ID A0A0D5MER0_CLOEH Unreviewed; 451 AA. AC A0A0D5MER0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 29-MAY-2024, entry version 36. 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, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to CC GTPase activity of alpha-tubulin. {ECO:0000256|RuleBase:RU000352}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000256|ARBA:ARBA00001702}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000256|ARBA:ARBA00001702}; 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 AlphaFoldDB; A0A0D5MER0; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:TreeGrafter. DR GO; GO:0000278; P:mitotic cell cycle; IEA:TreeGrafter. DR CDD; cd02186; alpha_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; 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; TUBULIN; 1. DR PANTHER; PTHR11588:SF239; TUBULIN ALPHA CHAIN; 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; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. PE 2: Evidence at transcript level; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; 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/FtsZ GTPase" FT /evidence="ECO:0000259|SMART:SM00864" FT DOMAIN 249..394 FT /note="Tubulin/FtsZ 2-layer sandwich" 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 //