ID   TBB1_SOYBN              Reviewed;         445 AA.
AC   P12459;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
GN   Name=TUBB1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND92001189; DOI=10.1007/BF00016154;
RA   Guiltinan M.J., Ma D.-P., Barker R.F., Bustos M.M., Cyr R.J., Yadegari R.,
RA   Fosket D.E.;
RT   "The isolation, characterization and sequence of two divergent beta-tubulin
RT   genes from soybean (Glycine max L.).";
RL   Plant Mol. Biol. 10:171-184(1987).
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; M21296; AAA34009.1; -; Genomic_DNA.
DR   PIR; JA0048; JA0048.
DR   AlphaFoldDB; P12459; -.
DR   SMR; P12459; -.
DR   STRING; 3847.GLYMA08G01740.1; -.
DR   PRIDE; P12459; -.
DR   ProMEX; P12459; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   InParanoid; P12459; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..445
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000048381"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  49991 MW;  E68E24260D9AE1DC CRC64;
     MREILHVQAG QCGNQIGGKF WEVMCDEHGI DATGNYVGNF HLQLERVNVY YNEASGGRYV
     PRAVLMDLEP GTMDSLRSGP FGKIFRPDNF VFGQNGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAENCDCL QGFQICHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF AVPEGSDTVV
     EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLTNP SFGDLNHLIS TTMSGVTCCL
     RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRSLTIPELT QQMWDARNMM
     CAADPRHGRY LTASAMFRGK MSTKEVDQQM INVQNKNSSY FVEWIPNNVK SSVCDIPPTG
     LSMSSTFMGN STSIQEMFRR VSEQFTVMFK RKAFLHWYTG EGMDEMEFTE VRANMNDLVA
     EYQQYQDATA VDDHEDEDED EAMAA