ID   TBB2_SOLTU              Reviewed;         452 AA.
AC   P46264;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-2-tubulin;
GN   Name=TUBB2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7999992; DOI=10.1007/bf00028869;
RA   Taylor M.A., Wright F., Davies H.V.;
RT   "Characterisation of the cDNA clones of two beta-tubulin genes and their
RT   expression in the potato plant (Solanum tuberosum L.).";
RL   Plant Mol. Biol. 26:1013-1018(1994).
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; Z33402; CAA83853.1; -; mRNA.
DR   PIR; S50748; S50748.
DR   AlphaFoldDB; P46264; -.
DR   SMR; P46264; -.
DR   InParanoid; P46264; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P46264; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR013838; Beta-tubulin_BS.
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.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..452
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048380"
FT   REGION          414..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..444
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         143..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  50625 MW;  591A876DC6DEAC70 CRC64;
     MREILHIQGG QCGNQIGSKF WEVICDEHGV DPTGRYKGTA AESDLQLERI NVYFNEASGG
     RYVPRAVLMD LEPGTMDSIR SGPYGQIFRP DNLVFGQSGA GNNWAKGHYT EGAELIDAVL
     DVVRKEAENC DCLQGFQVCH SLGGGTGSGM GTLLISKVRE EYPDRMMLTF SVFPSPKVSD
     TVVEPYNATL SVHQLVENAD ECMVLDNEAL YDICFRTLKL TTPSFGDLNH LISATMSGVT
     CCLRFPGQLN SDLRKLAVNL IPLPRLHFFM VGFAPLTSRG SQQYISLTVP ELTQQMWDAK
     NMMCAADPRH GRYLTASAMF RGKMSTKEVD EQMINVQNKN SSYFVEWIPN NVKSSVCDIP
     PTGLKMASTF VGNSTSIQEM FRRVSEQFTA MFRRKAFLHW YTGEGMDEME FTEAESNMND
     PVAEYQQYQD ATADDEEEYD DEAADDHHQY ES