ID   TBB1_BRUPA              Reviewed;         448 AA.
AC   P18241;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2052017; DOI=10.1016/0166-6851(91)90001-m;
RA   Guenette S., Prichard R.K., Klein R.D., Matlashewski G.;
RT   "Characterization of a beta-tubulin gene and a beta-tubulin gene products
RT   of Brugia pahangi.";
RL   Mol. Biochem. Parasitol. 44:153-164(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-448.
RX   PubMed=2685715; DOI=10.1111/j.1365-3024.1989.tb00683.x;
RA   Helm R., Selkirk M.E., Bradley J.E., Burns R.G., Hamilton A.J., Croft S.,
RA   Maizels R.M.;
RT   "Localization and immunogenicity of tubulin in the filarial nematodes
RT   Brugia malayi and B. pahangi.";
RL   Parasite Immunol. 11:479-502(1989).
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; M36380; AAA27865.1; -; Genomic_DNA.
DR   PIR; A60645; A60645.
DR   AlphaFoldDB; P18241; -.
DR   SMR; P18241; -.
DR   STRING; 6280.P18241; -.
DR   PRIDE; P18241; -.
DR   WBParaSite; BPAG_0000048501-mRNA-1; BPAG_0000048501-mRNA-1; BPAG_0000048501.
DR   Proteomes; UP000038020; Unplaced.
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..448
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000048284"
FT   REGION          427..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..448
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   448 AA;  50191 MW;  65BB5BB9384A8735 CRC64;
     MREIVHVQAG QCGNQIGAKF WEVISDEHGV QPDGTYKGDS DLQIERINVY YNEANGGKYV
     PRAVLVDLEP GTMDSIRGGE FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDNVLDVI
     RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMSSFSVV PSPKVSDVVL
     EPYNATLSVH QLVENTDETF CIDNEALYDI CFRTLKLANP TYGDLNHLVS VTMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLSARDAAA YRALNVAELT QQMFDAKNMM
     AACDPRHGRY LTVAAMFRGR MSMREVDEQM MQVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMSATFIGN TTAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA DEEGDLQEGE SEYIEQEE