ID   TBB2_GEOCN              Reviewed;         453 AA.
AC   P32925;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-2-tubulin;
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=1173061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1836049; DOI=10.1007/bf00290657;
RA   Gold S.E., Casale W.L., Keen N.T.;
RT   "Characterization of two beta-tubulin genes from Geotrichum candidum.";
RL   Mol. Gen. Genet. 230:104-112(1991).
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; S69627; AAB20557.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S18597; S18597.
DR   AlphaFoldDB; P32925; -.
DR   SMR; P32925; -.
DR   PRIDE; P32925; -.
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; 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   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..453
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048417"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   453 AA;  50399 MW;  2EA9D8A0246E0371 CRC64;
     MREIVSIQCG QAGMNQVSTA FWSTITDEHG LDADGHLRPD ASSLESDRLD VFFNEASNKK
     YVPRAVAVDL EPATLDAIRS GPLGHIYRPD NLISGESGAG NNWAKGFYTE GAELMDSVMD
     IIRREAEQSE SLQGFQLAHS LGGGTGSGLG TLLLTKIREE YPDRMLSTYS VLPSPKVSDT
     VTEPYNAVLS FHQLIDNADA TYCLDNEALY DICEKTLKIN RPSHQDLNSL IALVMSGVTT
     GLRYPGQLNG DLRKLAVNLV PFPRLHFFTT GFAPLFAKNS RAFHNLTVPE LTQQLFNPAN
     VMAACNPYHG RYLTISTIFR GQVAMKEVED AIHTARTKYS PYFVEWIPNN VQTSVCNVPP
     KGLTTSATFI ANSTAVQELF ERTANQFSVM FKRKGFLHWY TGEGMEPVEF SEAQSDLEDL
     ILEYQQYQNA GVDEDEELMD HEEYADEGVE DFN