TBB1_PARTE
ID TBB1_PARTE Reviewed; 442 AA.
AC P33188; Q546B0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=bPT2; ORFNames=GSPATT00021361001;
GN and
GN Name=bPT3; ORFNames=GSPATT00036831001;
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Stock d4-2;
RX PubMed=1339345; DOI=10.1002/j.1460-2075.1992.tb05456.x;
RA Dupuis P.;
RT "The beta-tubulin genes of Paramecium are interrupted by two 27 bp
RT introns.";
RL EMBO J. 11:3713-3719(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14871951; DOI=10.1128/ec.3.1.212-220.2004;
RA Ruiz F., Dupuis-Williams P., Klotz C., Forquignon F., Bergdoll M.,
RA Beisson J., Koll F.;
RT "Genetic evidence for interaction between eta- and beta-tubulins.";
RL Eukaryot. Cell 3:212-220(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2;
RX PubMed=17086204; DOI=10.1038/nature05230;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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; X67237; CAA47663.1; -; Genomic_DNA.
DR EMBL; AJ608918; CAE75645.1; -; Genomic_DNA.
DR EMBL; AJ608919; CAE75646.1; -; Genomic_DNA.
DR EMBL; CT868056; CAK68048.1; -; Genomic_DNA.
DR EMBL; CT868629; CAK87728.1; -; Genomic_DNA.
DR PIR; S25182; S25182.
DR RefSeq; XP_001435445.1; XM_001435408.1.
DR RefSeq; XP_001455125.1; XM_001455088.1.
DR AlphaFoldDB; P33188; -.
DR SMR; P33188; -.
DR STRING; 5888.CAK68048; -.
DR EnsemblProtists; CAK68048; CAK68048; GSPATT00036831001.
DR EnsemblProtists; CAK87728; CAK87728; GSPATT00021361001.
DR GeneID; 5021230; -.
DR GeneID; 5040910; -.
DR KEGG; ptm:GSPATT00021361001; -.
DR KEGG; ptm:GSPATT00036831001; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P33188; -.
DR OMA; VCSVAPK; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
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..442
FT /note="Tubulin beta chain"
FT /id="PRO_0000048307"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 442 AA; 49456 MW; B080F67A714B016A CRC64;
MREIVHIQGG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGRYV
PRAILMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAEGCDCL QGFQITHSLG GGTGSGMGTL LISKVREEYP DRIMETFSVV PSPKVSDTVV
EPYNATLSVH QLVENADECM VIDNEALYDI CFRTLKLTTP TYGDLNHLVS AAMSGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
CAADPRHGRY LTASALFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK SSICDIPPKG
LKMAVTFVGN STAIQEMFKR VAEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFEEEG EQ
