ID   TTL_RAT                 Reviewed;         377 AA.
AC   Q9QXJ0; Q9Z1E5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Tubulin--tyrosine ligase;
DE            Short=TTL;
DE            EC=6.3.2.25 {ECO:0000269|PubMed:9108330};
GN   Name=Ttl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX   PubMed=12512949; DOI=10.1023/a:1021640203644;
RA   Mas C.R., Arregui C.O., Filiberti A., Argarana C.E., Barra H.S.;
RT   "Cloning of rat olfactory bulb tubulin tyrosine ligase cDNA: a dominant
RT   negative mutant and an antisense cDNA increase the proliferation rate of
RT   cells in culture.";
RL   Neurochem. Res. 27:1453-1458(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-220, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=9108330; DOI=10.1046/j.1440-169x.1997.t01-1-00005.x;
RA   Arregui C.O., Mas C.R., Argarana C.E., Barra H.S.;
RT   "Tubulin tyrosine ligase: protein and mRNA expression in developing rat
RT   skeletal muscle.";
RL   Dev. Growth Differ. 39:167-178(1997).
CC   -!- FUNCTION: Catalyzes the post-translational addition of a tyrosine to
CC       the C-terminal end of detyrosinated alpha-tubulin.
CC       {ECO:0000269|PubMed:9108330}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-
CC         [tubulin] + L-tyrosine = ADP + C-terminal L-alpha-aminoacyl-L-
CC         glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H(+) + phosphate;
CC         Xref=Rhea:RHEA:17605, Rhea:RHEA-COMP:16434, Rhea:RHEA-COMP:16435,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58315, ChEBI:CHEBI:149554, ChEBI:CHEBI:149555,
CC         ChEBI:CHEBI:456216; EC=6.3.2.25;
CC         Evidence={ECO:0000269|PubMed:9108330};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P38584};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P38584};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P38584}.
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC       {ECO:0000305}.
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DR   EMBL; AF207605; AAF18465.1; -; mRNA.
DR   EMBL; U53214; AAD10402.1; -; mRNA.
DR   RefSeq; NP_612545.1; NM_138536.1.
DR   AlphaFoldDB; Q9QXJ0; -.
DR   SMR; Q9QXJ0; -.
DR   STRING; 10116.ENSRNOP00000024695; -.
DR   PhosphoSitePlus; Q9QXJ0; -.
DR   jPOST; Q9QXJ0; -.
DR   PaxDb; Q9QXJ0; -.
DR   GeneID; 171572; -.
DR   KEGG; rno:171572; -.
DR   UCSC; RGD:621113; rat.
DR   CTD; 150465; -.
DR   RGD; 621113; Ttl.
DR   eggNOG; KOG2157; Eukaryota.
DR   InParanoid; Q9QXJ0; -.
DR   OrthoDB; 626048at2759; -.
DR   PhylomeDB; Q9QXJ0; -.
DR   BRENDA; 6.3.2.25; 5301.
DR   PRO; PR:Q9QXJ0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; IDA:RGD.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0030516; P:regulation of axon extension; ISO:RGD.
DR   GO; GO:0090235; P:regulation of metaphase plate congression; ISO:RGD.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Magnesium; Nucleotide-binding; Potassium;
KW   Reference proteome.
FT   CHAIN           1..377
FT                   /note="Tubulin--tyrosine ligase"
FT                   /id="PRO_0000212437"
FT   DOMAIN          3..370
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
SQ   SEQUENCE   377 AA;  43118 MW;  1CB3B914D088A316 CRC64;
     MYTFVVRQEN SSVYAEVSRL LLATGYWKRL RRDNPRFNLM LGGRNRLPFG RLGHEPGLAQ
     LVNYYRGADK LCRKASLVKL VKTSPELSES CSWFPESYVI HPTNLKTPVA PAQNGIQLPV
     SNSRTDEREF FLASYNRKKE DGEGNVWIAK SSAGAKGEGI LISSEASELL DFIDNQGQVH
     VIQKYLEHPL LLEPGHRKFD IRSWVLVDHQ YNIYLYREGV LRTASEPYHV DNFQDKTCHL
     TNHCIQKEYS KNYGKYEEGN EMFFEEFNQY LTSALNITLE NSILLQIKHI IRSCLMSVEP
     AISTKHLPYQ SFQLLGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAISSVFP
     PPDTEQVPQQ PAAFMKL