ID   TBB1_GLOMM              Reviewed;         447 AA.
AC   Q27U48;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fat body;
RX   PubMed=16907828; DOI=10.1111/j.1365-2583.2006.00649.x;
RA   Attardo G.M., Strickler-Dinglasan P., Perkin S.A.H., Caler E.,
RA   Bonaldo M.F., Soares M.B., El-Sayeed N.M.A., Aksoy S.;
RT   "Analysis of fat body transcriptome from the adult tsetse fly, Glossina
RT   morsitans morsitans.";
RL   Insect Mol. Biol. 15:411-424(2006).
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 (By similarity).
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; DQ377071; ABD60995.1; -; mRNA.
DR   AlphaFoldDB; Q27U48; -.
DR   SMR; Q27U48; -.
DR   STRING; 37546.Q27U48; -.
DR   PRIDE; Q27U48; -.
DR   VEuPathDB; VectorBase:GMOY000148; -.
DR   PhylomeDB; Q27U48; -.
DR   Proteomes; UP000092444; Unassembled WGS sequence.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..447
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000291646"
FT   REGION          427..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..447
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:0000250"
SQ   SEQUENCE   447 AA;  50161 MW;  9E6F6775C96731DB CRC64;
     MREIVHIQAG QCGNQIGAKF WEIISDEHGI DATGAYHGDS DLQLERINVY YNEASGGKYV
     PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTYSVV PSPKVSDTVV
     EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNIQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQEATA DEDAEFEEEQ EAEVEEN