ID A0A0D5MER0_CLOEH Unreviewed; 451 AA. AC A0A0D5MER0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 20-DEC-2017, entry version 21. DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352}; 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. CC {ECO:0000256|RuleBase:RU000352, ECO:0000256|SAAS:SAAS00103398}. CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is CC a hollow water-filled tube with an outer diameter of 25 nm and an CC inner diameter of 15 nM. Alpha-beta heterodimers associate head- CC to-tail to form protofilaments running lengthwise along the CC microtubule wall with the beta-tubulin subunit facing the CC microtubule plus end conferring a structural polarity. CC Microtubules usually have 13 protofilaments but different CC protofilament numbers can be found in some organisms and CC specialized cells. {ECO:0000256|RuleBase:RU000352, CC ECO:0000256|SAAS:SAAS00810909}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000256|SAAS:SAAS00103388}. CC -!- SIMILARITY: Belongs to the tubulin family. CC {ECO:0000256|RuleBase:RU000352, ECO:0000256|SAAS:SAAS00576975}. 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-UniRule. DR GO; GO:0003924; F:GTPase activity; 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; 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; IPR037103; Tubulin/FtsZ_C_sf. DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf. 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:RU000352, KW ECO:0000256|SAAS:SAAS00033556}; KW Microtubule {ECO:0000256|RuleBase:RU000352, KW ECO:0000256|SAAS:SAAS00576796}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000352, KW ECO:0000256|SAAS:SAAS00432823}. FT DOMAIN 50 247 Tubulin. {ECO:0000259|SMART:SM00864}. FT DOMAIN 249 394 Tubulin_C. {ECO:0000259|SMART:SM00865}. 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 //