ID   TBB3_ELEIN              Reviewed;         446 AA.
AC   Q9ZPN8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Tubulin beta-3 chain;
DE   AltName: Full=Beta-3-tubulin;
GN   Name=TUBB3; Synonyms=TUB3;
OS   Eleusine indica (Goosegrass) (Cynosurus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Chloridoideae; Cynodonteae; Eleusininae; Eleusine.
OX   NCBI_TaxID=29674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10080708; DOI=10.1023/a:1006108412801;
RA   Yamamoto E., Baird W.V.;
RT   "Molecular characterization of four beta-tubulin genes from dinitroaniline
RT   susceptible and resistant biotypes of Eleusine indica.";
RL   Plant Mol. Biol. 39:45-61(1999).
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; AF059289; AAD20180.1; -; mRNA.
DR   AlphaFoldDB; Q9ZPN8; -.
DR   SMR; Q9ZPN8; -.
DR   PRIDE; Q9ZPN8; -.
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-3 chain"
FT                   /id="PRO_0000048344"
FT   REGION          423..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..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;  50107 MW;  9EA9E0C9C2AD9FBE CRC64;
     MREILHIQGG QCGNQIGAKF WEVICDEHGI DHTGKYAGDS DLQLERINVY YNEAGGGRFV
     PRAVLMDLEP GTMDSLRSGP YGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLATP TFGDLNHLIS ATMSGVTCCL
     RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRSLTVPELT QQMWDAKNMM
     CAADPRHGRY LTASAMFRGK MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK SSVCDIPPRG
     LTMSSTFIGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVA
     EYQQYQDATA EEEEEYDDDE EEEVAA