ID A0A0D5MER0_CLOEH Unreviewed; 451 AA. AC A0A0D5MER0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 03-AUG-2022, entry version 31. DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352}; OS Closterium ehrenbergii (Green alga). OC Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae; OC Desmidiales; Closteriaceae; Closterium. OX NCBI_TaxID=102165 {ECO:0000313|EMBL:AJY58974.1}; RN [1] {ECO:0000313|EMBL:AJY58974.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25724346; RA Lee M.-A., Guo R., Ebenezer V., Ki J.-S.; RT "Evaluation and selection of reference genes for ecotoxicogenomic study of RT the green alga Closterium ehrenbergii using quantitative real-time PCR."; RL Ecotoxicology 0:0-0(2015). 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 {ECO:0000256|RuleBase:RU000352}. 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. {ECO:0000256|RuleBase:RU000352}. CC -!- SIMILARITY: Belongs to the tubulin family. CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}. 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; KM229555; AJY58974.1; -; mRNA. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. 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; 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 2: Evidence at transcript level; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352}; KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000352}. FT DOMAIN 50..247 FT /note="Tubulin" FT /evidence="ECO:0000259|SMART:SM00864" FT DOMAIN 249..394 FT /note="Tubulin_C" FT /evidence="ECO:0000259|SMART:SM00865" FT REGION 430..451 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 451 AA; 49569 MW; 80136A3F086A9E1D CRC64; MRECISVHIG QAGIQVGNAC WELYCLEHGI QPDGQLMTGD KTVGGGDDAF STFFSETGAG KHVPRAVFLD LEPTVIDEVR TGAYRQLFHP EQLISGKEDA ANNFARGHYT IGKEIVDLCL DRIRKLADNC TGLQGFLVFN AVGGGTGSGL GSLLLERLSV DYGKKSKLGF TVYPSPQVST SVVEPYNSVL STHSLLEHTD VAVLLDNEAI YDICRRSLDI ERPTYTNLNR LVSQVISSLT ASLRFDGALN VDVTEFQTNL VPYPRIHFML SSYAPVISAE KAYHEQLSVA EITNSAFEPS SMMAKCDPRH GKYMACCLMF RGDVVPKDVN AAVATIKTKR TIQFVDWCPT GFKCGINYQP PTVVPGGDLA KVQRAVCMIS NSTSVAEVFS RIDHKFDLMY AKRAFVHWYV GEGMEEGEFS EAREDVAALE KDYEEVGADS TEPGDDEGEE Y //