ID   TTL_PIG                 Reviewed;         379 AA.
AC   P38160;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Tubulin--tyrosine ligase;
DE            Short=TTL;
DE            EC=6.3.2.25 {ECO:0000250|UniProtKB:Q9QXJ0};
GN   Name=TTL;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=8093886; DOI=10.1083/jcb.120.3.725;
RA   Ersfeld K., Wehland J., Plessmann U., Dodemont H., Gerke V., Weber K.;
RT   "Characterization of the tubulin-tyrosine ligase.";
RL   J. Cell Biol. 120:725-732(1993).
CC   -!- FUNCTION: Catalyzes the post-translational addition of a tyrosine to
CC       the C-terminal end of detyrosinated alpha-tubulin.
CC       {ECO:0000250|UniProtKB:Q9QXJ0}.
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:0000250|UniProtKB:Q9QXJ0};
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; X68453; CAA48494.1; -; mRNA.
DR   PIR; A45443; A45443.
DR   RefSeq; NP_001004041.1; NM_001004041.1.
DR   AlphaFoldDB; P38160; -.
DR   SMR; P38160; -.
DR   STRING; 9823.ENSSSCP00000008644; -.
DR   PaxDb; P38160; -.
DR   PRIDE; P38160; -.
DR   Ensembl; ENSSSCT00000084504; ENSSSCP00000068994; ENSSSCG00000008097.
DR   Ensembl; ENSSSCT00025005277; ENSSSCP00025002037; ENSSSCG00025003981.
DR   Ensembl; ENSSSCT00045033729; ENSSSCP00045023389; ENSSSCG00045019764.
DR   Ensembl; ENSSSCT00050105059; ENSSSCP00050046153; ENSSSCG00050076474.
DR   Ensembl; ENSSSCT00065085571; ENSSSCP00065037402; ENSSSCG00065062368.
DR   Ensembl; ENSSSCT00070045327; ENSSSCP00070038207; ENSSSCG00070022661.
DR   GeneID; 445530; -.
DR   KEGG; ssc:445530; -.
DR   CTD; 150465; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   GeneTree; ENSGT00940000164409; -.
DR   HOGENOM; CLU_010131_2_0_1; -.
DR   InParanoid; P38160; -.
DR   OMA; LAQLVNY; -.
DR   OrthoDB; 626048at2759; -.
DR   TreeFam; TF350555; -.
DR   Proteomes; UP000008227; Chromosome 3.
DR   Proteomes; UP000314985; Chromosome 3.
DR   Bgee; ENSSSCG00000008097; Expressed in occipital cortex and 45 other tissues.
DR   ExpressionAtlas; P38160; baseline and differential.
DR   Genevisible; P38160; SS.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
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; Direct protein sequencing; Ligase; Magnesium;
KW   Nucleotide-binding; Potassium; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Tubulin--tyrosine ligase"
FT                   /id="PRO_0000212436"
FT   DOMAIN          3..370
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
SQ   SEQUENCE   379 AA;  43510 MW;  9CF23C049E9AB543 CRC64;
     MYTFVVRDEN SSVYAEVSRL LLATGHWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLMQ
     LVNYYRGADK LCRKASLVKL IKTSPELAES CTWFPESYVI YPTNLKTPVA PAQNGIHPPI
     HSSRTDEREF FLTSYNKKKE DGEGNVWIAK SSAGAKGEGI LISSEATELL DFIDNQGQVH
     VIQKYLERPL LLEPGHRKFD IRSWVLVDHQ YNIYLYREGV LRTASEPYHT DNFQDKTCHL
     TNHCIQKEYS KNYGKYEEGN EMFFEEFNQY LTSALNITLE SSILLQIKHI IRSCLLSVEP
     AISTRHLPYQ SFQLFGFDFM VDEDLKVWLI EVNGAPACAQ KLYAELCQGI VDIAIASVFP
     PPDAEQQQQQ PPPAAFIKL