ID   TBB2_PHYPO              Reviewed;         454 AA.
AC   P12458;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Tubulin beta-major chain;
GN   Name=BETC;
OS   Physarum polycephalum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC   Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX   NCBI_TaxID=5791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2835667; DOI=10.1128/mcb.8.3.1275-1281.1988;
RA   Burland T.G., Paul E.C.A., Oetliker M., Dove W.F.;
RT   "A gene encoding the major beta tubulin of the mitotic spindle in Physarum
RT   polycephalum plasmodia.";
RL   Mol. Cell. Biol. 8:1275-1281(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   -!- FUNCTION: This is the major beta tubulin of mitotic spindle.
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, spindle. Nucleus.
CC       Note=Mitosis in the slime mold Plasmodium differs from the process in
CC       many eukaryotes. The tubulin chains must be transported to the nuclei
CC       for intranuclear assembly of the spindle.
CC   -!- DEVELOPMENTAL STAGE: Preferentially expressed in Plasmodium.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; M20191; AAA29977.1; -; mRNA.
DR   PIR; A33655; A33655.
DR   AlphaFoldDB; P12458; -.
DR   SMR; P12458; -.
DR   PRIDE; P12458; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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;
KW   Nucleus.
FT   CHAIN           1..454
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048310"
FT   REGION          426..454
FT                   /note="Disordered"
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   454 AA;  50364 MW;  A913D46AF63F1AD4 CRC64;
     MREIVHVQVG QCGNQVGAKF WEVVSEEHGI DSAGTYKGDT DLQLERINVY YNEVAGSKYV
     PRAVLVDLEP GVLDSIRASS IGSMFRPDNF THAQSGAGNN WAKGHYTEGA ELVESVVDVV
     RKEAENCDCL QGFQICHSLG GGTGSGLGTL LISKIREEFP DRMMCTFSVM PSPKVSDTVV
     EPYNATLSIH QLVENADEVM CIDNEALYDI CFRTLKLTTP TYGDLNHLVS GVMSGITACL
     RFPGQLNSDL RKLAVNLIPF PRLHFFLIGY APLTARSAMG FRALTVPELT QQIFDSRNMM
     AASDPRHGRY LTASATFRGK MSTKEVDEQM HAVQTKNSSF FVEWIPNNIK SSVCDIPPKG
     MKMSATFIGN NTCIQELFKR IGLQFSAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQEASV DDEAMEDDAE AEGGAGQNEA VEEF