ID TBA3_MOUSE Reviewed; 450 AA. AC P05214; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 14-OCT-2015, entry version 144. DE RecName: Full=Tubulin alpha-3 chain; DE AltName: Full=Alpha-tubulin 3/7; DE AltName: Full=Alpha-tubulin isotype M-alpha-3/7; DE AltName: Full=Tubulin alpha-3/alpha-7 chain; GN Name=Tuba3a; Synonyms=Tuba3; GN and GN Name=Tuba3b; Synonyms=Tuba7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=3785200; 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 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 230-280, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [4] 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., RA Suryavanshi S., Gaertig J., Edde B.; RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein RT family."; RL Science 308:1758-1762(2005). RN [5] 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., RA Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., RA Janke C.; RT "Evolutionary divergence of enzymatic mechanisms for posttranslational RT polyglycylation."; RL Cell 137:1076-1087(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a non-exchangeable site on the alpha chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is CC a hollow water-filled tube with an outer diameter of 25 nm and an CC inner diameter of 15 nM. Alpha-beta heterodimers associate head- CC to-tail to form protofilaments running lengthwise along the CC microtubule wall with the beta-tubulin subunit facing the CC microtubule plus end conferring a structural polarity. CC Microtubules usually have 13 protofilaments but different CC protofilament numbers can be found in some organisms and CC specialized cells. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Alpha-3 and alpha-7 are identical but coded by CC two different genes, they are testis-specific. CC {ECO:0000269|PubMed:3785200}. CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic CC removal and re-addition of a C-terminal tyrosine residue by the CC enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin CC tyrosine ligase (TTL), respectively. {ECO:0000250}. CC -!- PTM: Some glutamate residues at the C-terminus are either CC polyglutamylated or polyglycylated. These 2 modifications occur CC exclusively on glutamate residues and result in either CC polyglutamate or polyglycine chains on the gamma-carboxyl group. CC Glycylation is mainly limited to tubulin incorporated into CC axonemes (cilia and flagella) whereas glutamylation is prevalent CC in neuronal cells, centrioles, axonemes, and the mitotic spindle. CC Both modifications can coexist on the same protein on adjacent CC residues, and lowering polyglycylation levels increases CC polyglutamylation, and reciprocally. The precise function of such CC modifications is still unclear but they are regulate the assembly CC and dynamics of axonemal microtubules. CC -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules CC and affects affinity and processivity of microtubule motors. This CC modification has a role in multiple cellular functions, ranging CC from cell motility, cell cycle progression or cell differentiation CC to intracellular trafficking and signaling (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}. 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; M13442; AAA40501.1; -; mRNA. DR EMBL; M13443; AAA40504.1; -; mRNA. DR EMBL; BC050769; AAH50769.1; -; mRNA. DR EMBL; BC050770; AAH50770.1; -; mRNA. DR CCDS; CCDS39640.1; -. DR CCDS; CCDS39707.1; -. DR PIR; I77426; I77426. DR RefSeq; NP_033472.1; NM_009446.2. DR RefSeq; NP_033475.1; NM_009449.3. DR UniGene; Mm.270295; -. DR UniGene; Mm.287784; -. DR ProteinModelPortal; P05214; -. DR SMR; P05214; 1-440. DR BioGrid; 204374; 2. DR STRING; 10090.ENSMUSP00000085580; -. DR BindingDB; P05214; -. DR PhosphoSite; P05214; -. DR REPRODUCTION-2DPAGE; P05214; -. DR MaxQB; P05214; -. DR PRIDE; P05214; -. DR GeneID; 22144; -. DR GeneID; 22147; -. DR KEGG; mmu:22144; -. DR KEGG; mmu:22147; -. DR UCSC; uc009dui.1; mouse. DR CTD; 22144; -. DR CTD; 22147; -. DR MGI; MGI:1095406; Tuba3a. DR MGI; MGI:1095408; Tuba3b. DR HOGENOM; HOG000165711; -. DR HOVERGEN; HBG000089; -. DR InParanoid; P05214; -. DR KO; K07374; -. DR OMA; NDQSECE; -. DR OrthoDB; EOG7TBC1W; -. DR PhylomeDB; P05214; -. DR TreeFam; TF300314; -. DR Reactome; R-MMU-1445148; Translocation of GLUT4 to the plasma membrane. DR Reactome; R-MMU-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane. DR Reactome; R-MMU-190861; Gap junction assembly. 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-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-MMU-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-MMU-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-MMU-389977; Post-chaperonin tubulin folding pathway. DR Reactome; R-MMU-437239; Recycling pathway of L1. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5617833; Assembly of the primary cilium. DR Reactome; R-MMU-5620924; Intraflagellar transport. DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-MMU-5632684; Hedgehog 'on' state. DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins. DR Reactome; R-MMU-68877; Mitotic Prometaphase. DR Reactome; R-MMU-983189; Kinesins. DR ChiTaRS; Tuba3a; mouse. DR NextBio; 302046; -. DR PRO; PR:P05214; -. DR Proteomes; UP000000589; Unplaced. DR Bgee; P05214; -. DR CleanEx; MM_TUBA3A; -. DR CleanEx; MM_TUBA3B; -. DR ExpressionAtlas; P05214; baseline and differential. DR Genevisible; P05214; MM. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro. DR GO; GO:0051258; P:protein polymerization; IEA:InterPro. 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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. 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; Complete proteome; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; GTP-binding; Microtubule; Nitration; KW Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1 450 Tubulin alpha-3 chain. FT /FTId=PRO_0000048122. FT NP_BIND 142 148 GTP. {ECO:0000255}. FT SITE 450 450 Involved in polymerization. FT {ECO:0000250}. FT MOD_RES 48 48 Phosphoserine. FT {ECO:0000250|UniProtKB:P68366}. FT MOD_RES 83 83 Nitrated tyrosine. FT {ECO:0000250|UniProtKB:P68368}. FT MOD_RES 282 282 Nitrated tyrosine. FT {ECO:0000250|UniProtKB:P68373}. FT MOD_RES 432 432 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q9BQE3}. FT MOD_RES 439 439 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BQE3}. SQ SEQUENCE 450 AA; 49960 MW; 2A78714CBA782D55 CRC64; MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD RIRKLADLCT GLQGFLIFHS FGGGTGSGFA SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSV EAEAEEGEEY //