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 11-MAY-2016, entry version 151. 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: 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 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 CC polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}. CC -!- PTM: Some glutamate residues at the C-terminus are CC polyglutamylated, resulting in polyglutamate chains on the gamma- CC carboxyl group (PubMed:15890843). Polyglutamylation plays a key CC role in microtubule severing by spastin (SPAST). SPAST CC preferentially recognizes and acts on microtubules decorated with CC short polyglutamate tails: severing activity by SPAST increases as CC the number of glutamates per tubulin rises from one to eight, but CC decreases beyond this glutamylation threshold (By similarity). CC {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}. 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. CC {ECO:0000250|UniProtKB:P68370}. 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|UniProtKB:P41351}. 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; 70. DR IntAct; P05214; 69. DR STRING; 10090.ENSMUSP00000085580; -. DR BindingDB; P05214; -. DR iPTMnet; P05214; -. DR PhosphoSite; P05214; -. DR REPRODUCTION-2DPAGE; P05214; -. DR EPD; P05214; -. DR PaxDb; P05214; -. DR PRIDE; P05214; -. DR Ensembl; ENSMUST00000087445; ENSMUSP00000084713; ENSMUSG00000067338. DR Ensembl; ENSMUST00000088246; ENSMUSP00000085580; ENSMUSG00000067702. 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 eggNOG; KOG1376; Eukaryota. DR eggNOG; COG5023; LUCA. DR HOGENOM; HOG000165711; -. DR HOVERGEN; HBG000089; -. DR InParanoid; P05214; -. DR KO; K07374; -. DR OMA; HSIPREC; -. DR OrthoDB; EOG7TBC1W; -. DR PhylomeDB; P05214; -. DR TreeFam; TF300314; -. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5620924; Intraflagellar transport. DR Reactome; R-MMU-5632684; Hedgehog 'on' state. DR ChiTaRS; Tuba3a; mouse. DR NextBio; 302046; -. DR PRO; PR:P05214; -. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; P05214; -. DR CleanEx; MM_TUBA3A; -. DR CleanEx; MM_TUBA3B; -. DR ExpressionAtlas; P05214; baseline and differential. DR Genevisible; P05214; MM. DR GO; GO:0036064; C:ciliary basal body; IDA:MGI. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005874; C:microtubule; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. 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 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 40 40 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P41351}. 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 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 //