ID   TBA1A_MOUSE             Reviewed;         451 AA.
AC   P68369; P02551; P05210; P05212; Q3TGF0; Q3TIW2; Q3TPJ1; Q3ULN1; Q5XJF8;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Tubulin alpha-1A chain;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
DE   AltName: Full=Alpha-tubulin 1;
DE   AltName: Full=Alpha-tubulin isotype M-alpha-1;
DE   AltName: Full=Tubulin alpha-1 chain;
DE   Contains:
DE     RecName: Full=Detyrosinated tubulin alpha-1A chain;
GN   Name=Tuba1a; Synonyms=Tuba1;
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=C57BL/6J;
RC   TISSUE=Heart, Kidney, Placenta, Spinal ganglion, and Thymus;
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].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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   PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-280; 312-320;
RP   327-336; 340-370; 374-401 AND 403-440, 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   NUCLEOTIDE SEQUENCE [MRNA] OF 254-451.
RX   PubMed=3839797; DOI=10.1083/jcb.101.3.852;
RA   Lewis S.A., Lee M.G.-S., Cowan N.J.;
RT   "Five mouse tubulin isotypes and their regulated expression during
RT   development.";
RL   J. Cell Biol. 101:852-861(1985).
RN   [6]
RP   PROTEIN SEQUENCE OF 440-448, AND GLUTAMYLATION AT GLU-445.
RX   PubMed=1967194; DOI=10.1126/science.1967194;
RA   Edde B., Rossier J., Le Caer J.P., Desbruyeres E., Gros F., Denoulet P.;
RT   "Posttranslational glutamylation of alpha-tubulin.";
RL   Science 247:83-85(1990).
RN   [7]
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   [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   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   [10]
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   [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, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
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   -!- INTERACTION:
CC       P68369; Q80TQ2: Cyld; NbExp=5; IntAct=EBI-400542, EBI-943859;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, although primarily in lung
CC       and brain. {ECO:0000269|PubMed:3785200}.
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:1967194, PubMed:15890843). Polyglutamylation plays a key role
CC       in microtubule severing by spastin (SPAST). SPAST preferentially
CC       recognizes and acts on microtubules decorated with short polyglutamate
CC       tails: severing activity by SPAST increases as the number of glutamates
CC       per tubulin rises from one to eight, but decreases beyond this
CC       glutamylation threshold (By similarity). Glutamylation is also involved
CC       in cilia motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36,
CC       ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:1967194,
CC       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-451 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 (MATCAP, VASH1 or VASH2) and tubulin tyrosine
CC       ligase (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-1A 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-1A 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:Q71U36,
CC       ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; M13445; AAA40499.1; -; mRNA.
DR   EMBL; AK077529; BAC36848.1; -; mRNA.
DR   EMBL; AK145404; BAE26417.1; -; mRNA.
DR   EMBL; AK146983; BAE27586.1; -; mRNA.
DR   EMBL; AK164335; BAE37745.1; -; mRNA.
DR   EMBL; AK167687; BAE39734.1; -; mRNA.
DR   EMBL; AK168762; BAE40598.1; -; mRNA.
DR   EMBL; AK169610; BAE41258.1; -; mRNA.
DR   EMBL; BC056169; AAH56169.1; -; mRNA.
DR   EMBL; BC083343; AAH83343.1; -; mRNA.
DR   EMBL; BC083345; AAH83345.1; -; mRNA.
DR   EMBL; BC085256; AAH85256.1; -; mRNA.
DR   EMBL; M28729; AAA40506.1; -; mRNA.
DR   EMBL; BC083344; AAH83344.1; -; mRNA.
DR   CCDS; CCDS37196.1; -.
DR   PIR; I77424; I77424.
DR   RefSeq; NP_035783.1; NM_011653.2.
DR   PDB; 6JZD; X-ray; 2.48 A; C=437-451.
DR   PDB; 8IXA; EM; 4.20 A; A/B/C/D/E/F/G/H/I=1-451.
DR   PDB; 8IXB; EM; 4.20 A; A/E/F/H=1-451.
DR   PDB; 8TO0; EM; 7.70 A; A5/A7/A9/AM/AO/AQ/AS/AU/AW/AY/Aj/Al/An/Ap/Ar/At/Av/B0/B2/B4/B8/BA/BC/BE/BO/BQ/BS/BU/BW/BY=1-451.
DR   PDBsum; 6JZD; -.
DR   PDBsum; 8IXA; -.
DR   PDBsum; 8IXB; -.
DR   PDBsum; 8TO0; -.
DR   AlphaFoldDB; P68369; -.
DR   EMDB; EMD-35790; -.
DR   EMDB; EMD-41431; -.
DR   SMR; P68369; -.
DR   BioGRID; 204372; 72.
DR   CORUM; P68369; -.
DR   IntAct; P68369; 25.
DR   MINT; P68369; -.
DR   STRING; 10090.ENSMUSP00000094778; -.
DR   GlyGen; P68369; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P68369; -.
DR   PhosphoSitePlus; P68369; -.
DR   SwissPalm; P68369; -.
DR   EPD; P68369; -.
DR   jPOST; P68369; -.
DR   MaxQB; P68369; -.
DR   PaxDb; 10090-ENSMUSP00000094778; -.
DR   PeptideAtlas; P68369; -.
DR   Pumba; P68369; -.
DR   Antibodypedia; 3282; 802 antibodies from 39 providers.
DR   DNASU; 22142; -.
DR   Ensembl; ENSMUST00000097014.7; ENSMUSP00000094778.6; ENSMUSG00000072235.7.
DR   GeneID; 22142; -.
DR   KEGG; mmu:22142; -.
DR   UCSC; uc007xok.1; mouse.
DR   AGR; MGI:98869; -.
DR   CTD; 7846; -.
DR   MGI; MGI:98869; Tuba1a.
DR   VEuPathDB; HostDB:ENSMUSG00000072235; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   GeneTree; ENSGT00950000182825; -.
DR   HOGENOM; CLU_015718_0_0_1; -.
DR   InParanoid; P68369; -.
DR   OMA; TKQTIQF; -.
DR   OrthoDB; 899149at2759; -.
DR   PhylomeDB; P68369; -.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
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-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-MMU-5620924; Intraflagellar transport.
DR   Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
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-8854518; AURKA Activation by TPX2.
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   Reactome; R-MMU-9833482; PKR-mediated signaling.
DR   BioGRID-ORCS; 22142; 12 hits in 59 CRISPR screens.
DR   ChiTaRS; Tuba1a; mouse.
DR   PRO; PR:P68369; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P68369; Protein.
DR   Bgee; ENSMUSG00000072235; Expressed in trigeminal ganglion and 250 other cell types or tissues.
DR   GO; GO:0005879; C:axonemal microtubule; ISO:MGI.
DR   GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IMP:MGI.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IMP:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR   GO; GO:0007098; P:centrosome cycle; IMP:MGI.
DR   GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR   GO; GO:0048853; P:forebrain morphogenesis; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0046785; P:microtubule polymerization; IMP:MGI.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0061744; P:motor behavior; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0140058; P:neuron projection arborization; IMP:MGI.
DR   GO; GO:0072384; P:organelle transport along microtubule; IMP:MGI.
DR   GO; GO:0021859; P:pyramidal neuron differentiation; IMP:MGI.
DR   GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR   GO; GO:1902065; P:response to L-glutamate; IDA:MGI.
DR   GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IDA:MGI.
DR   GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
DR   GO; GO:0001964; P:startle response; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   CDD; cd02186; alpha_tubulin; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF133; TUBULIN ALPHA-1A CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   SWISS-2DPAGE; P68369; -.
DR   Genevisible; P68369; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Hydrolase; Isopeptide bond;
KW   Magnesium; Metal-binding; Methylation; Microtubule; Nitration;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Tubulin alpha-1A chain"
FT                   /id="PRO_0000048120"
FT   CHAIN           1..450
FT                   /note="Detyrosinated tubulin alpha-1A chain"
FT                   /evidence="ECO:0000305|PubMed:26446751,
FT                   ECO:0000305|PubMed:27102488, ECO:0000305|PubMed:29146868"
FT                   /id="PRO_0000437379"
FT   REGION          432..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         11
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         179
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   SITE            451
FT                   /note="Involved in polymerization"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71U36"
FT   MOD_RES         282
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P68373"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68373"
FT   MOD_RES         443
FT                   /note="5-glutamyl polyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:Q71U36"
FT   MOD_RES         445
FT                   /note="5-glutamyl polyglutamate"
FT                   /evidence="ECO:0000269|PubMed:1967194"
FT   MOD_RES         451
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71U36"
FT   CONFLICT        124
FT                   /note="K -> E (in Ref. 2; BAE40598)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="L -> P (in Ref. 2; BAE26417)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="T -> I (in Ref. 2; BAE37745)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="A -> S (in Ref. 3; AAH83344)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="V -> G (in Ref. 2; BAE26417)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   451 AA;  50136 MW;  00F8429A4A10E5FE CRC64;
     MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
     RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
//