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   03-AUG-2022, entry version 85.
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: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   REGION          390..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         108..114
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
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