TTLL1_HUMAN
ID TTLL1_HUMAN Reviewed; 423 AA.
AC O95922; B2RDS7; Q9BR27; Q9NRS9; Q9UMU0;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Polyglutamylase complex subunit TTLL1 {ECO:0000250|UniProtKB:Q91V51};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q91V51};
DE AltName: Full=Tubulin polyglutamylase TTLL1;
DE AltName: Full=Tubulin polyglutamylase complex subunit 3 {ECO:0000250|UniProtKB:Q91V51};
DE Short=PGs3 {ECO:0000250|UniProtKB:Q91V51};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 1 {ECO:0000250|UniProtKB:Q91V51};
GN Name=TTLL1 {ECO:0000312|HGNC:HGNC:1312}; Synonyms=C22orf7;
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] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
RX PubMed=11054573; DOI=10.1016/s0378-1119(00)00383-8;
RA Trichet V., Ruault M., Roizes G., De Sario A.;
RT "Characterization of the human tubulin tyrosine ligase-like 1 gene (TTLL1)
RT mapping to 22q13.1.";
RL Gene 257:109-117(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND 4).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Eye;
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 [9]
RP INTERACTION WITH PCM1; CSTPP1 AND LRRC49, FUNCTION, AND MUTAGENESIS OF
RP GLU-326.
RX PubMed=34782749; DOI=10.1038/s41422-021-00584-9;
RA Wang L., Paudyal S.C., Kang Y., Owa M., Liang F.X., Spektor A., Knaut H.,
RA Sanchez I., Dynlacht B.D.;
RT "Regulators of tubulin polyglutamylation control nuclear shape and cilium
RT disassembly by balancing microtubule and actin assembly.";
RL Cell Res. 32:190-209(2022).
CC -!- FUNCTION: Catalytic subunit of a polyglutamylase complex which modifies
CC tubulin, generating side chains of glutamate on the gamma-carboxyl
CC group of specific glutamate residues within the C-terminal tail of
CC tubulin (PubMed:34782749). Probably involved in the side-chain
CC elongation step of the polyglutamylation reaction rather than the
CC initiation step. Modifies both alpha- and beta-tubulins with a
CC preference for the alpha-tail. Unlike most polyglutamylases of the
CC tubulin--tyrosine ligase family, only displays a catalytic activity
CC when in complex with other proteins as it is most likely lacking
CC domains important for autonomous activity. Part of the neuronal tubulin
CC polyglutamylase complex. Mediates cilia and flagella polyglutamylation
CC which is essential for their biogenesis and motility. Involved in
CC respiratory motile cilia function through the regulation of beating
CC asymmetry. Essential for sperm flagella biogenesis, motility and male
CC fertility. Involved in KLF4 glutamylation which impedes its
CC ubiquitination, thereby leading to somatic cell reprogramming,
CC pluripotency maintenance and embryogenesis.
CC {ECO:0000250|UniProtKB:Q91V51, ECO:0000269|PubMed:34782749}.
CC -!- CATALYTIC ACTIVITY:
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:0000250|UniProtKB:Q91V51};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000250|UniProtKB:Q91V51};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which
CC contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. Interacts with PCM1,
CC CSTPP1 and LRRC49 (PubMed:34782749). {ECO:0000250|UniProtKB:Q91V51,
CC ECO:0000269|PubMed:34782749}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium
CC axoneme {ECO:0000250|UniProtKB:Q91V51}. Cell projection, cilium,
CC flagellum {ECO:0000250|UniProtKB:Q91V51}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=A; Synonyms=TTLL1a;
CC IsoId=O95922-1; Sequence=Displayed;
CC Name=B; Synonyms=TTLL1b, Truncated;
CC IsoId=O95922-2; Sequence=VSP_006671, VSP_006672;
CC Name=4;
CC IsoId=O95922-4; Sequence=VSP_011825;
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues. Has a
CC stronger expression in heart, brain and testis.
CC {ECO:0000269|PubMed:11054573}.
CC -!- DOMAIN: Gln-144 is the main determinant for regioselectivity, which
CC segregates between initiases and elongases in all tubulin--tyrosine
CC ligase family. A glutamine residue at this position is found in
CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC chain elongation, whereas an arginine residue is found in initiases
CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC {ECO:0000250|UniProtKB:A4Q9E8}.
CC -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB51423.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AF104927; AAG29879.1; -; mRNA.
DR EMBL; AF173935; AAF91088.1; -; mRNA.
DR EMBL; AL136687; CAB66622.1; -; mRNA.
DR EMBL; AL096883; CAB51423.1; ALT_SEQ; mRNA.
DR EMBL; AL096886; CAB51469.1; -; mRNA.
DR EMBL; AL589867; CAC34478.1; -; mRNA.
DR EMBL; CR456599; CAG30485.1; -; mRNA.
DR EMBL; AK315658; BAG38024.1; -; mRNA.
DR EMBL; AL022476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73279.1; -; Genomic_DNA.
DR EMBL; BC014968; AAH14968.1; -; mRNA.
DR CCDS; CCDS14043.1; -. [O95922-1]
DR RefSeq; NP_036395.1; NM_012263.4. [O95922-1]
DR RefSeq; XP_011528410.1; XM_011530108.2.
DR RefSeq; XP_016884240.1; XM_017028751.1. [O95922-1]
DR RefSeq; XP_016884241.1; XM_017028752.1. [O95922-1]
DR RefSeq; XP_016884242.1; XM_017028753.1.
DR AlphaFoldDB; O95922; -.
DR SMR; O95922; -.
DR BioGRID; 117340; 25.
DR IntAct; O95922; 20.
DR STRING; 9606.ENSP00000266254; -.
DR iPTMnet; O95922; -.
DR PhosphoSitePlus; O95922; -.
DR BioMuta; TTLL1; -.
DR EPD; O95922; -.
DR jPOST; O95922; -.
DR MassIVE; O95922; -.
DR PaxDb; O95922; -.
DR PeptideAtlas; O95922; -.
DR PRIDE; O95922; -.
DR ProteomicsDB; 51124; -. [O95922-1]
DR ProteomicsDB; 51125; -. [O95922-2]
DR ProteomicsDB; 51126; -. [O95922-4]
DR Antibodypedia; 27458; 42 antibodies from 19 providers.
DR DNASU; 25809; -.
DR Ensembl; ENST00000266254.12; ENSP00000266254.7; ENSG00000100271.17. [O95922-1]
DR Ensembl; ENST00000331018.8; ENSP00000333734.7; ENSG00000100271.17. [O95922-4]
DR Ensembl; ENST00000439248.5; ENSP00000401518.1; ENSG00000100271.17. [O95922-2]
DR Ensembl; ENST00000440761.1; ENSP00000403332.1; ENSG00000100271.17. [O95922-2]
DR GeneID; 25809; -.
DR KEGG; hsa:25809; -.
DR MANE-Select; ENST00000266254.12; ENSP00000266254.7; NM_012263.5; NP_036395.1.
DR UCSC; uc003bdi.5; human. [O95922-1]
DR CTD; 25809; -.
DR DisGeNET; 25809; -.
DR GeneCards; TTLL1; -.
DR HGNC; HGNC:1312; TTLL1.
DR HPA; ENSG00000100271; Low tissue specificity.
DR MIM; 608955; gene.
DR neXtProt; NX_O95922; -.
DR OpenTargets; ENSG00000100271; -.
DR PharmGKB; PA35030; -.
DR VEuPathDB; HostDB:ENSG00000100271; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000156720; -.
DR HOGENOM; CLU_2960116_0_0_1; -.
DR InParanoid; O95922; -.
DR OMA; TMYGRLP; -.
DR PhylomeDB; O95922; -.
DR TreeFam; TF313087; -.
DR PathwayCommons; O95922; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; O95922; -.
DR BioGRID-ORCS; 25809; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; TTLL1; human.
DR GeneWiki; TTLL1; -.
DR GenomeRNAi; 25809; -.
DR Pharos; O95922; Tdark.
DR PRO; PR:O95922; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O95922; protein.
DR Bgee; ENSG00000100271; Expressed in cortical plate and 149 other tissues.
DR ExpressionAtlas; O95922; baseline and differential.
DR Genevisible; O95922; HS.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
DR GO; GO:0002395; P:immune response in nasopharyngeal-associated lymphoid tissue; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0120197; P:mucociliary clearance; IEA:Ensembl.
DR GO; GO:0018095; P:protein polyglutamylation; IBA:GO_Central.
DR GO; GO:0120222; P:regulation of blastocyst development; IEA:Ensembl.
DR GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027750; TTLL1.
DR PANTHER; PTHR12241:SF31; PTHR12241:SF31; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Flagellum; Ligase; Magnesium; Metal-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..423
FT /note="Polyglutamylase complex subunit TTLL1"
FT /id="PRO_0000212438"
FT DOMAIN 1..367
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 243..244
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 391..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 144..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 144
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 181..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 194..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 220
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 241..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 259
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 344
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 144
FT /note="Essential for specifying alpha-elongation versus
FT initiation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT VAR_SEQ 39..59
FT /note="MSVQTIRNVFSVEAGYRLSDD -> LLDLPEFRYRSCLNEFPDFRV (in
FT isoform B)"
FT /evidence="ECO:0000303|PubMed:11054573,
FT ECO:0000303|PubMed:12529303"
FT /id="VSP_006671"
FT VAR_SEQ 60..423
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11054573,
FT ECO:0000303|PubMed:12529303"
FT /id="VSP_006672"
FT VAR_SEQ 298..326
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12529303"
FT /id="VSP_011825"
FT VARIANT 168
FT /note="S -> L (in dbSNP:rs6003030)"
FT /id="VAR_052409"
FT MUTAGEN 326
FT /note="E->G: Abolishes microtubule polyglutamylation.
FT Decreases MAP4 recruitment to microtubules."
FT /evidence="ECO:0000269|PubMed:34782749"
SQ SEQUENCE 423 AA; 48988 MW; AFFDEEE008D2E655 CRC64;
MAGKVKWVTD IEKSVLINNF EKRGWVQVTE NEDWNFYWMS VQTIRNVFSV EAGYRLSDDQ
IVNHFPNHYE LTRKDLMVKN IKRYRKELEK EGSPLAEKDE NGKYLYLDFV PVTYMLPADY
NLFVEEFRKS PSSTWIMKPC GKAQGKGIFL INKLSQIKKW SRDSKTSSFV SQSNKEAYVI
SLYINNPLLI GGRKFDLRLY VLVSTYRPLR CYMYKLGFCR FCTVKYTPST SELDNMFVHL
TNVAIQKHGE DYNHIHGGKW TVSNLRLYLE STRGKEVTSK LFDEIHWIIV QSLKAVAPVM
NNDKHCFECY GYDIIIDDKL KPWLIEVNAS PSLTSSTAND RILKYNLIND TLNIAVPNGE
IPDCKWNKSP PKEVLGNYEI LYDEELAQGD GADRELRSRQ GQSLGPRAGR SRDSGRAVLT
TWK
