TBA8_MOUSE
ID TBA8_MOUSE Reviewed; 449 AA.
AC Q9JJZ2; D4P911; Q9CV57;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Tubulin alpha-8 chain;
DE AltName: Full=Alpha-tubulin 8;
GN Name=Tuba8;
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].
RC TISSUE=Skeletal muscle;
RX PubMed=10772959; DOI=10.1006/bbrc.2000.2571;
RA Stanchi F., Corso V., Scannapieco P., Ievolella C., Negrisolo E., Tiso N.,
RA Lanfranchi G., Valle G.;
RT "TUBA8: a new tissue-specific isoform of alpha-tubulin that is highly
RT conserved in human and mouse.";
RL Biochem. Biophys. Res. Commun. 270:1111-1118(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20466094; DOI=10.1016/j.ajhg.2010.03.019;
RA Braun A., Breuss M., Salzer M.C., Flint J., Cowan N.J., Keays D.A.;
RT "Tuba8 is expressed at low levels in the developing mouse and human
RT brain.";
RL Am. J. Hum. Genet. 86:819-822(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-449.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [6]
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 [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=19896110; DOI=10.1016/j.ajhg.2009.10.007;
RA Abdollahi M.R., Morrison E., Sirey T., Molnar Z., Hayward B.E., Carr I.M.,
RA Springell K., Woods C.G., Ahmed M., Hattingh L., Corry P., Pilz D.T.,
RA Stoodley N., Crow Y., Taylor G.R., Bonthron D.T., Sheridan E.;
RT "Mutation of the variant alpha-tubulin TUBA8 results in polymicrogyria with
RT optic nerve hypoplasia.";
RL Am. J. Hum. Genet. 85:737-744(2009).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, and 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 expression.";
RL Cell 143:1174-1189(2010).
RN [10]
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 [11]
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. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in the testis, followed
CC by skeletal and heart muscle. Expressed at low levels in the developing
CC brain. {ECO:0000269|PubMed:20466094}.
CC -!- DEVELOPMENTAL STAGE: At embryonic day (E) 13.5, expressed in the
CC cortical preplate and cingulate cortex. By 15.5 dpc, the strongest
CC expression is seen in the cortical plate. By 18.5 dpc, cortical
CC expression is most intense in the upper layers and subplate. There is
CC strong expression in the areas CA1-3 of the hippocampus. At P0,
CC cortical expression is strongest in the dense cortical plate and
CC subplate. Hippocampal expression is more intense in areas CA1-3 than in
CC the dentate gyrus. At P8, lamination is almost complete and cortical
CC expression is strongest in layers II-III and V and the subplate. There
CC is also expression in the mediodorsal nuclei of the thalamus, the
CC mitral cell layer of the olfactory bulb, and the external granular
CC layer, molecular layer, and internal granular cell layer of the
CC cerebellum. {ECO:0000269|PubMed:19896110, ECO:0000269|PubMed:20466094}.
CC -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P68363}.
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:15890843). Polyglutamylation plays a key role in microtubule
CC severing by spastin (SPAST). SPAST preferentially recognizes and acts
CC on microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (By similarity). Glutamylation is also involved in cilia
CC motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36,
CC ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:23897886}.
CC -!- MISCELLANEOUS: This tubulin does not have a C-terminal tyrosine.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AJ245923; CAB88033.1; -; mRNA.
DR EMBL; GU591980; ADD82895.1; -; mRNA.
DR EMBL; CH466523; EDK99659.1; -; Genomic_DNA.
DR EMBL; BC017631; AAH17631.1; -; mRNA.
DR EMBL; AK009439; BAB26288.1; -; mRNA.
DR CCDS; CCDS39615.1; -.
DR RefSeq; NP_059075.1; NM_017379.2.
DR AlphaFoldDB; Q9JJZ2; -.
DR SMR; Q9JJZ2; -.
DR BioGRID; 207491; 4.
DR IntAct; Q9JJZ2; 4.
DR MINT; Q9JJZ2; -.
DR STRING; 10090.ENSMUSP00000032233; -.
DR iPTMnet; Q9JJZ2; -.
DR PhosphoSitePlus; Q9JJZ2; -.
DR SwissPalm; Q9JJZ2; -.
DR EPD; Q9JJZ2; -.
DR jPOST; Q9JJZ2; -.
DR MaxQB; Q9JJZ2; -.
DR PaxDb; Q9JJZ2; -.
DR PeptideAtlas; Q9JJZ2; -.
DR PRIDE; Q9JJZ2; -.
DR ProteomicsDB; 254857; -.
DR Antibodypedia; 22762; 208 antibodies from 25 providers.
DR DNASU; 53857; -.
DR Ensembl; ENSMUST00000032233; ENSMUSP00000032233; ENSMUSG00000030137.
DR GeneID; 53857; -.
DR KEGG; mmu:53857; -.
DR UCSC; uc009dof.1; mouse.
DR CTD; 51807; -.
DR MGI; MGI:1858225; Tuba8.
DR VEuPathDB; HostDB:ENSMUSG00000030137; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00940000159668; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; Q9JJZ2; -.
DR OMA; AQASKVN; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; Q9JJZ2; -.
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-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-5617833; Cilium Assembly.
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-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 BioGRID-ORCS; 53857; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9JJZ2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JJZ2; protein.
DR Bgee; ENSMUSG00000030137; Expressed in hindlimb stylopod muscle and 154 other tissues.
DR Genevisible; Q9JJZ2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISA:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISA:MGI.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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; 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; 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 Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..449
FT /note="Tubulin alpha-8 chain"
FT /id="PRO_0000048125"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 447
FT /note="E -> G (in Ref. 5; BAB26288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 50052 MW; AA979E2DB21FC5DD CRC64;
MRECISVHVG QAGVQIGNAC WELFCLEHGI QADGTFGTQA SKINDDDSFT TFFSETGNGK
HVPRAVMVDL EPTVVDEVRA GTYRQLFHPE QLITGKEDAA NNYARGHYTV GKESIDLVLD
RIRKLTDACS GLQGFLIFHS FGGGTGSGFT SLLMERLSLD YGKKSKLEFA IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPIISAEK AYHEQLSVAE ITSSCFEPNS
QMVKCDPRHG KYMACCMLYR GDVVPKDVNV AIAAIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGTDSF EEENEGEEF
