TTL_MOUSE
ID TTL_MOUSE Reviewed; 377 AA.
AC P38585; Q8R1L7; Q8VEG2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Tubulin--tyrosine ligase;
DE Short=TTL;
DE EC=6.3.2.25 {ECO:0000250|UniProtKB:Q9QXJ0};
GN Name=Ttl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-239.
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION.
RX PubMed=27102488; DOI=10.1126/science.aaf0659;
RA Robison P., Caporizzo M.A., Ahmadzadeh H., Bogush A.I., Chen C.Y.,
RA Margulies K.B., Shenoy V.B., Prosser B.L.;
RT "Detyrosinated microtubules buckle and bear load in contracting
RT cardiomyocytes.";
RL Science 352:417-428(2016).
CC -!- FUNCTION: Catalyzes the post-translational addition of a tyrosine to
CC the C-terminal end of detyrosinated alpha-tubulin.
CC {ECO:0000269|PubMed:27102488}.
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; BC018513; AAH18513.1; -; mRNA.
DR EMBL; BC024414; AAH24414.1; -; mRNA.
DR CCDS; CCDS16719.1; -.
DR RefSeq; NP_081468.1; NM_027192.2.
DR AlphaFoldDB; P38585; -.
DR SMR; P38585; -.
DR STRING; 10090.ENSMUSP00000046883; -.
DR PhosphoSitePlus; P38585; -.
DR EPD; P38585; -.
DR MaxQB; P38585; -.
DR PaxDb; P38585; -.
DR PRIDE; P38585; -.
DR ProteomicsDB; 297682; -.
DR Antibodypedia; 33272; 177 antibodies from 25 providers.
DR DNASU; 69737; -.
DR Ensembl; ENSMUST00000035812; ENSMUSP00000046883; ENSMUSG00000027394.
DR GeneID; 69737; -.
DR KEGG; mmu:69737; -.
DR UCSC; uc008mhe.2; mouse.
DR CTD; 150465; -.
DR MGI; MGI:1916987; Ttl.
DR VEuPathDB; HostDB:ENSMUSG00000027394; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000161907; -.
DR HOGENOM; CLU_010131_2_0_1; -.
DR InParanoid; P38585; -.
DR OMA; LAQLVNY; -.
DR OrthoDB; 626048at2759; -.
DR PhylomeDB; P38585; -.
DR TreeFam; TF350555; -.
DR BioGRID-ORCS; 69737; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ttl; mouse.
DR PRO; PR:P38585; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P38585; protein.
DR Bgee; ENSMUSG00000027394; Expressed in barrel cortex and 257 other tissues.
DR ExpressionAtlas; P38585; baseline and differential.
DR Genevisible; P38585; MM.
DR GO; GO:0005874; C:microtubule; IC:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004835; F:tubulin-tyrosine ligase activity; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
DR GO; GO:0030516; P:regulation of axon extension; IMP:MGI.
DR GO; GO:0090235; P:regulation of metaphase plate congression; ISO:MGI.
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_0000212435"
FT DOMAIN 3..370
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT CONFLICT 222
FT /note="R -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="V -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="H -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="K -> N (in Ref. 1; AAH24414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 43136 MW; 4D4E75243BB2CEDD CRC64;
MYTFVVRDEN SSVYAEVSRL LLATGYWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLAQ
LVNYYRGADK LCRKASLVKL VKTSPELSES CSWFPESYVI YPTNLKTPVA PAQNGIQLPV
SNSRTDEREF FLASYNRKKE DGEGNVWIAK SSAGAKGEGI LISSEASELL DFIDSQGQVH
VIQKYLERPL LLEPGHRKFD IRSWVLVDHQ YNIYLYREGV LRTASEPYHV DNFQDKTCHL
TNHCIQKEYS KNYGKYEEGN EMFFEEFNQY LTSALNITLE SSILLQIKHI IRSCLMSVEP
AISTKHLPYQ SFQLLGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAISSVFP
PPDTEQVPQQ PAAFVKL
