ID   TBB3_OOMCK              Reviewed;         445 AA.
AC   P50261;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Tubulin beta-3 chain;
DE   AltName: Full=Beta-3-tubulin;
GN   Name=TUBB3;
OS   Oomycete-like sp. (strain MacKay2000).
OC   Eukaryota; Sar; Stramenopiles.
OX   NCBI_TaxID=129195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mackay R.M., Gallant J.W.;
RT   "Expression of beta-tubulin genes in the sporophyte and gametophyte of the
RT   red alga Porphyra purpurea.";
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REVISES SPECIES OF ORIGIN.
RX   PubMed=9783459; DOI=10.1111/j.1550-7408.1998.tb05117.x;
RA   Keeling P.J., Deane J.A., McFadden G.I.;
RT   "The phylogenetic position of alpha- and beta-tubulins from the
RT   Chlorarachnion host and Cercomonas (Cercozoa).";
RL   J. Eukaryot. Microbiol. 45:561-570(1998).
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   -!- CAUTION: Was originally (Ref.1) thought to originate from Porphyra
CC       purpurea. {ECO:0000305}.
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DR   EMBL; Z67993; CAA91941.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50261; -.
DR   SMR; P50261; -.
DR   PRIDE; P50261; -.
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..445
FT                   /note="Tubulin beta-3 chain"
FT                   /id="PRO_0000048377"
FT   REGION          417..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..445
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  49743 MW;  8482D4230F0174F9 CRC64;
     MREIVHIQAG QCGNQIGAKF WQVISDEHGV DPTGTYKGDS DLQLERINVY YNEATGGRYV
     PRAVLIDLEP GTMDAVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
     RNEAESCDCL QGFQMTHSLG GGTGSGMGTL LIAKLREEYP DRVMMTFSVC PSPKVSDTVV
     EPYNATLSVH QIVENTDESF VLDNEALYDI CFRTLKLTTP TYGDLNHLVC VCMSGVTSSL
     RFPGQLNCDL RKVAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQCFDAKNMM
     CAADPRHGRF LTASCMFRGR MSTKEVDEQM LNVQTKNSSY FVEWIPNNIK ASVCDIPPKG
     LKMSSTFVGN STAIQEMFKR VGEQFTAMYK RKAFLHWYTG EGMDDMEFTE AESNMNDLVS
     EYQQYQEASA DDEADEFDEE EGDEE