TTLL7_HUMAN
ID TTLL7_HUMAN Reviewed; 887 AA.
AC Q6ZT98; Q5TAX8; Q5TAX9; Q6P990; Q86YS1; Q9H5U4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Tubulin polyglutamylase TTLL7 {ECO:0000305|PubMed:16901895};
DE EC=6.3.2.- {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:25959773};
DE AltName: Full=Testis development protein NYD-SP30 {ECO:0000303|Ref.1};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 7 {ECO:0000305|PubMed:25959773};
GN Name=TTLL7 {ECO:0000312|HGNC:HGNC:26242};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Xu M., Xu Y.Z., Li M.J., Zhou M.Z., Sha H.J.;
RT "Cloning and identification of a novel gene related to testis development,
RT NYD-SP30.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum, and Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=16901895; DOI=10.1074/jbc.m603984200;
RA Ikegami K., Mukai M., Tsuchida J., Heier R.L., Macgregor G.R., Setou M.;
RT "TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth of
RT MAP2-positive neurites.";
RL J. Biol. Chem. 281:30707-30716(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 36-518 OF MUTANT GLN-349 IN
RP COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF ARG-106; 143-ASN--LYS-146; LYS-178; ARG-205; ARG-227;
RP LYS-271; GLU-349; ARG-352; 385-LYS--LYS-393; 425-ARG--LYS-427 AND
RP 477-PHE--PHE-480.
RX PubMed=25959773; DOI=10.1016/j.cell.2015.04.003;
RA Garnham C.P., Vemu A., Wilson-Kubalek E.M., Yu I., Szyk A., Lander G.C.,
RA Milligan R.A., Roll-Mecak A.;
RT "Multivalent microtubule recognition by tubulin tyrosine ligase-like family
RT glutamylases.";
RL Cell 161:1112-1123(2015).
CC -!- FUNCTION: Polyglutamylase which modifies tubulin, generating
CC polyglutamate side chains of variable lengths on the gamma-carboxyl
CC group of specific glutamate residues within the C-terminal tail of
CC tubulin (PubMed:16901895, PubMed:25959773). Mediates both ATP-dependent
CC initiation and elongation steps of the polyglutamylation reaction
CC (PubMed:16901895, PubMed:25959773). Preferentially modifies the beta-
CC tubulin tail over an alpha-tail (PubMed:16901895, PubMed:25959773).
CC Competes with monoglycylase TTLL3 for modification site on beta-tubulin
CC substrate, thereby creating an anticorrelation between glycylation and
CC glutamylation reactions (By similarity). Required for neurite growth;
CC responsible for the strong increase in tubulin polyglutamylation during
CC postnatal neuronal maturation (By similarity).
CC {ECO:0000250|UniProtKB:A4Q9F0, ECO:0000250|UniProtKB:F7E540,
CC ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:25959773}.
CC -!- CATALYTIC ACTIVITY: [Tubulin polyglutamylase TTLL7]:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16901895,
CC ECO:0000269|PubMed:25959773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000305|PubMed:16901895, ECO:0000305|PubMed:25959773};
CC -!- CATALYTIC ACTIVITY: [Tubulin polyglutamylase TTLL7]:
CC Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP +
CC L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein]
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519,
CC Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16901895,
CC ECO:0000269|PubMed:25959773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000305|PubMed:16901895, ECO:0000305|PubMed:25959773};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBUNIT: Interacts with both alpha- and beta-tubulin (via C-terminal
CC tubulin tails). {ECO:0000269|PubMed:25959773}.
CC -!- INTERACTION:
CC Q6ZT98-3; P61968: LMO4; NbExp=3; IntAct=EBI-13339851, EBI-2798728;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:A4Q9F0}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:A4Q9F0}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:A4Q9F0}. Perikaryon
CC {ECO:0000250|UniProtKB:A4Q9F0}. Note=In cells with primary cilia, found
CC in both cilia and basal bodies. In neuronal cells, found in dendrites
CC and perikaryon. {ECO:0000250|UniProtKB:A4Q9F0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZT98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZT98-2; Sequence=VSP_015199, VSP_015200;
CC Name=3;
CC IsoId=Q6ZT98-3; Sequence=VSP_015201, VSP_015202;
CC -!- TISSUE SPECIFICITY: Highly expressed in the nervous system including
CC spinal cord, thalamus, hippocampus, hypothalamus and cerebellum.
CC {ECO:0000269|PubMed:16901895}.
CC -!- DOMAIN: The enzyme uses its core to engage the disordered anionic tails
CC of alpha- and beta-tubulin and the flexible c-MTBD (cationic
CC microtubule binding domain) region to bind the microtubule and position
CC itself for beta-tail modification. The c-MTBD region is positively
CC charged and becomes ordered when bound to microtubules: it interacts
CC with a negatively charged patch on alpha-tubulin. The presence of
CC positive charges in the c-MTBD region is essential for proper binding.
CC {ECO:0000269|PubMed:25959773}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
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DR EMBL; AY170843; AAO37763.1; -; mRNA.
DR EMBL; AK026686; BAB15526.1; -; mRNA.
DR EMBL; AK126792; BAC86695.1; -; mRNA.
DR EMBL; AC104454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060878; AAH60878.1; -; mRNA.
DR CCDS; CCDS690.2; -. [Q6ZT98-1]
DR RefSeq; NP_078962.4; NM_024686.4. [Q6ZT98-1]
DR RefSeq; XP_016857836.1; XM_017002347.1.
DR PDB; 4YLR; X-ray; 2.55 A; A=36-518.
DR PDB; 4YLS; X-ray; 2.60 A; A=36-518.
DR PDBsum; 4YLR; -.
DR PDBsum; 4YLS; -.
DR AlphaFoldDB; Q6ZT98; -.
DR SMR; Q6ZT98; -.
DR BioGRID; 122852; 15.
DR IntAct; Q6ZT98; 10.
DR MINT; Q6ZT98; -.
DR STRING; 9606.ENSP00000260505; -.
DR iPTMnet; Q6ZT98; -.
DR PhosphoSitePlus; Q6ZT98; -.
DR BioMuta; TTLL7; -.
DR DMDM; 73920151; -.
DR MassIVE; Q6ZT98; -.
DR PaxDb; Q6ZT98; -.
DR PeptideAtlas; Q6ZT98; -.
DR PRIDE; Q6ZT98; -.
DR ProteomicsDB; 68266; -. [Q6ZT98-1]
DR ProteomicsDB; 68267; -. [Q6ZT98-2]
DR ProteomicsDB; 68268; -. [Q6ZT98-3]
DR TopDownProteomics; Q6ZT98-2; -. [Q6ZT98-2]
DR Antibodypedia; 53234; 35 antibodies from 12 providers.
DR DNASU; 79739; -.
DR Ensembl; ENST00000260505.13; ENSP00000260505.8; ENSG00000137941.17. [Q6ZT98-1]
DR Ensembl; ENST00000480174.5; ENSP00000435334.1; ENSG00000137941.17. [Q6ZT98-2]
DR GeneID; 79739; -.
DR KEGG; hsa:79739; -.
DR MANE-Select; ENST00000260505.13; ENSP00000260505.8; NM_024686.6; NP_078962.4.
DR UCSC; uc001djc.4; human. [Q6ZT98-1]
DR CTD; 79739; -.
DR DisGeNET; 79739; -.
DR GeneCards; TTLL7; -.
DR HGNC; HGNC:26242; TTLL7.
DR HPA; ENSG00000137941; Tissue enriched (brain).
DR MIM; 618813; gene.
DR neXtProt; NX_Q6ZT98; -.
DR OpenTargets; ENSG00000137941; -.
DR PharmGKB; PA142670678; -.
DR VEuPathDB; HostDB:ENSG00000137941; -.
DR eggNOG; KOG2158; Eukaryota.
DR GeneTree; ENSGT00940000159078; -.
DR HOGENOM; CLU_010131_7_1_1; -.
DR InParanoid; Q6ZT98; -.
DR OMA; NCCRRIV; -.
DR OrthoDB; 1251554at2759; -.
DR PhylomeDB; Q6ZT98; -.
DR TreeFam; TF313087; -.
DR BRENDA; 6.3.2.B24; 2681.
DR PathwayCommons; Q6ZT98; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q6ZT98; -.
DR BioGRID-ORCS; 79739; 6 hits in 1071 CRISPR screens.
DR ChiTaRS; TTLL7; human.
DR GenomeRNAi; 79739; -.
DR Pharos; Q6ZT98; Tbio.
DR PRO; PR:Q6ZT98; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6ZT98; protein.
DR Bgee; ENSG00000137941; Expressed in corpus callosum and 152 other tissues.
DR ExpressionAtlas; Q6ZT98; baseline and differential.
DR Genevisible; Q6ZT98; HS.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018095; P:protein polyglutamylation; IDA:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell projection; Cilium;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Ligase;
KW Magnesium; Metal-binding; Microtubule; Neurogenesis; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..887
FT /note="Tubulin polyglutamylase TTLL7"
FT /id="PRO_0000212444"
FT DOMAIN 38..390
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..252
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 388..450
FT /note="c-MTBD region"
FT /evidence="ECO:0000269|PubMed:25959773"
FT REGION 519..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 166..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 188..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25959773"
FT BINDING 201..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25959773"
FT BINDING 227
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 249..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 271
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 367
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 106
FT /note="Binds negatively charged residues of beta-tubulin C-
FT terminal tails"
FT /evidence="ECO:0000269|PubMed:25959773"
FT SITE 352
FT /note="Binds negatively charged residues of beta-tubulin C-
FT terminal tails"
FT /evidence="ECO:0000269|PubMed:25959773"
FT VAR_SEQ 665..669
FT /note="SESLR -> IILAQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015199"
FT VAR_SEQ 670..887
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015200"
FT VAR_SEQ 791..792
FT /note="SS -> YV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015201"
FT VAR_SEQ 793..887
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015202"
FT MUTAGEN 106
FT /note="R->E: Nearly abolished polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 143..146
FT /note="NYVK->EYVE: 70% decreased polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 178
FT /note="K->E: Decreased polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 205
FT /note="R->E: Nearly abolished polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 227
FT /note="R->E: Nearly abolished polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 271
FT /note="K->E: Nearly abolished polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 349
FT /note="E->Q: Loss of polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 352
FT /note="R->A,E: Nearly abolished polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 385..393
FT /note="KRRNLAKQK->EEENLAEQE: 45% decreased binding to
FT microtubules. Decreased polyglutamylase activity. 76%
FT decreased binding to microtubules; when associated with
FT 425-E--E-427."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 425..427
FT /note="RRK->EEE: 76% decreased binding to microtubules;
FT when associated with 385-E--E-393."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 477..480
FT /note="FQTF->AQTA: 40% decreased polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT MUTAGEN 490..500
FT /note="RELNNPLKRMK->DELNNPLDDMD: 69% decreased
FT polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
FT CONFLICT 13
FT /note="P -> S (in Ref. 1; AAO37763)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="T -> A (in Ref. 2; BAC86695)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="L -> M (in Ref. 4; AAH60878)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="Q -> R (in Ref. 4; AAH60878)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="N -> D (in Ref. 4; AAH60878)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="R -> G (in Ref. 4; AAH60878)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="S -> F (in Ref. 2; BAB15526)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="E -> G (in Ref. 4; AAH60878)"
FT /evidence="ECO:0000305"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4YLR"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:4YLR"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4YLR"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:4YLR"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 217..228
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 288..317
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 361..378
FT /evidence="ECO:0007829|PDB:4YLR"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:4YLR"
FT HELIX 463..483
FT /evidence="ECO:0007829|PDB:4YLR"
SQ SEQUENCE 887 AA; 102999 MW; 881C46437FB385EA CRC64;
MPSLPQEGVI QGPSPLDLNT ELPYQSTMKR KVRKKKKKGT ITANVAGTKF EIVRLVIDEM
GFMKTPDEDE TSNLIWCDSA VQQEKISELQ NYQRINHFPG MGEICRKDFL ARNMTKMIKS
RPLDYTFVPR TWIFPAEYTQ FQNYVKELKK KRKQKTFIVK PANGAMGHGI SLIRNGDKLP
SQDHLIVQEY IEKPFLMEGY KFDLRIYILV TSCDPLKIFL YHDGLVRMGT EKYIPPNESN
LTQLYMHLTN YSVNKHNEHF ERDETENKGS KRSIKWFTEF LQANQHDVAK FWSDISELVV
KTLIVAEPHV LHAYRMCRPG QPPGSESVCF EVLGFDILLD RKLKPWLLEI NRAPSFGTDQ
KIDYDVKRGV LLNALKLLNI RTSDKRRNLA KQKAEAQRRL YGQNSIKRLL PGSSDWEQQR
HQLERRKEEL KERLAQVRKQ ISREEHENRH MGNYRRIYPP EDKALLEKYE NLLAVAFQTF
LSGRAASFQR ELNNPLKRMK EEDILDLLEQ CEIDDEKLMG KTTKTRGPKP LCSMPESTEI
MKRPKYCSSD SSYDSSSSSS ESDENEKEEY QNKKREKQVT YNLKPSNHYK LIQQPSSIRR
SVSCPRSISA QSPSSGDTRP FSAQQMISVS RPTSASRSHS LNRASSYMRH LPHSNDACST
NSQVSESLRQ LKTKEQEDDL TSQTLFVLKD MKIRFPGKSD AESELLIEDI IDNWKYHKTK
VASYWLIKLD SVKQRKVLDI VKTSIRTVLP RIWKVPDVEE VNLYRIFNRV FNRLLWSRGQ
GLWNCFCDSG SSWESIFNKS PEVVTPLQLQ CCQRLVELCK QCLLVVYKYA TDKRGSLSGI
GPDWGNSRYL LPGSTQFFLR TPTYNLKYNS PGMTRSNVLF TSRYGHL
