ID TBB2_ANEPH Reviewed; 411 AA. AC P33631; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 01-OCT-2014, entry version 71. DE RecName: Full=Tubulin beta-2 chain; DE AltName: Full=Beta-2-tubulin; DE Flags: Fragment; GN Name=TUBB2; OS Anemia phyllitidis (Fern) (Osmunda phyllitidis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Moniliformopses; Polypodiidae; Schizaeales; Anemiaceae; Anemia. OX NCBI_TaxID=12940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Moepps B., Maucher H.P., Bogenberger J.M., Schraudolf H.; RT "Charcterization of the alpha and beta tubulin gene families from RT Anemia phyllitidis L.Sw."; RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases. 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 -!- 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 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; X69186; CAA48930.1; -; mRNA. DR PIR; S32669; S32669. DR PRIDE; P33631; -. 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; IPR002453; Beta_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; PR01163; BETATUBULIN. 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 Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding. FT CHAIN <1 411 Tubulin beta-2 chain. FT /FTId=PRO_0000048330. FT NP_BIND 108 114 GTP. {ECO:0000255}. FT NON_TER 1 1 SQ SEQUENCE 411 AA; 46218 MW; C66DC6A067F3A9A3 CRC64; TGTYRGDSET QLERVNVYYN EASCGRYVPR AVLMDLEPGT MDSVRSGPYG QIFRPDNFVF GQSGAGNNWA KGHYTEGAEL IDSVLDVVRK EAENCDCLQG FQVCHSLGGG TGSGMGTLLI SKIREEYPDR MMXTFSVFPS PKVSDTVVEP YNATLSVHQL VENADECMVL DNEALYDICF RTLKLVTPTF GDLNHLISAT MSGVTCCLRF PGQLNSDLRK LAVNLIPFPR LHFFMVGFAP LTSRGSQQYR ALTVPELTQQ MRDAKNMMCA ADPRHGRYLT ASAMFRGKMS TKEVDEQMIN VQNKNSSYFV EWIPNNVKSS VCDIPPVGLK MACTFIGNST SIQEMFRRVR DQFTAMFRXK AFLHWYTGEG MDEMEFTEAE SNMNDLVSEY QQYQDATAEP EGXYEEDYDE A //