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   03-AUG-2022, entry version 118.
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; 1.
DR   STRING; 6239.D2013.9.2; -.
DR   iPTMnet; Q09512; -.
DR   EPD; Q09512; -.
DR   PaxDb; Q09512; -.
DR   PeptideAtlas; Q09512; -.
DR   EnsemblMetazoa; D2013.9.1; D2013.9.1; WBGene00008405.
DR   GeneID; 174480; -.
DR   KEGG; cel:CELE_D2013.9; -.
DR   CTD; 174480; -.
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; 611643at2759; -.
DR   PhylomeDB; Q09512; -.
DR   Reactome; R-CEL-8955332; Carboxyterminal post-translational modifications of tubulin.
DR   PRO; PR:Q09512; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00008405; Expressed in germ line (C elegans) and 4 other 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:oviposition; IMP:WormBase.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   InterPro; IPR027749; TTLL12.
DR   PANTHER; PTHR46088; PTHR46088; 1.
DR   Pfam; PF03133; TTL; 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