ID   TBB_TRYBR               Reviewed;         442 AA.
AC   P04107;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Trypanosoma brucei rhodesiense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=31286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=4043732; DOI=10.1016/0378-1119(85)90002-2;
RA   Kimmel B.E., Samson S., Wu J., Hirschberg R., Yarbrough L.R.;
RT   "Tubulin genes of the African trypanosome Trypanosoma brucei rhodesiense:
RT   nucleotide sequence of a 3.7-kb fragment containing genes for alpha and
RT   beta tubulins.";
RL   Gene 35:237-248(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 AND 433-442.
RX   PubMed=2994042; DOI=10.1073/pnas.82.17.5695;
RA   Sather S., Agabian N.;
RT   "A 5' spliced leader is added in trans to both alpha- and beta-tubulin
RT   transcripts in Trypanosoma brucei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:5695-5699(1985).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; K02836; AAA30261.1; -; Genomic_DNA.
DR   EMBL; M11747; AAA30265.1; -; Genomic_DNA.
DR   EMBL; M11748; AAA30268.1; -; Genomic_DNA.
DR   PIR; A02976; UBUTB.
DR   AlphaFoldDB; P04107; -.
DR   SMR; P04107; -.
DR   PRIDE; P04107; -.
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..442
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048319"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   442 AA;  49704 MW;  628D04DB20170A4B CRC64;
     MREIVCVQAG QCGNQIGSKF WEVISDEHGV DPTGTYQGDS DLQLERINVY FDEATGGRYV
     PRSVLIDLEP GTMDSVRAGP YGQIFRPDNF IFGQSGAGNN WAKGHYTEGA ELIDSVLDVC
     CKEAESCDCL QGFQICHSLG GGTGSGMGTL LISKLREQYP DRIMMTFSII PSPKVSDTVV
     EPYNTTLSVH QLVENSDESM CIDNEALYDI CFRTLKLTTP TFGDLNHLVS AVVSGVTCCL
     RFPGQLNSDL RKLAVNLVPF PRLHFFMMGF APLTSRGSQQ YRGLSVPELT QQMFDAKNMM
     QAADPRHGRY LTASALFRGR MSTKEVDEQM LNVQNKNSSY FIEWIPNNIK SSVCDIPPKG
     LKMAVTFIGN NTCIQEMFRR VGEQFTLMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATI EEEGEFDEEE QY