TBB1_PHYPO
ID TBB1_PHYPO Reviewed; 467 AA.
AC P07436;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 4.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=BETA;
GN and
GN Name=BETB;
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.
RC STRAIN=LU352;
RA Paul E.C.A., Buchschacher G.L. Jr., Cunningham D.B., Dove W.F.,
RA Burland T.G.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-445.
RC STRAIN=LU352;
RX PubMed=1556551; DOI=10.1099/00221287-138-1-229;
RA Paul E.C.A., Buchschacher G.L. Jr., Cunningham D.B., Dove W.F.,
RA Burland T.G.;
RT "Preferential expression of one beta-tubulin gene during flagellate
RT development in Physarum.";
RL J. Gen. Microbiol. 138:229-238(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-207.
RC STRAIN=CL;
RX PubMed=3391166; DOI=10.1111/j.1432-1033.1988.tb14125.x;
RA Werenskiold A.K., Poetsch B., Haugli F.;
RT "Cloning and expression of a beta tubulin gene of Physarum polycephalum.";
RL Eur. J. Biochem. 174:491-495(1988).
RN [4]
RP PROTEIN SEQUENCE OF 1-217; 234-262 AND 277-286.
RX PubMed=3539596; DOI=10.1111/j.1432-1033.1986.tb10492.x;
RA Singhofer-Wowra M., Clayton L., Dawson P., Gull K., Little M.;
RT "Amino-acid sequence data of beta-tubulin from Physarum polycephalum
RT myxamoebae.";
RL Eur. J. Biochem. 161:669-679(1986).
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, 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: BetA is preferentially expressed in flagellate and
CC BetB in amoeba.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M58521; AAA29974.1; -; mRNA.
DR EMBL; X12371; CAA30932.1; -; Genomic_DNA.
DR PIR; A25342; A25342.
DR PIR; A44848; A44848.
DR PIR; S02532; S02532.
DR AlphaFoldDB; P07436; -.
DR SMR; P07436; -.
DR PRIDE; P07436; -.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW Microtubule; Nucleotide-binding; Nucleus.
FT CHAIN 1..467
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048309"
FT REGION 429..448
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"
FT VARIANT 39
FT /note="E -> D (in BETB)"
FT VARIANT 283
FT /note="S -> A (in BETB)"
FT CONFLICT 165
FT /note="C -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="A -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="C -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 52134 MW; BA2C330A66FDC964 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGES DLQLERINVY YNEATGGKYV
PRAVLVDLEP GTMDSVRAGP FGQIFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAESCDCL QGFQIAHSLG GGTGSGMGTL LISKIREEYP DRMMCTFSVV PSPKVSDTVV
EPYNATLSVH QLVENADEVM CIDNEALYDI SFRTLKLTTP TYGDLNHLVS AVMSGITCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFLVGF APLTSRGSVG YRSLTVPELT QQMFDAKNMM
AASDPRHGRY LTASAMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK SSVCDIPPKG
LKMAVTFIGN STAIQELFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATI DDEEGGEEEE GGAEEEARQR KHYVIDYVPS VCVILIR
