ID   TBB2_SUIBO              Reviewed;         445 AA.
AC   Q8J1R4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-2-tubulin;
GN   Name=TUBB2;
OS   Suillus bovinus (Jersey cow bolete) (Boletus bovinus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX   NCBI_TaxID=48563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Juuti J.T., Jokela S.;
RT   "The second beta tubulin gene of ectomycorrhizal basidiomycete Suillus
RT   bovinus.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SBH1;
RX   PubMed=15770509; DOI=10.1007/s00294-005-0564-6;
RA   Juuti J.T., Jokela S., Tarkka M.T., Paulin L., Lahdensalo J.;
RT   "Two phylogenetically highly distinct beta-tubulin genes of the
RT   basidiomycete Suillus bovinus.";
RL   Curr. Genet. 47:253-263(2005).
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}.
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DR   EMBL; AJ509091; CAD48933.1; -; mRNA.
DR   EMBL; AJ698041; CAG27309.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J1R4; -.
DR   SMR; Q8J1R4; -.
DR   PRIDE; Q8J1R4; -.
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..445
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048432"
FT   BINDING         143..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  49484 MW;  2AC581F6FD161F2F CRC64;
     MSREIVNIQA GQAGNQVGEA FWRMLLAEHG LDDAGMYKGN DPQQIARAGV YFTQVDSSGP
     TKYVPRSVQV DLESGVCNRL RSGPLGQLFR PDTYFTSDSG AGNNWAKGYY TEGAELIDGI
     LDIVRRQCEA TEALQGFQMI HSLGGGTGAG LGSLLLSKLR EEYPDRMLST FSILPAPNVS
     ETVVEPYNSL LSIHQLVDNC DLTICIDNEA LYDIAVRTLK IKSPGYKDLN QLIAKVMCGV
     STSLRFPGQL NGDLRKLGMN LVPFPRLHFL MPSFAPFYDP KARTFQRLSV SELTSSLFDK
     KNLLVASDPR FGRYLTAACI FRGKVSSHEA ENSVMQLQRK NSNLFVEWIP DNVSVSLCSV
     PPVGQPQAAV ALANSTCMQE LFKRNLDQFA LMFKRRAFLH WYTGEGMDVM EFTEAESNTQ
     DLISEYQQYQ EATVEEEEAD IEGEQ