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 23-FEB-2022, entry version 84. 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 Polypodiopsida; 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 "Characterization of the alpha and beta tubulin gene families from Anemia RT phyllitidis L.Sw."; RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases. 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 -!- 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. 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 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; 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; 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 FT /note="Tubulin beta-2 chain" FT /id="PRO_0000048330" FT NP_BIND 108..114 FT /note="GTP" FT /evidence="ECO:0000255" FT REGION 390..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 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 //