ID A0A0D5MER0_CLOEH Unreviewed; 451 AA. AC A0A0D5MER0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 11-NOV-2015, entry version 5. DE SubName: Full=Alpha-tubulin {ECO:0000313|EMBL:AJY58974.1}; OS Closterium ehrenbergii (Green alga). OC Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Desmidiales; OC 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 RT study of the green alga Closterium ehrenbergii using quantitative RT real-time PCR."; RL Ecotoxicology 0:0-0(2015). 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 (By CC similarity). {ECO:0000256|SAAS:SAAS00207870}. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC {ECO:0000256|RuleBase:RU003505}. CC -!- SIMILARITY: Belongs to the tubulin family. CC {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:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro. DR GO; GO:0051258; P:protein polymerization; 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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00103391}; KW Cytoskeleton {ECO:0000256|SAAS:SAAS00103395}; KW GTP-binding {ECO:0000256|RuleBase:RU000351, KW ECO:0000256|SAAS:SAAS00033556}; KW Microtubule {ECO:0000256|RuleBase:RU000352, KW ECO:0000256|SAAS:SAAS00328831}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000351, KW ECO:0000256|SAAS:SAAS00033492}. FT COILED 419 439 {ECO:0000256|SAM:Coils}. 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 //