ID   TBB_CANAX               Reviewed;         449 AA.
AC   P10875;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
GN   Name=TUB2;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3290053; DOI=10.1016/0378-1119(88)90545-8;
RA   Smith R.A., Allaudeen H.S., Whitman M.H., Koltin Y., Gorman J.A.;
RT   "Isolation and characterization of a beta-tubulin gene from Candida
RT   albicans.";
RL   Gene 63:53-63(1988).
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; M19398; AAA34375.1; -; Genomic_DNA.
DR   PIR; JT0276; UBCKBA.
DR   AlphaFoldDB; P10875; -.
DR   SMR; P10875; -.
DR   ChEMBL; CHEMBL3988634; -.
DR   DrugBank; DB00400; Griseofulvin.
DR   DrugCentral; P10875; -.
DR   VEuPathDB; FungiDB:C1_00710C_A; -.
DR   VEuPathDB; FungiDB:CAWG_01302; -.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:EnsemblFungi.
DR   GO; GO:0005876; C:spindle microtubule; IEA:EnsemblFungi.
DR   GO; GO:0045298; C:tubulin complex; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:EnsemblFungi.
DR   GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR   GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:EnsemblFungi.
DR   GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi.
DR   GO; GO:0000022; P:mitotic spindle elongation; IEA:EnsemblFungi.
DR   GO; GO:1903087; P:mitotic spindle pole body duplication; IEA:EnsemblFungi.
DR   GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; IEA:EnsemblFungi.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; IEA:EnsemblFungi.
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..449
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048397"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   449 AA;  49942 MW;  FFC2C7F22AD59459 CRC64;
     MREIIHLSTG QCGNQIGAAF WETICGEHGL DNNGTYVGNN ELQKSKLDVY FNEATSGKYV
     PRAVLVDLEP GTIDNVKTSQ IGNLFRPDNF IFGQSSAGNV WAKGHYTEGA ELVDSVLDVV
     RREAEGCDSL QGFQITHSLG GGTGSGMGTL LISKIREEFP DTMMATFSVV PSPKVSDTVI
     EPYNATLSVH QLVENSDETF CIDNEALYNI CQNTLKLPQP SYAELNNLVS SVMSGVTTSL
     RYPGQLNSDL RKLAVNLVPF PRLHFFMVGY APLTSMGSKS FRSVTVPELT QQMFDAKNMM
     AASDPRNGRY LTVAAFFRGK VSVKEVDDEM HKIQTRNSSY FVDWIPNNVQ TAVCSVPPKD
     LDMSATFIGN STSIQELFKR VGDQFSAMFR RKAFLHWYTS EGMDEMEFTE AESNMNDLVS
     EYQQYQEASI DEEELEYADE IPLEDAAME