ID TTL12_CAEEL Reviewed; 662 AA.
AC Q09512;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 12;
DE AltName: Full=Inactive tubulin--tyrosine ligase-like protein 12 {ECO:0000305};
GN Name=ttll-12 {ECO:0000312|WormBase:D2013.9};
GN ORFNames=D2013.9 {ECO:0000312|WormBase:D2013.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
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).
CC -!- FUNCTION: Regulates microtubule dynamics in uterine muscle cells.
CC {ECO:0000269|PubMed:24780738}.
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 and in hermaphrodite specific neurons.
CC {ECO:0000269|PubMed:24780738}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the tubulin--tyrosine ligase family,
CC the TTL domain lacks some of the ATP binding sites predicted to be
CC essential for TTL activity (By similarity). Lacks tyrosine ligase
CC activity in vitro (By similarity). Lacks glutamylation activity in
CC vitro (By similarity). {ECO:0000250|UniProtKB:Q14166,
CC ECO:0000250|UniProtKB:Q3UDE2}.
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DR EMBL; BX284602; CAA87778.1; -; Genomic_DNA.
DR EMBL; Z47809; CAA87778.1; JOINED; Genomic_DNA.
DR PIR; T20343; T20343.
DR RefSeq; NP_495990.1; NM_063589.3.
DR AlphaFoldDB; Q09512; -.
DR SMR; Q09512; -.
DR BioGRID; 39804; 2.
DR STRING; 6239.D2013.9.1; -.
DR iPTMnet; Q09512; -.
DR EPD; Q09512; -.
DR PaxDb; 6239-D2013-9-2; -.
DR PeptideAtlas; Q09512; -.
DR EnsemblMetazoa; D2013.9.1; D2013.9.1; WBGene00008405.
DR GeneID; 174480; -.
DR KEGG; cel:CELE_D2013.9; -.
DR AGR; WB:WBGene00008405; -.
DR WormBase; D2013.9; CE01535; WBGene00008405; ttll-12.
DR eggNOG; KOG2155; Eukaryota.
DR GeneTree; ENSGT00390000006760; -.
DR HOGENOM; CLU_018324_0_0_1; -.
DR InParanoid; Q09512; -.
DR OMA; CKRACDY; -.
DR OrthoDB; 1366030at2759; -.
DR PhylomeDB; Q09512; -.
DR PRO; PR:Q09512; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008405; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
DR GO; GO:0030017; C:sarcomere; HDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018991; P:egg-laying behavior; IMP:WormBase.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027749; TTLL12.
DR PANTHER; PTHR46088; TUBULIN--TYROSINE LIGASE-LIKE PROTEIN 12; 1.
DR PANTHER; PTHR46088:SF1; TUBULIN--TYROSINE LIGASE-LIKE PROTEIN 12; 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; Nucleotide-binding; Reference proteome.
FT CHAIN 1..662
FT /note="Tubulin--tyrosine ligase-like protein 12"
FT /id="PRO_0000212449"
FT DOMAIN 324..660
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT BINDING 472..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ SEQUENCE 662 AA; 76751 MW; 5044C76422145698 CRC64;
MSEDRSAYPF STFLDQHSGQ LNASDVPPEL WHSLYKKLSD QTFDAGDHFQ IICEMNEDDE
KTLFVRALED LHNNDEDNIF LIDHFMSFSS ESARKCVEST EGLVERLAGL FGIDTDSTEE
VDETVEKIET SVEKEEAEHA KKISSETGNL PRHESVDARL SSYSVDDPKN ELTEKVLKAL
WKYSQTYSVS YQLDNGEIEK KSVWYVMDDF GTRVRHSTEP NVRIVPLMFL PQNCAYSIMF
LTKPVNTDEE IMMDWASNVI TAQHPEWRKY IEQPWAAQDF SKETMIPDAP TLEYFTSGRN
PDFLAGPTEQ QTCQSAIFTS LPILKKRKIK VYADDTQLTE HLKNHKVEYV DDIKKADVIW
MIKHFHDYKQ LSEENPCGMI NQFPFESCIT VKDLLAACAM RDPAKNDWYQ LTYNLNTQLP
EFVARFQNRE LNGQHNVWIV KPWNLARGMD MTVTEDLNQI IRMIETGPKI VCEYIPRPLL
FPRPDNGNKV KFDLRYIVFL NGIAPVTAYV YNRFWIRFAI NEFSLSNFED VETHFTVFNY
LDKEKILQMK CENFIETIEK AYPRIQWSEV QKDINLTIRK AIEAAAKEEA PRGVAPNVQS
RAMYGVDIML QHGDNDVIKS TLLEINFMPD TTRACQYYPD FADTVFETLF LDEIDPTKVT
PI
//
