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 06-FEB-2007, entry version 68. DE Tubulin alpha-3/alpha-7 chain (Alpha-tubulin 3/7) (Alpha-tubulin DE isotype M-alpha-3/7). GN Name=Tuba3; GN and GN Name=Tuba7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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). 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 -!- 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 -!- 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 PIR; I77426; I77426. DR UniGene; Mm.287784; -. DR UniGene; Mm.391547; -. DR HSSP; P02550; 1FFX. DR SMR; P05214; 2-439. DR REPRODUCTION-2DPAGE; P05214; MOUSE. DR Ensembl; ENSMUSG00000055391; Mus musculus. DR KEGG; mmu:22144; -. DR KEGG; mmu:22147; -. DR MGI; MGI:1095406; Tuba3. DR MGI; MGI:1095408; Tuba7. DR ArrayExpress; P05214; -. DR GermOnline; ENSMUSG00000072235; Mus musculus. DR InterPro; IPR002452; Alpha_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. 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 PROSITE; PS00227; TUBULIN; 1. KW GTP-binding; Microtubule; Nucleotide-binding. FT CHAIN 1 450 Tubulin alpha-3/alpha-7 chain. FT /FTId=PRO_0000048122. FT NP_BIND 142 148 GTP (Potential). FT SITE 450 450 Involved in polymerization (By FT 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 //