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-JUL-2012, entry version 114. 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 MEDLINE=87064538; 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 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 POLYGLUTAMYLATION. 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 POLYGLYCYLATION. 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). 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. 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 -!- 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 (By similarity). 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-tubulins at Lys-40 stabilizes CC microtubules and affects affinity and processivity of microtubule CC motors. This modification has a role in multiple cellular CC functions, ranging from cell motility, cell cycle progression or CC cell differentiation to intracellular trafficking and signaling CC (By similarity). CC -!- SIMILARITY: Belongs to the tubulin family. 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 IPI; IPI00466390; -. 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; 1-438. DR STRING; P05214; -. DR PhosphoSite; P05214; -. DR REPRODUCTION-2DPAGE; 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 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; ISAVREC; -. DR OrthoDB; EOG44J2HZ; -. DR NextBio; 302046; -. DR ArrayExpress; P05214; -. DR Bgee; P05214; -. DR CleanEx; MM_TUBA3A; -. DR CleanEx; MM_TUBA3B; -. DR Genevestigator; P05214; -. DR GermOnline; ENSMUSG00000072235; Mus musculus. 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:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro. DR GO; GO:0051258; P:protein polymerization; IEA:InterPro. DR Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1. DR Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1. DR Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 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; Tubulin; 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; Tub_FtsZ_C; 1. DR SUPFAM; SSF52490; Tubulin_FtsZ; 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; KW Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1 450 Tubulin alpha-3 chain. FT /FTId=PRO_0000048122. FT NP_BIND 142 148 GTP (Potential). FT SITE 450 450 Involved in polymerization (By FT similarity). FT MOD_RES 40 40 N6-acetyllysine (By similarity). FT MOD_RES 439 439 Phosphoserine (By similarity). 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 //