TBB_GIAIN
ID TBB_GIAIN Reviewed; 446 AA.
AC P05304;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3267222; DOI=10.1093/nar/16.6.2733;
RA Kirk-Mason K.E., Turner M.J., Chakraborty P.R.;
RT "Cloning and sequence of beta tubulin cDNA from Giardia lamblia.";
RL Nucleic Acids Res. 16:2733-2733(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; X06748; CAA29923.1; -; mRNA.
DR PIR; S00743; S00743.
DR AlphaFoldDB; P05304; -.
DR SMR; P05304; -.
DR PRIDE; P05304; -.
DR VEuPathDB; GiardiaDB:DHA2_153187; -.
DR VEuPathDB; GiardiaDB:GL50581_1380; -.
DR VEuPathDB; GiardiaDB:GL50803_00136021; -.
DR eggNOG; KOG1375; Eukaryota.
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..446
FT /note="Tubulin beta chain"
FT /id="PRO_0000048297"
FT REGION 427..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
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 446 AA; 49956 MW; 517FA5DDCE288FC7 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGV DPSGEYRGDS ELQIERINVY FNEAAGGRYV
PRAILVDLEP GTMDSVRAGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDAVLDVV
RKRSEACDCL QGFQICHSLG GGTGAGMGTL LIAKIREEYP DRMMCTFSVV PSPKVSDTVV
EPYNATLSVH QLVEHADEVF CIDNEALYDI CFRTLKLTCP TYGDLNHLVS LVMSGCTSCL
RFPGQLNADL RKLAVNLIPF PRLHFFLVGF APLTSRGSQI YRALTVPELV SQMFDNKNMM
AASDPRHGRY LTAAAMFRGR MSTKEVDEQM LNIQNKNSSY FVEWIPNNMK VSVCDIPPRG
LKMAATFIGN STCIQELFKR VGEQFSAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEAGV DEGEEFEEEE DFGDEQ