CC similarity). Together with ttll-4 and ttll-11, required for male mating
CC (PubMed:27635036). Probably by regulating microtubule stability via the
CC glutamylation of tubulin, negatively regulates axon regrowth after
CC injury in PLM neurons (PubMed:23000142). {ECO:0000250|UniProtKB:Q8CHB8,
CC ECO:0000269|PubMed:23000142, ECO:0000269|PubMed:27635036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q8CHB8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000250|UniProtKB:Q8CHB8};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:C55A6.2b};
CC IsoId=E9P886-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C55A6.2a};
CC IsoId=E9P886-2; Sequence=VSP_060272;
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles (PubMed:20519502).
CC Not expressed in sensory neurons (PubMed:20519502).
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; CAB02862.3; -; Genomic_DNA.
DR EMBL; BX284605; CBZ01788.1; -; Genomic_DNA.
DR PIR; C89217; C89217.
DR PIR; T20262; T20262.
DR RefSeq; NP_001256331.1; NM_001269402.1. [E9P886-1]
DR RefSeq; NP_001256332.1; NM_001269403.1. [E9P886-2]
DR AlphaFoldDB; E9P886; -.
DR SMR; E9P886; -.
DR STRING; 6239.C55A6.2b; -.
DR PaxDb; E9P886; -.
DR PeptideAtlas; E9P886; -.
DR EnsemblMetazoa; C55A6.2a.1; C55A6.2a.1; WBGene00008331. [E9P886-2]
DR EnsemblMetazoa; C55A6.2b.1; C55A6.2b.1; WBGene00008331. [E9P886-1]
DR GeneID; 179582; -.
DR KEGG; cel:CELE_C55A6.2; -.
DR UCSC; C55A6.2; c. elegans.
DR CTD; 179582; -.
DR WormBase; C55A6.2a; CE29733; WBGene00008331; ttll-5. [E9P886-2]
DR WormBase; C55A6.2b; CE45770; WBGene00008331; ttll-5. [E9P886-1]
DR eggNOG; KOG2157; Eukaryota.
DR eggNOG; KOG4506; Eukaryota.
DR GeneTree; ENSGT00940000162910; -.
DR HOGENOM; CLU_010131_1_4_1; -.
DR InParanoid; E9P886; -.
DR OMA; YLMEDYD; -.
DR OrthoDB; 219807at2759; -.
DR PhylomeDB; E9P886; -.
DR Reactome; R-CEL-8955332; Carboxyterminal post-translational modifications of tubulin.
DR PRO; PR:E9P886; -.
DR Proteomes; UP000001940; Chromosome V.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0034606; P:response to hermaphrodite contact; IGI:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..730
FT /note="Tubulin polyglutamylase ttll-5"
FT /id="PRO_0000447855"
FT DOMAIN 120..478
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 594..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060272"
SQ SEQUENCE 730 AA; 82827 MW; BDF2C3CC64C29479 CRC64;
MKPKNVPREI FNPFTNKTSL GTRREGLFLC KRLKLRPDNY LEEYCADLEV IDIMAPIRPA
DETERCPPTS TSDDQEAGDY LVSRNKKSRN SDYMLFSSDA LVHIAHDAKV SEKYTWLGER
LRLTFKMMRS DSRLIRTMCH SHGFMQCSSK NPSVNVIWMG APVKSVRMRE LMPWQRLNQF
PRSTELTKKD RLYENIERSK SIFGESFDFI PEFYVTPREN RKMENAFVRV AKEIAAAGGE
LCFPGEFIVK PTNSRQGKGI FFANSMADIP AEGPLLVSRY LKDPYLVNNH KFDLRIYVAV
TSFYPLVAYV YSEGLARLAS RPYDTSASSA DSNEYVHLTN YSINKNSTSF VRNESMSSED
LGHKWTLGAL LRYVENEGKD AKLLMLRIED LIVKSLLSIQ NSVATASRTN LRFACTNFEL
FGFDVLVDQA LKPWLLEVNL SPSLACDAPL DSLLKTRLIA DLLNLACVPL LDRKIIDSVT
PALRKSMNSQ ESESSETDDL ELDPMCAKTL KRRPVGLKRS VLNKKIVSGS TSLIPNNEKK
FDQIVRKAEL EDGRRGDFIR VFPRNGTWGM YSPVMEDLGN EDFDERLFDE VVTKKNTKNS
SGSSKASSSS ASASSSSSSM HIEDLSDLFH EVMMQCDKYS SIADVPIEIR EIISPWYEEA
SEYTKKITQE GETYACKLPV IRSTARLRTK SCAEFYEVRK VQLAKKKESE AMASKENEPI
VLQAVVAKRI
