TTL15_CAEEL
ID TTL15_CAEEL Reviewed; 513 AA.
AC Q21279;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable tubulin polyglutamylase ttll-15 {ECO:0000305};
DE EC=6.-.-.- {ECO:0000255|PROSITE-ProRule:PRU00568};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 15 {ECO:0000312|WormBase:K07C5.7};
GN Name=ttll-15 {ECO:0000312|WormBase:K07C5.7};
GN ORFNames=K07C5.7 {ECO:0000312|EMBL:CAA94900.3};
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, AND DISRUPTION PHENOTYPE.
RX PubMed=24780738; DOI=10.1016/j.devcel.2014.03.007;
RA Lacroix B., Bourdages K.G., Dorn J.F., Ihara S., Sherwood D.R.,
RA Maddox P.S., Maddox A.S.;
RT "In situ imaging in C. elegans reveals developmental regulation of
RT microtubule dynamics.";
RL Dev. Cell 29:203-216(2014).
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: Probable polyglutamylase that forms polyglutamate side chains
CC on tubulin (PubMed:27635036). Probably acts when complexed with other
CC proteins (PubMed:27635036). Appears to be dispensable for polar spindle
CC formation in dividing embryonic cells, for cilia-dependent osmotic
CC avoidance and for male mating behavior (PubMed:27635036). Regulates
CC microtubule dynamics in uterine muscle cells (PubMed:24780738).
CC {ECO:0000269|PubMed:24780738, ECO:0000269|PubMed:27635036,
CC ECO:0000303|PubMed:27635036}.
CC -!- TISSUE SPECIFICITY: Expressed in hypodermis and pharyngeal muscles.
CC {ECO:0000269|PubMed:20519502}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults.
CC {ECO:0000269|PubMed:27635036}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L1 larval stage
CC causes a reduction in egg-laying, likely due to a defect in the egg-
CC laying apparatus muscles. {ECO:0000269|PubMed:24780738}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CAA94900.3; -; Genomic_DNA.
DR RefSeq; NP_505663.3; NM_073262.5.
DR AlphaFoldDB; Q21279; -.
DR SMR; Q21279; -.
DR STRING; 6239.K07C5.7; -.
DR EPD; Q21279; -.
DR PaxDb; Q21279; -.
DR PeptideAtlas; Q21279; -.
DR EnsemblMetazoa; K07C5.7.1; K07C5.7.1; WBGene00010630.
DR GeneID; 187090; -.
DR KEGG; cel:CELE_K07C5.7; -.
DR UCSC; K07C5.7; c. elegans.
DR CTD; 187090; -.
DR WormBase; K07C5.7; CE41580; WBGene00010630; ttll-15.
DR eggNOG; KOG2156; Eukaryota.
DR GeneTree; ENSGT00390000006352; -.
DR HOGENOM; CLU_038007_0_0_1; -.
DR InParanoid; Q21279; -.
DR OMA; DLCTTQL; -.
DR OrthoDB; 309204at2759; -.
DR PhylomeDB; Q21279; -.
DR PRO; PR:Q21279; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010630; Expressed in larva and 2 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR InterPro; IPR004344; TTL/TTLL_fam.
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..513
FT /note="Probable tubulin polyglutamylase ttll-15"
FT /id="PRO_0000447858"
FT DOMAIN 73..411
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT BINDING 216..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ SEQUENCE 513 AA; 59523 MW; 2850FAE9D0B3CCB0 CRC64;
MGLLDSKLCM MILAVSVLII DINFEARIGT FFDLRLRTSY FKKSSSPLLS HTDSEEDLNY
LSKHEDKRPV AIVTGSYESA HTGHMMHIRE MFEHTGYKIV TKNELSLDTK WDVMWHHEYS
FTQEPFKTLI KNASPNQIVN HVPGSGFYTS KVQLATSDLS NGVPKAFQLP AEKSKLLEYA
EKNPDVLWVQ KDNTHRNIKI KSTNDMDLSK NNSFVQKFVD NPLLIDNKKF DIGIYTVVTS
LLPLRVYIYD GDVLIRFCPE DYHPFDANNV DKYVVGDDYT PIWEINSLKK YFNTQKMSFK
STIDSYLGMQ GMDTSKIWLQ IRNIIGEVFR TQQTKMLMSL QNLKLNPQYF ELSRFDFVVD
DQLNVFLMEA NMSPNLSSGH FKQNQILYEQ VLMNIFSLTG ISTPITKEAD ILFKSRTSEQ
NPLVNSRDIN LPLKFCVENK CESCDEAPEC QLCGHCMNTE TRKILEQTFV ENSNRKQMKR
IQFDYENHHP LTKEDHLLTL WLSTKCQLDN TWC
