TBA1C_MOUSE
ID TBA1C_MOUSE Reviewed; 449 AA.
AC P68373; P05216; Q9CSE9;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Tubulin alpha-1C chain;
DE AltName: Full=Alpha-tubulin 6;
DE AltName: Full=Alpha-tubulin isotype M-alpha-6;
DE AltName: Full=Tubulin alpha-6 chain;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha-1C chain;
GN Name=Tuba1c; Synonyms=Tuba6;
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], AND TISSUE SPECIFICITY.
RX PubMed=3785200; DOI=10.1128/mcb.6.7.2409-2419.1986;
RA Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.;
RT "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-
RT specific expression of two sister genes.";
RL Mol. Cell. Biol. 6:2409-2419(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-449.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-280; 312-320;
RP 327-336; 340-370; 374-390; 395-401 AND 403-430, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP GLUTAMYLATION.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
RN [6]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-282, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [7]
RP GLYCYLATION.
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 [8]
RP TYROSINATION.
RX PubMed=16954346; DOI=10.1083/jcb.200512058;
RA Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K.,
RA Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J.,
RA Andrieux A., Job D.;
RT "Tubulin tyrosination is a major factor affecting the recruitment of CAP-
RT Gly proteins at microtubule plus ends.";
RL J. Cell Biol. 174:839-849(2006).
RN [9]
RP TYROSINATION.
RX PubMed=19564401; DOI=10.1083/jcb.200902142;
RA Peris L., Wagenbach M., Lafanechere L., Brocard J., Moore A.T.,
RA Kozielski F., Job D., Wordeman L., Andrieux A.;
RT "Motor-dependent microtubule disassembly driven by tubulin tyrosination.";
RL J. Cell Biol. 185:1159-1166(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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 [11]
RP GLYCYLATION, AND GLUTAMYLATION.
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 [12]
RP DETYROSINATION.
RX PubMed=26446751; DOI=10.1038/ncomms9526;
RA Kerr J.P., Robison P., Shi G., Bogush A.I., Kempema A.M., Hexum J.K.,
RA Becerra N., Harki D.A., Martin S.S., Raiteri R., Prosser B.L., Ward C.W.;
RT "Detyrosinated microtubules modulate mechanotransduction in heart and
RT skeletal muscle.";
RL Nat. Commun. 6:8526-8526(2015).
RN [13]
RP DETYROSINATION.
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).
RN [14]
RP DETYROSINATION.
RX PubMed=29146868; DOI=10.1126/science.aao4165;
RA Aillaud C., Bosc C., Peris L., Bosson A., Heemeryck P., Van Dijk J.,
RA Le Friec J., Boulan B., Vossier F., Sanman L.E., Syed S., Amara N.,
RA Coute Y., Lafanechere L., Denarier E., Delphin C., Pelletier L.,
RA Humbert S., Bogyo M., Andrieux A., Rogowski K., Moutin M.J.;
RT "Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron
RT differentiation.";
RL Science 358:1448-1453(2017).
RN [15]
RP GLYCYLATION.
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: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Minor alpha-tubulin expressed in all tissues.
CC {ECO:0000269|PubMed:3785200}.
CC -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P68363}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm motility
CC (PubMed:33414192). {ECO:0000269|PubMed:19524510,
CC ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:15890843). Polyglutamylation plays a key role in microtubule
CC severing by spastin (SPAST). SPAST preferentially recognizes and acts
CC on microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (By similarity). Glutamylation is also involved in cilia
CC motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36,
CC ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:23897886}.
CC -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
CC microtubule lumen. This modification has been correlated with increased
CC microtubule stability, intracellular transport and ciliary assembly.
CC {ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
CC microtubules and is required for normal mitosis and cytokinesis
CC contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.
CC -!- PTM: Nitration of Tyr-449 is irreversible and interferes with normal
CC dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase
CC (TTL), respectively. {ECO:0000269|PubMed:16954346,
CC ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751,
CC ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}.
CC -!- PTM: [Tubulin alpha-1C chain]: Tyrosination promotes microtubule
CC interaction with CAP-Gly domain-containing proteins such as CLIP1,
CC CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination
CC regulates the initiation of dynein-dynactin motility via interaction
CC with DCTN1, which brings the dynein-dynactin complex into contact with
CC microtubules. In neurons, tyrosinated tubulins mediate the initiation
CC of retrograde vesicle transport (By similarity).
CC {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346,
CC ECO:0000269|PubMed:19564401}.
CC -!- PTM: [Detyrosinated tubulin alpha-1C chain]: Detyrosination is involved
CC in metaphase plate congression by guiding chromosomes during mitosis:
CC detyrosination promotes interaction with CENPE, promoting pole-proximal
CC transport of chromosomes toward the equator (By similarity).
CC Detyrosination increases microtubules-dependent mechanotransduction in
CC dystrophic cardiac and skeletal muscle (PubMed:26446751). In
CC cardiomyocytes, detyrosinated microtubules are required to resist to
CC contractile compression during contraction: detyrosination promotes
CC association with desmin (DES) at force-generating sarcomeres, leading
CC to buckled microtubules and mechanical resistance to contraction
CC (PubMed:27102488). {ECO:0000250|UniProtKB:Q9BQE3,
CC ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M13441; AAA40503.1; -; mRNA.
DR EMBL; BC004745; AAH04745.1; -; mRNA.
DR EMBL; BC022182; AAH22182.1; -; mRNA.
DR EMBL; BC026753; AAH26753.1; -; mRNA.
DR EMBL; AK013029; BAB28608.1; -; mRNA.
DR CCDS; CCDS37198.1; -.
DR PIR; I77428; I77428.
DR PIR; PH0108; PH0108.
DR RefSeq; NP_033474.1; NM_009448.4.
DR AlphaFoldDB; P68373; -.
DR SMR; P68373; -.
DR BioGRID; 204376; 15.
DR IntAct; P68373; 12.
DR STRING; 10090.ENSMUSP00000051033; -.
DR iPTMnet; P68373; -.
DR PhosphoSitePlus; P68373; -.
DR SwissPalm; P68373; -.
DR REPRODUCTION-2DPAGE; P68373; -.
DR SWISS-2DPAGE; P99040; -.
DR EPD; P68373; -.
DR jPOST; P68373; -.
DR PaxDb; P68373; -.
DR PeptideAtlas; P68373; -.
DR PRIDE; P68373; -.
DR ProteomicsDB; 263128; -.
DR TopDownProteomics; P68373; -.
DR Ensembl; ENSMUST00000058914; ENSMUSP00000051033; ENSMUSG00000043091.
DR GeneID; 22146; -.
DR KEGG; mmu:22146; -.
DR UCSC; uc007xom.1; mouse.
DR CTD; 84790; -.
DR MGI; MGI:1095409; Tuba1c.
DR VEuPathDB; HostDB:ENSMUSG00000043091; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00950000182825; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P68373; -.
DR OMA; FYTRECI; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; P68373; -.
DR TreeFam; TF300314; -.
DR Reactome; R-MMU-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5617833; Cilium Assembly.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 22146; 15 hits in 43 CRISPR screens.
DR ChiTaRS; Tuba1c; mouse.
DR PRO; PR:P68373; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P68373; protein.
DR Bgee; ENSMUSG00000043091; Expressed in ectoplacental cone and 209 other tissues.
DR ExpressionAtlas; P68373; baseline and differential.
DR Genevisible; P68373; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW GTP-binding; Methylation; Microtubule; Nitration; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..449
FT /note="Tubulin alpha-1C chain"
FT /id="PRO_0000048124"
FT CHAIN 1..448
FT /note="Detyrosinated tubulin alpha-1C chain"
FT /evidence="ECO:0000305|PubMed:26446751,
FT ECO:0000305|PubMed:27102488, ECO:0000305|PubMed:29146868"
FT /id="PRO_0000437395"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 449
FT /note="Involved in polymerization"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE3"
FT MOD_RES 282
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 432
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE3"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 449
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT CONFLICT 167
FT /note="L -> P (in Ref. 3; BAB28608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49909 MW; 0DA9F082D9DC8549 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGADSA EGDDEGEEY
