ID TBB3_HUMAN Reviewed; 450 AA. AC Q13509; A8K854; Q9BTZ0; Q9BW10; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 2. DT 27-MAR-2024, entry version 217. DE RecName: Full=Tubulin beta-3 chain; DE AltName: Full=Tubulin beta-4 chain; DE AltName: Full=Tubulin beta-III; GN Name=TUBB3; Synonyms=TUBB4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9473684; DOI=10.1016/s0167-4781(97)00168-1; RA Ranganathan S., Dexter D.W., Benetatos C.A., Hudes G.R.; RT "Cloning and sequencing of human betaIII-tubulin cDNA: induction of betaIII RT isotype in human prostate carcinoma cells by acute exposure to RT antimicrotubule agents."; RL Biochim. Biophys. Acta 1395:237-245(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Mammary cancer; RA Banerjee A.; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain, and Esophagus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [7] RP PROTEIN SEQUENCE OF 63-77; 104-121; 242-251; 163-174 AND 381-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP TISSUE SPECIFICITY. RX PubMed=14736079; DOI=10.1177/088307380301801205; RA Katsetos C.D., Legido A., Perentes E., Mork S.J.; RT "Class III beta-tubulin isotype: a key cytoskeletal protein at the RT crossroads of developmental neurobiology and tumor neuropathology."; RL J. Child Neurol. 18:851-866(2003). RN [9] RP ERRATUM OF PUBMED:14736079. RA Katsetos C.D., Legido A., Perentes E., Mork S.J.; RL J. Child Neurol. 19:531-531(2004). RN [10] RP PHOSPHORYLATION AT SER-172 BY CDK1. RX PubMed=16371510; DOI=10.1091/mbc.e05-07-0621; RA Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C., RA Lantez V., Job D.; RT "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin- RT dependent kinase Cdk1."; RL Mol. Biol. Cell 17:1041-1050(2006). RN [11] 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 [12] RP FUNCTION, VARIANTS CFEOM3A GLN-62; CYS-262; HIS-262; THR-302; CYS-380; RP LYS-410; HIS-417 AND ASN-417, AND CHARACTERIZATION OF VARIANTS CFEOM3A RP GLN-62; CYS-262; HIS-262; THR-302; CYS-380 AND LYS-410. RX PubMed=20074521; DOI=10.1016/j.cell.2009.12.011; RA Tischfield M.A., Baris H.N., Wu C., Rudolph G., Van Maldergem L., He W., RA Chan W.M., Andrews C., Demer J.L., Robertson R.L., Mackey D.A., RA Ruddle J.B., Bird T.D., Gottlob I., Pieh C., Traboulsi E.I., Pomeroy S.L., RA Hunter D.G., Soul J.S., Newlin A., Sabol L.J., Doherty E.J., RA de Uzcategui C.E., de Uzcategui N., Collins M.L., Sener E.C., Wabbels B., RA Hellebrand H., Meitinger T., de Berardinis T., Magli A., Schiavi C., RA Pastore-Trossello M., Koc F., Wong A.M., Levin A.V., Geraghty M.T., RA Descartes M., Flaherty M., Jamieson R.V., Moller H.U., Meuthen I., RA Callen D.F., Kerwin J., Lindsay S., Meindl A., Gupta M.L. Jr., Pellman D., RA Engle E.C.; RT "Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, RT and axon guidance."; RL Cell 140:74-87(2010). RN [13] RP TISSUE SPECIFICITY. RX PubMed=20191564; DOI=10.1002/cm.20436; RA Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C., RA Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C.; RT "Tumoral and tissue-specific expression of the major human beta-tubulin RT isotypes."; RL Cytoskeleton 67:214-223(2010). RN [14] RP INTERACTION WITH NLRP5. RX PubMed=24374158; DOI=10.1016/j.ydbio.2013.12.025; RA Kim B., Zhang X., Kan R., Cohen R., Mukai C., Travis A.J., Coonrod S.A.; RT "The role of MATER in endoplasmic reticulum distribution and calcium RT homeostasis in mouse oocytes."; RL Dev. Biol. 386:331-339(2014). RN [15] RP GLUTAMYLATION. RX PubMed=26875866; DOI=10.1016/j.cell.2016.01.019; RA Valenstein M.L., Roll-Mecak A.; RT "Graded control of microtubule severing by tubulin glutamylation."; RL Cell 164:911-921(2016). RN [16] RP FUNCTION, AND INTERACTION WITH UNC5C. RX PubMed=28483977; DOI=10.1523/jneurosci.2617-16.2017; RA Shao Q., Yang T., Huang H., Alarmanazi F., Liu G.; RT "Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates RT Netrin-1 Repulsion."; RL J. Neurosci. 37:5620-5633(2017). RN [17] RP INTERACTION WITH DPYSL5. RX PubMed=33894126; DOI=10.1016/j.ajhg.2021.04.004; RA Jeanne M., Demory H., Moutal A., Vuillaume M.L., Blesson S., Thepault R.A., RA Marouillat S., Halewa J., Maas S.M., Motazacker M.M., Mancini G.M.S., RA van Slegtenhorst M.A., Andreou A., Cox H., Vogt J., Laufman J., RA Kostandyan N., Babikyan D., Hancarova M., Bendova S., Sedlacek Z., RA Aldinger K.A., Sherr E.H., Argilli E., England E.M., Audebert-Bellanger S., RA Bonneau D., Colin E., Denomme-Pichon A.S., Gilbert-Dussardier B., RA Isidor B., Kuery S., Odent S., Redon R., Khanna R., Dobyns W.B., RA Bezieau S., Honnorat J., Lohkamp B., Toutain A., Laumonnier F.; RT "Missense variants in DPYSL5 cause a neurodevelopmental disorder with RT corpus callosum agenesis and cerebellar abnormalities."; RL Am. J. Hum. Genet. 108:951-961(2021). RN [18] {ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7SJ8, ECO:0007744|PDB:7SJ9, ECO:0007744|PDB:7SJA} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH RP ALPHA-TUBULIN AND GDP, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=34996871; DOI=10.1073/pnas.2114994119; RA LaFrance B.J., Roostalu J., Henkin G., Greber B.J., Zhang R., Normanno D., RA McCollum C.O., Surrey T., Nogales E.; RT "Structural transitions in the GTP cap visualized by cryo-electron RT microscopy of catalytically inactive microtubules."; RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022). RN [19] RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) IN COMPLEX WITH RP ALPHA-TUBULIN; KIAA0895L AND GDP, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=35482892; DOI=10.1126/science.abn6020; RA Landskron L., Bak J., Adamopoulos A., Kaplani K., Moraiti M., RA van den Hengel L.G., Song J.Y., Bleijerveld O.B., Nieuwenhuis J., RA Heidebrecht T., Henneman L., Moutin M.J., Barisic M., Taraviras S., RA Perrakis A., Brummelkamp T.R.; RT "Posttranslational modification of microtubules by the MATCAP RT detyrosinase."; RL Science 376:eabn6020-eabn6020(2022). RN [20] RP VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323, AND CHARACTERIZATION RP OF VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323. RX PubMed=20829227; DOI=10.1093/hmg/ddq377; RA Poirier K., Saillour Y., Bahi-Buisson N., Jaglin X.H., Fallet-Bianco C., RA Nabbout R., Castelnau-Ptakhine L., Roubertie A., Attie-Bitach T., RA Desguerre I., Genevieve D., Barnerias C., Keren B., Lebrun N., Boddaert N., RA Encha-Razavi F., Chelly J.; RT "Mutations in the neuronal ss-tubulin subunit TUBB3 result in malformation RT of cortical development and neuronal migration defects."; RL Hum. Mol. Genet. 19:4462-4473(2010). CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers (PubMed:34996871). Microtubules CC grow by the addition of GTP-tubulin dimers to the microtubule end, CC where a stabilizing cap forms (PubMed:34996871). Below the cap, tubulin CC dimers are in GDP-bound state, owing to GTPase activity of alpha- CC tubulin (PubMed:34996871). TUBB3 plays a critical role in proper axon CC guidance and maintenance (PubMed:20074521). Binding of NTN1/Netrin-1 to CC its receptor UNC5C might cause dissociation of UNC5C from polymerized CC TUBB3 in microtubules and thereby lead to increased microtubule CC dynamics and axon repulsion (PubMed:28483977). Plays a role in dorsal CC root ganglion axon projection towards the spinal cord CC (PubMed:28483977). {ECO:0000269|PubMed:20074521, CC ECO:0000269|PubMed:28483977, ECO:0000269|PubMed:34996871}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC -!- SUBUNIT: Dimer of alpha and beta chains (PubMed:34996871, CC PubMed:35482892). A typical microtubule is a hollow water-filled tube CC with an outer diameter of 25 nm and an inner diameter of 15 nM CC (PubMed:34996871, PubMed:35482892). Alpha-beta heterodimers associate CC head-to-tail to form protofilaments running lengthwise along the CC microtubule wall with the beta-tubulin subunit facing the microtubule CC plus end conferring a structural polarity (PubMed:34996871, CC PubMed:35482892). Microtubules usually have 13 protofilaments but CC different protofilament numbers can be found in some organisms and CC specialized cells (PubMed:34996871, PubMed:35482892). Interacts with CC UNC5C (via cytoplasmic domain); this interaction is decreased by CC NTN1/Netrin-1 (PubMed:28483977). Interacts with NLRP5/MATER at CC cytoskeleton microtubules (PubMed:24374158). Interacts with DPYSL5 CC (PubMed:33894126). Interacts with CFAP61 (By similarity). CC {ECO:0000250|UniProtKB:Q9ERD7, ECO:0000269|PubMed:24374158, CC ECO:0000269|PubMed:28483977, ECO:0000269|PubMed:33894126, CC ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:35482892}. CC -!- INTERACTION: CC Q13509; P54274: TERF1; NbExp=2; IntAct=EBI-350989, EBI-710997; CC Q13509; P68363: TUBA1B; NbExp=3; IntAct=EBI-350989, EBI-487083; CC Q13509; O95185: UNC5C; NbExp=2; IntAct=EBI-350989, EBI-11343380; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:35482892}. Cell CC projection, growth cone {ECO:0000250|UniProtKB:Q9ERD7}. Cell CC projection, lamellipodium {ECO:0000250|UniProtKB:Q9ERD7}. Cell CC projection, filopodium {ECO:0000250|UniProtKB:Q9ERD7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13509-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13509-2; Sequence=VSP_054659; CC -!- TISSUE SPECIFICITY: Expression is primarily restricted to central and CC peripheral nervous system. Greatly increased expression in most CC cancerous tissues. {ECO:0000269|PubMed:14736079, CC ECO:0000269|PubMed:20191564}. CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such as CC calcium. CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and CC may be critical for tubulin autoregulation. CC {ECO:0000250|UniProtKB:P07437}. CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated, CC resulting in polyglutamate chains on the gamma-carboxyl group CC (PubMed:26875866). 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 (PubMed:26875866). Glutamylation is also involved in cilia CC motility (By similarity). {ECO:0000250|UniProtKB:P99024, CC ECO:0000269|PubMed:26875866}. CC -!- PTM: Some glutamate residues at the C-terminus are monoglycylated but CC not polyglycylated due to the absence of functional TTLL10 in human. CC Monoglycylation is mainly limited to tubulin incorporated into cilia CC and flagella axonemes, which is required for their stability and CC maintenance. Flagella glycylation controls sperm motility. Both CC polyglutamylation and monoglycylation can coexist on the same protein CC on adjacent residues, and lowering glycylation levels increases CC polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437, CC ECO:0000305|PubMed:19524510}. CC -!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from CC metaphase to telophase, but not in interphase. This phosphorylation CC inhibits tubulin incorporation into microtubules. CC {ECO:0000269|PubMed:16371510}. CC -!- DISEASE: Fibrosis of extraocular muscles, congenital, 3A (CFEOM3A) CC [MIM:600638]: A congenital ocular motility disorder marked by CC restrictive ophthalmoplegia affecting extraocular muscles innervated by CC the oculomotor and/or trochlear nerves. It is clinically characterized CC by anchoring of the eyes in downward gaze, ptosis, and backward tilt of CC the head. Congenital fibrosis of extraocular muscles type 3 presents as CC a non-progressive, autosomal dominant disorder with variable CC expression. Patients may be bilaterally or unilaterally affected, and CC their oculo-motility defects range from complete ophthalmoplegia (with CC the eyes fixed in a hypo- and exotropic position), to mild asymptomatic CC restrictions of ocular movement. Ptosis, refractive error, amblyopia, CC and compensatory head positions are associated with the more severe CC forms of the disorder. In some cases, the ocular phenotype is CC accompanied by additional features including developmental delay, CC corpus callosum agenesis, basal ganglia dysmorphism, facial weakness, CC polyneuropathy. {ECO:0000269|PubMed:20074521}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 1 CC (CDCBM1) [MIM:614039]: A disorder of aberrant neuronal migration and CC disturbed axonal guidance. Affected individuals have mild to severe CC intellectual disability, strabismus, axial hypotonia, and spasticity. CC Brain imaging shows variable malformations of cortical development, CC including polymicrogyria, gyral disorganization, and fusion of the CC basal ganglia, as well as thin corpus callosum, hypoplastic brainstem, CC and dysplastic cerebellar vermis. Extraocular muscles are not involved. CC {ECO:0000269|PubMed:20829227}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; U47634; AAC52035.1; -; mRNA. DR EMBL; AF427491; AAL28094.1; -; mRNA. DR EMBL; AK122757; BAG53710.1; -; mRNA. DR EMBL; AK292219; BAF84908.1; -; mRNA. DR EMBL; AC092143; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471184; EAW66674.1; -; Genomic_DNA. DR EMBL; BC000748; AAH00748.1; -; mRNA. DR EMBL; BC003021; AAH03021.2; -; mRNA. DR CCDS; CCDS10988.1; -. [Q13509-1] DR CCDS; CCDS56012.1; -. [Q13509-2] DR RefSeq; NP_001184110.1; NM_001197181.1. [Q13509-2] DR RefSeq; NP_006077.2; NM_006086.3. [Q13509-1] DR PDB; 5IJ0; EM; 3.80 A; B=1-426. DR PDB; 5IJ9; EM; 3.70 A; B=1-426. DR PDB; 5JCO; EM; 4.00 A; C/D/I/J/K/L=1-426. DR PDB; 6E7B; EM; 3.50 A; B=1-426. DR PDB; 6S8L; X-ray; 1.80 A; B=1-450. DR PDB; 6WSL; EM; 3.10 A; B/F=1-450. DR PDB; 7LXB; EM; 3.26 A; B/D/F/H/J/L/N/P=1-450. DR PDB; 7M18; EM; 3.38 A; B/D/F/H/J/L/N/P=1-450. DR PDB; 7M20; EM; 3.84 A; B/D/F/H/J/L/N/P/R=1-450. DR PDB; 7PJF; X-ray; 1.86 A; B=1-450. DR PDB; 7SJ7; EM; 3.80 A; B/D/F/G/H/I=1-450. DR PDB; 7SJ8; EM; 3.60 A; B/D/F/G/H/I=1-450. DR PDB; 7SJ9; EM; 3.80 A; B/D/F/G/H/I=1-450. DR PDB; 7SJA; EM; 3.80 A; B/D/F/G/H/I=1-450. DR PDB; 7Z6S; EM; 2.90 A; B/H=1-450. DR PDBsum; 5IJ0; -. DR PDBsum; 5IJ9; -. DR PDBsum; 5JCO; -. DR PDBsum; 6E7B; -. DR PDBsum; 6S8L; -. DR PDBsum; 6WSL; -. DR PDBsum; 7LXB; -. DR PDBsum; 7M18; -. DR PDBsum; 7M20; -. DR PDBsum; 7PJF; -. DR PDBsum; 7SJ7; -. DR PDBsum; 7SJ8; -. DR PDBsum; 7SJ9; -. DR PDBsum; 7SJA; -. DR PDBsum; 7Z6S; -. DR AlphaFoldDB; Q13509; -. DR EMDB; EMD-14529; -. DR EMDB; EMD-21893; -. DR EMDB; EMD-23569; -. DR EMDB; EMD-23615; -. DR EMDB; EMD-23627; -. DR EMDB; EMD-25156; -. DR EMDB; EMD-25157; -. DR EMDB; EMD-25159; -. DR EMDB; EMD-25160; -. DR EMDB; EMD-8094; -. DR EMDB; EMD-8095; -. DR EMDB; EMD-8150; -. DR EMDB; EMD-8997; -. DR SMR; Q13509; -. DR BioGRID; 115654; 452. DR CORUM; Q13509; -. DR DIP; DIP-31505N; -. DR IntAct; Q13509; 274. DR MINT; Q13509; -. DR STRING; 9606.ENSP00000320295; -. DR BindingDB; Q13509; -. DR ChEMBL; CHEMBL2597; -. DR DrugBank; DB05147; CYT997. DR DrugBank; DB01873; Epothilone D. DR DrugBank; DB04845; Ixabepilone. DR DrugBank; DB03010; Patupilone. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR DrugBank; DB06042; ZEN-012. DR DrugCentral; Q13509; -. DR GuidetoPHARMACOLOGY; 2752; -. DR GlyGen; Q13509; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q13509; -. DR MetOSite; Q13509; -. DR PhosphoSitePlus; Q13509; -. DR SwissPalm; Q13509; -. DR BioMuta; TUBB3; -. DR DMDM; 20455526; -. DR OGP; Q13509; -. DR EPD; Q13509; -. DR jPOST; Q13509; -. DR MassIVE; Q13509; -. DR MaxQB; Q13509; -. DR PaxDb; 9606-ENSP00000320295; -. DR PeptideAtlas; Q13509; -. DR PRIDE; Q13509; -. DR ProteomicsDB; 1874; -. DR ProteomicsDB; 59510; -. [Q13509-1] DR Pumba; Q13509; -. DR TopDownProteomics; Q13509-1; -. [Q13509-1] DR ABCD; Q13509; 1 sequenced antibody. DR Antibodypedia; 54822; 1374 antibodies from 45 providers. DR DNASU; 10381; -. DR Ensembl; ENST00000315491.12; ENSP00000320295.7; ENSG00000258947.8. [Q13509-1] DR Ensembl; ENST00000554444.5; ENSP00000451617.1; ENSG00000258947.8. [Q13509-2] DR GeneID; 10381; -. DR KEGG; hsa:10381; -. DR MANE-Select; ENST00000315491.12; ENSP00000320295.7; NM_006086.4; NP_006077.2. DR UCSC; uc002fph.2; human. [Q13509-1] DR AGR; HGNC:20772; -. DR CTD; 10381; -. DR DisGeNET; 10381; -. DR GeneCards; TUBB3; -. DR GeneReviews; TUBB3; -. DR HGNC; HGNC:20772; TUBB3. DR HPA; ENSG00000258947; Tissue enriched (brain). DR MalaCards; TUBB3; -. DR MIM; 600638; phenotype. DR MIM; 602661; gene. DR MIM; 614039; phenotype. DR neXtProt; NX_Q13509; -. DR OpenTargets; ENSG00000258947; -. DR Orphanet; 45358; Congenital fibrosis of extraocular muscles. DR Orphanet; 300570; Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation. DR Orphanet; 467166; Tubulinopathy-associated dysgyria. DR PharmGKB; PA134953867; -. DR VEuPathDB; HostDB:ENSG00000258947; -. DR eggNOG; KOG1375; Eukaryota. DR GeneTree; ENSGT00940000159115; -. DR HOGENOM; CLU_015718_0_0_1; -. DR InParanoid; Q13509; -. DR OMA; HARHITK; -. DR OrthoDB; 3124041at2759; -. DR PhylomeDB; Q13509; -. DR TreeFam; TF300298; -. DR PathwayCommons; Q13509; -. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane. DR Reactome; R-HSA-190861; Gap junction assembly. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway. DR Reactome; R-HSA-437239; Recycling pathway of L1. DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-5617833; Cilium Assembly. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors. DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs. DR Reactome; R-HSA-9646399; Aggrephagy. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III. DR Reactome; R-HSA-983189; Kinesins. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; Q13509; -. DR SIGNOR; Q13509; -. DR BioGRID-ORCS; 10381; 93 hits in 1167 CRISPR screens. DR ChiTaRS; TUBB3; human. DR GeneWiki; TUBB3; -. DR GenomeRNAi; 10381; -. DR Pharos; Q13509; Tclin. DR PRO; PR:Q13509; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q13509; Protein. DR Bgee; ENSG00000258947; Expressed in cortical plate and 99 other cell types or tissues. DR ExpressionAtlas; Q13509; baseline and differential. DR GO; GO:0030424; C:axon; ISS:ARUK-UCL. DR GO; GO:0071944; C:cell periphery; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0030175; C:filopodium; ISS:UniProtKB. DR GO; GO:0030426; C:growth cone; ISS:UniProtKB. DR GO; GO:0045171; C:intercellular bridge; IDA:HPA. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0072686; C:mitotic spindle; IDA:HPA. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990890; F:netrin receptor binding; IPI:UniProtKB. DR GO; GO:0042277; F:peptide binding; IEA:Ensembl. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB. DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB. DR GO; GO:1990791; P:dorsal root ganglion development; IDA:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR CDD; cd02187; beta_tubulin; 1. DR Gene3D; 1.10.287.600; Helix hairpin bin; 1. DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1. DR InterPro; IPR013838; Beta-tubulin_BS. DR InterPro; IPR002453; Beta_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; TUBULIN; 1. DR PANTHER; PTHR11588:SF43; TUBULIN BETA-3 CHAIN; 1. DR Pfam; PF00091; Tubulin; 1. DR Pfam; PF03953; Tubulin_C; 1. DR PRINTS; PR01163; BETATUBULIN. DR PRINTS; PR01161; TUBULIN. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1. DR Genevisible; Q13509; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Disease variant; GTP-binding; KW Intellectual disability; Isopeptide bond; Magnesium; Metal-binding; KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..450 FT /note="Tubulin beta-3 chain" FT /id="PRO_0000048250" FT REGION 425..450 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1..4 FT /note="MREI motif" FT /evidence="ECO:0000250|UniProtKB:P07437" FT COMPBIAS 431..450 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 11 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:34996871, FT ECO:0000305|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 138 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0007744|PDB:7SJ7" FT BINDING 138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:34996871, FT ECO:0007744|PDB:7SJ7" FT BINDING 142 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 142 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:34996871, FT ECO:0000305|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 143 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 143 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:34996871, FT ECO:0000305|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 144 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:34996871, FT ECO:0000305|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 204 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:34996871, FT ECO:0000305|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 226 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 226 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:34996871, FT ECO:0000305|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT MOD_RES 172 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:16371510" FT MOD_RES 438 FT /note="5-glutamyl polyglutamate" FT /evidence="ECO:0000250|UniProtKB:Q2T9S0" FT MOD_RES 444 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q2T9S0" FT VAR_SEQ 1..72 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054659" FT VARIANT 62 FT /note="R -> Q (in CFEOM3A; affects heterodimers formation; FT results in increased stability and reduced dynamics of FT microtubules; dbSNP:rs864321714)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062758" FT VARIANT 178 FT /note="T -> M (in CDCBM1; can form tubulin heterodimers FT that are properly incorporated into microtubules; the FT microtubules are less stable than wild-type; FT dbSNP:rs747480526)" FT /evidence="ECO:0000269|PubMed:20829227" FT /id="VAR_066206" FT VARIANT 205 FT /note="E -> K (in CDCBM1; does not form tubulin FT heterodimers; patient fibroblasts show no major alterations FT in the microtubule network, but the microtubules are less FT stable than wild-type; dbSNP:rs878853257)" FT /evidence="ECO:0000269|PubMed:20829227" FT /id="VAR_066207" FT VARIANT 262 FT /note="R -> C (in CFEOM3A; affects heterodimers formation; FT affects microtubules polymerization and depolymerization FT rates; dbSNP:rs267607162)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062759" FT VARIANT 262 FT /note="R -> H (in CFEOM3A; severe phenotype with congenital FT facial weakness, congenital wrist and finger contractures; FT affects microtubules polymerization and depolymerization FT rates; dbSNP:rs864321716)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062760" FT VARIANT 302 FT /note="A -> T (in CFEOM3A; affects heterodimers formation; FT results in increased stability and reduced dynamics of FT microtubules; dbSNP:rs267607163)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062761" FT VARIANT 302 FT /note="A -> V (in CDCBM1; does not form tubulin FT heterodimers; dbSNP:rs878853258)" FT /evidence="ECO:0000269|PubMed:20829227" FT /id="VAR_066208" FT VARIANT 323 FT /note="M -> V (in CDCBM1; reduced heterodimers formation; FT dbSNP:rs878853256)" FT /evidence="ECO:0000269|PubMed:20829227" FT /id="VAR_066209" FT VARIANT 380 FT /note="R -> C (in CFEOM3A; affects heterodimers formation; FT results in increased stability and reduced dynamics of FT microtubules; dbSNP:rs864321717)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062762" FT VARIANT 410 FT /note="E -> K (in CFEOM3A; severe phenotype with congenital FT facial weakness; lower extremity weakness and sensory loss FT in the second to third decade of life in one patient; FT affects microtubules polymerization and depolymerization FT rates; dbSNP:rs267607165)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062763" FT VARIANT 417 FT /note="D -> H (in CFEOM3A; severe phenotype with congenital FT facial weakness, congenital wrist and finger contractures; FT dbSNP:rs267607164)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062764" FT VARIANT 417 FT /note="D -> N (in CFEOM3A; some patients with lower FT extremity weakness and sensory loss in the second to third FT decade of life; also found in patients without CFEOM3A who FT developed polyneuropathy; dbSNP:rs267607164)" FT /evidence="ECO:0000269|PubMed:20074521" FT /id="VAR_062765" FT CONFLICT 275 FT /note="A -> R (in Ref. 1; AAC52035)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 10..28 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:7M18" FT HELIX 42..45 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:6S8L" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:7Z6S" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 101..106 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 108..125 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 132..142 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 143..158 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 162..170 FT /evidence="ECO:0007829|PDB:6S8L" FT TURN 173..175 FT /evidence="ECO:0007829|PDB:7PJF" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:7Z6S" FT HELIX 181..195 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 204..213 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 222..241 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:7PJF" FT HELIX 250..257 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 259..262 FT /evidence="ECO:0007829|PDB:7Z6S" FT STRAND 265..272 FT /evidence="ECO:0007829|PDB:6S8L" FT TURN 278..281 FT /evidence="ECO:0007829|PDB:7Z6S" FT HELIX 286..294 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 310..320 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 323..335 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:7Z6S" FT STRAND 349..356 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:7Z6S" FT STRAND 364..371 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 375..390 FT /evidence="ECO:0007829|PDB:6S8L" FT TURN 391..394 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 395..399 FT /evidence="ECO:0007829|PDB:6S8L" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 405..427 FT /evidence="ECO:0007829|PDB:6S8L" SQ SEQUENCE 450 AA; 50433 MW; 4B9CDE7DBA102949 CRC64; MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEMYEDD EEESEAQGPK //