ID   TBB2_PEA                Reviewed;         447 AA.
AC   P29501;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-2-tubulin;
DE   Flags: Fragment;
GN   Name=TUBB2; Synonyms=TUB2;
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; X54845; CAA38614.1; -; mRNA.
DR   PIR; S20869; S20869.
DR   AlphaFoldDB; P29501; -.
DR   SMR; P29501; -.
DR   PRIDE; P29501; -.
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..447
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048372"
FT   REGION          411..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..447
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         138..144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   447 AA;  50401 MW;  51607435DA236526 CRC64;
     EIVHIQGGQC GNQIGAKFWE VVCAEHGIDP TGRYGGDTDL QLERINVYYN EASCGRYVPR
     AVLMDLEPGT MDSVRSGPYG QIFRPDNFVF GQSGAGNNWA KGHYTEGAEL IDSVLDVVRK
     EAENCDCLQG FQVCHSLGGG TGSGMGTLLI SKIREEYPDR MMLTFSVFPS PKVSDTVVEP
     YNATLSVHQL VENADECMVL DNEALYDICF RTLKLTTPSF GDLNHLISAT MSGVTCCLRF
     PGQLNSDLRK LAVNLIPFPR LHFFMLGFAP LTSRGSQQYR ALSVPEITQQ MWDSKNMMCA
     ADPRHGRYLT ASAIFRGKMS TKEVDEQMMN VQNKNSSYFV EWIPNNVKST VCDIPPTGLK
     MASTFIGNST SIQEMFRRVS EQFTAMFRRK AFLHWYTGEG MDEMEFTEAE SNMNDLVSEY
     QQYQDATAEE DEYEEEEEDY HQEHDEM