ID   TBB3_PEA                Reviewed;         440 AA.
AC   P29502;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin beta-3 chain;
DE   AltName: Full=Beta-3-tubulin;
DE   Flags: Fragment;
GN   Name=TUBB3; Synonyms=TUB3;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Rosakrone;
RX   PubMed=1558942; DOI=10.1007/bf00020007;
RA   Liaud M.-F., Brinkmann H., Cerff R.;
RT   "The beta-tubulin gene family of pea: primary structures, genomic
RT   organization and intron-dependent evolution of genes.";
RL   Plant Mol. Biol. 18:639-651(1992).
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; X54846; CAA38615.1; -; mRNA.
DR   PIR; S20870; S20870.
DR   AlphaFoldDB; P29502; -.
DR   SMR; P29502; -.
DR   EnsemblPlants; Psat3g080760.1; Psat3g080760.1.cds; Psat3g080760.
DR   Gramene; Psat3g080760.1; Psat3g080760.1.cds; Psat3g080760.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           <1..440
FT                   /note="Tubulin beta-3 chain"
FT                   /id="PRO_0000048373"
FT   REGION          411..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..440
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         131..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   440 AA;  49512 MW;  8CAA5BE6D4C62133 CRC64;
     GQCGNQIGSK FWEVVCDEHG IDPTGRYVGN SDLQLERVNV YYNEASCGRF VPRAILMDLE
     PGTMDSVRTG PYGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELIDSVLDV VRKEAENCDC
     LQGFQVCHSL GGGTGSGMGT LLISKIREEY PDRMMLTFSV FPSPKVSDTV VEPYNATLSV
     HQLVENADEC MVLDNEALYD ICFRTLKLTT PSFGDLNHLI SATMSGVTCC LRFPGQLNSD
     LRKLAVNLIP FPRLHFFMVG FAPLTSRGSQ QYRALTVPEL TQQMWDSKNM MCAADPRHGR
     YLTASAMFRG KMSTKEVDEQ MINVQNKNSS YFVEWIPNNV KSSVCDIAPR GLSMASTFIG
     NSTSIQEMFR RVSEQFTAMF RRKAFLHWYT GEGMDEMEFT EAESNMNDLV SEYQQYQDAT
     ADEEGEYEDE EEEEPEHGYE