TTLL3_MOUSE
ID TTLL3_MOUSE Reviewed; 927 AA.
AC A4Q9E5; Q8BV51; Q8C0Y7; Q8VDS2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Tubulin monoglycylase TTLL3 {ECO:0000303|PubMed:19524510};
DE EC=6.3.2.- {ECO:0000269|PubMed:19524510};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 3 {ECO:0000303|PubMed:19524510};
GN Name=Ttll3 {ECO:0000312|EMBL:CAM84323.1, ECO:0000312|MGI:MGI:2141418};
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAM84323.1};
RC TISSUE=Testis {ECO:0000312|EMBL:CAM84323.1};
RX PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT "A targeted multienzyme mechanism for selective microtubule
RT polyglutamylation.";
RL Mol. Cell 26:437-448(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37878.1};
RC TISSUE=Head {ECO:0000312|EMBL:BAC26459.1}, and
RC Thymus {ECO:0000312|EMBL:BAC37878.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH21404.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH21404.1};
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-647; GLU-662 AND MET-669.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23897886; DOI=10.1083/jcb.201305041;
RA Bosch Grau M., Gonzalez Curto G., Rocha C., Magiera M.M., Marques Sousa P.,
RA Giordano T., Spassky N., Janke C.;
RT "Tubulin glycylases and glutamylases have distinct functions in
RT stabilization and motility of ependymal cilia.";
RL J. Cell Biol. 202:441-451(2013).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25180231; DOI=10.15252/embj.201488466;
RA Rocha C., Papon L., Cacheux W., Marques Sousa P., Lascano V., Tort O.,
RA Giordano T., Vacher S., Lemmers B., Mariani P., Meseure D., Medema J.P.,
RA Bieche I., Hahne M., Janke C.;
RT "Tubulin glycylases are required for primary cilia, control of cell
RT proliferation and tumor development in colon.";
RL EMBO J. 33:2247-2260(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=33414192; DOI=10.1126/science.abd4914;
RA Gadadhar S., Alvarez Viar G., Hansen J.N., Gong A., Kostarev A.,
RA Ialy-Radio C., Leboucher S., Whitfield M., Ziyyat A., Toure A., Alvarez L.,
RA Pigino G., Janke C.;
RT "Tubulin glycylation controls axonemal dynein activity, flagellar beat, and
RT male fertility.";
RL Science 371:0-0(2021).
CC -!- FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding
CC a single glycine on the gamma-carboxyl groups of specific glutamate
CC residues to generate monoglycine side chains within the C-terminal tail
CC of tubulin (PubMed:19524510). Not involved in elongation step of the
CC polyglycylation reaction (PubMed:19524510). Preferentially glycylates a
CC beta-tail peptide over the alpha-tail, although shifts its preference
CC toward alpha-tail as beta-tail glutamylation increases (By similarity).
CC Competes with polyglutamylases for modification site on beta-tubulin
CC substrate, thereby creating an anticorrelation between glycylation and
CC glutamylation reactions (PubMed:33414192). Together with TTLL8,
CC mediates microtubule glycylation of primary and motile cilia, which is
CC essential for their stability and maintenance (PubMed:23897886,
CC PubMed:25180231). Involved in microtubule glycylation of primary cilia
CC in colon which controls cell proliferation of epithelial cells and
CC plays an essential role in colon cancer development (PubMed:25180231).
CC Together with TTLL8, glycylates sperm flagella which regulates axonemal
CC dynein motor activity, thereby controlling flagellar beat, directional
CC sperm swimming and male fertility (PubMed:33414192).
CC {ECO:0000250|UniProtKB:B2GUB3, ECO:0000269|PubMed:19524510,
CC ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:25180231,
CC ECO:0000269|PubMed:33414192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-
CC glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180,
CC Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:19524510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181;
CC Evidence={ECO:0000305|PubMed:19524510};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19524510}. Cell projection, cilium
CC {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000305|PubMed:33414192}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:17499049};
CC IsoId=A4Q9E5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=A4Q9E5-2; Sequence=VSP_052724, VSP_052725, VSP_052726;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=A4Q9E5-3; Sequence=VSP_052722, VSP_052723;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and testis
CC (PubMed:17499049, PubMed:25180231). Expressed in heart, kidney, liver,
CC lung, muscle, spleen, trachea and colon (PubMed:17499049,
CC PubMed:25180231, PubMed:33414192). Expressed in sperm flagellum
CC (PubMed:33414192). In the brain, specifically expressed in ependymal
CC cilia (PubMed:23897886). {ECO:0000269|PubMed:17499049,
CC ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:25180231,
CC ECO:0000269|PubMed:33414192}.
CC -!- DOMAIN: Two conserved structural elements specific among
CC monoglycylases, IS1 and IS2, are involved in glycyl chains initiation.
CC Two conserved structural interfaces likely constitute the binding
CC platforms for tubulin tail and microtubule.
CC {ECO:0000250|UniProtKB:B2GUB3}.
CC -!- DOMAIN: Arg-482 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 -!- DISRUPTION PHENOTYPE: In knockout mice, colon epithelium shows absence
CC of glycylation, a reduced number of primary cilia accompanied by an
CC increased rate of cell division (PubMed:25180231). Knockout mice show
CC no visible motile ependymal cilia phenotype (PubMed:23897886).
CC Simultaneous TTLL3 and TTLL8 knockout mice are subfertile owing to
CC aberrant beat patterns of their sperm flagella, which impeded the
CC straight swimming of sperm cells (PubMed:33414192). Simultaneous TTLL3
CC and TTLL8 knockout mice show no visible motile ependymal cilia
CC phenotype in brain ventricles (PubMed:33414192).
CC {ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:25180231,
CC ECO:0000269|PubMed:33414192}.
CC -!- CAUTION: TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin
CC was initially reported to play a role in ependymal motile ciliary
CC maintenance (PubMed:23897886). However, contradictory results were
CC later observed (PubMed:33414192). {ECO:0000269|PubMed:23897886,
CC ECO:0000269|PubMed:33414192}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM690746; CAM84323.1; -; mRNA.
DR EMBL; AK029462; BAC26459.1; -; mRNA.
DR EMBL; AK080321; BAC37878.1; -; mRNA.
DR EMBL; BC021404; AAH21404.1; -; mRNA.
DR CCDS; CCDS39593.2; -. [A4Q9E5-1]
DR CCDS; CCDS85118.1; -. [A4Q9E5-2]
DR RefSeq; NP_001136204.1; NM_001142732.1. [A4Q9E5-2]
DR RefSeq; NP_598684.4; NM_133923.6. [A4Q9E5-1]
DR AlphaFoldDB; A4Q9E5; -.
DR SMR; A4Q9E5; -.
DR IntAct; A4Q9E5; 1.
DR STRING; 10090.ENSMUSP00000032414; -.
DR iPTMnet; A4Q9E5; -.
DR PhosphoSitePlus; A4Q9E5; -.
DR PaxDb; A4Q9E5; -.
DR PRIDE; A4Q9E5; -.
DR ProteomicsDB; 298014; -. [A4Q9E5-1]
DR ProteomicsDB; 298016; -. [A4Q9E5-3]
DR Antibodypedia; 74193; 4 antibodies from 4 providers.
DR Ensembl; ENSMUST00000032414; ENSMUSP00000032414; ENSMUSG00000030276. [A4Q9E5-1]
DR Ensembl; ENSMUST00000204026; ENSMUSP00000145049; ENSMUSG00000030276. [A4Q9E5-2]
DR GeneID; 101100; -.
DR KEGG; mmu:101100; -.
DR UCSC; uc009dfu.2; mouse. [A4Q9E5-2]
DR UCSC; uc009dfv.2; mouse. [A4Q9E5-1]
DR UCSC; uc009dfw.1; mouse. [A4Q9E5-3]
DR CTD; 26140; -.
DR MGI; MGI:2141418; Ttll3.
DR VEuPathDB; HostDB:ENSMUSG00000030276; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000154857; -.
DR InParanoid; A4Q9E5; -.
DR OMA; HHMGRLR; -.
DR OrthoDB; 1137333at2759; -.
DR PhylomeDB; A4Q9E5; -.
DR TreeFam; TF313087; -.
DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin.
DR BioGRID-ORCS; 101100; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ttll3; mouse.
DR PRO; PR:A4Q9E5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; A4Q9E5; protein.
DR Bgee; ENSMUSG00000030276; Expressed in granulocyte and 146 other tissues.
DR ExpressionAtlas; A4Q9E5; baseline and differential.
DR Genevisible; A4Q9E5; MM.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; IDA:UniProtKB.
DR GO; GO:0070736; F:protein-glycine ligase activity, initiating; IDA:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IGI:MGI.
DR GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0018094; P:protein polyglycylation; IDA:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027753; TTLL3.
DR PANTHER; PTHR45870:SF1; PTHR45870:SF1; 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..927
FT /note="Tubulin monoglycylase TTLL3"
FT /id="PRO_0000326159"
FT DOMAIN 345..702
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 35..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 482..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 482
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 514..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B2GUB3"
FT BINDING 527..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 571..572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 649
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B2GUB3"
FT BINDING 662
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 662
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 664
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 482
FT /note="Essential for specifying initiation versus
FT elongation step of the polyglycylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT VAR_SEQ 1..223
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052722"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052724"
FT VAR_SEQ 224..253
FT /note="EENEMFRESQLLDLDGFLEFDDLDGIHALM -> MDTSSPFYAAGQGEASPP
FT SLPVSISSPSLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052723"
FT VAR_SEQ 335..435
FT /note="EDFWLTAARNVLKLVVKLEEKSQSISIQAREEEAPEDTQPKKQEKKLVTVSS
FT DFVDEALSACQEHLSSIAHKDIDKDPNSPLYLSPDDWSQFLQRYYQIVH -> GKGTPI
FT PGLAPSCCLSHRGKEQASPCGLCNPSPFLLPMGLPFISQPWHSEKPREPGLYPVAGSRG
FT GWVGSVWSLDKLLAGPGSTKGNGSLRQSKFLFQHGF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052725"
FT VAR_SEQ 436..927
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052726"
FT MUTAGEN 647
FT /note="G->S: Loss of tubulin monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:19524510"
FT MUTAGEN 662
FT /note="E->G: Loss of tubulin monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:19524510"
FT MUTAGEN 669
FT /note="M->I: Loss of tubulin monoglycylation activity."
FT /evidence="ECO:0000269|PubMed:19524510"
FT CONFLICT 214
FT /note="D -> N (in Ref. 2; BAC26459)"
FT /evidence="ECO:0000305"
FT CONFLICT A4Q9E5-2:241
FT /note="P -> Q (in Ref. 2; BAC26459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 927 AA; 104428 MW; 9E04C14CABD8B311 CRC64;
MQGVSSALLL SAGQLGPGAA WYRQEGSSEC SWLRRSQPSE LRTNFSSRWP WPRNSESRRS
ERLQWPGPAS AKPEVASCGD SRRDYSSLPA RHLSSARESS MPGALGTVNP QPVRTLVPPT
LDEPLPDALR PPDDSLLLWR GLTKGPNHMG RLRNAKIHVE RAVKQKKIFM IHGRYPVIRC
LLRQRGWVEK KMVHPPGTAL PAPQKDLDSS MLGDSDATED EDEEENEMFR ESQLLDLDGF
LEFDDLDGIH ALMSRMVRNE TPYLIWTTRR DVLDCRFLSK DQMINHYARA GSFTTKVGLC
LNLRNLPWFD EADADSFFPR CYRLGAEDDK KAFIEDFWLT AARNVLKLVV KLEEKSQSIS
IQAREEEAPE DTQPKKQEKK LVTVSSDFVD EALSACQEHL SSIAHKDIDK DPNSPLYLSP
DDWSQFLQRY YQIVHEGAEL RYLEVQVQRC EDILQQLQNV VPQLDMEGDR NIWIVKPGAK
SRGRGIMCMN RLDEMLKLVD CNPMLMKDGK WIVQKYIERP LLIFGTKFDL RQWFLVTDWN
PLTVWFYRDS YIRFSTQPFS LKNLDNSVHL CNNSIQRHLE ASCHRHPMLP PDNMWSSQRF
QAHLQEVDAP KAWSSVIVPG MKAAVIHALQ TSQDNVQCRK ASFELYGADF VFGEDFQPWL
IEINASPTMA PSTAVTARLC AGVQADTLRV VIDRRLDRSC DTGAFELIYK QPAVEVPQYV
GIRLLVEGST IKKPVPVGHR RTGVRSSLPH LLTQQGSGES KDSGSPTHRS ASRKNARAES
LEHTEKPEPA AVASVSGKGK KAPFHFPSLH SKAWLPSPRV HRPQGRVLRL QHDQLVGSKA
LSTTGKALMT LPTAKVLMSF PPHPDLKLAP SMLKPGKVGF ELCCTTWRVV LSGGIGEEGH
RQRAAPRPSS APGKGLSSTE PCSKTET
