TBB_CHLRE
ID TBB_CHLRE Reviewed; 443 AA.
AC P04690;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Tubulin beta-1/beta-2 chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUBB1;
GN and
GN Name=TUBB2;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6098820; DOI=10.1128/mcb.4.12.2686-2696.1984;
RA Youngblom J., Schloss J.A., Silflow C.D.;
RT "The two beta-tubulin genes of Chlamydomonas reinhardtii code for identical
RT proteins.";
RL Mol. Cell. Biol. 4:2686-2696(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
RX PubMed=6738533; DOI=10.1128/mcb.4.6.1115-1124.1984;
RA Brunke K.J., Anthony J.G., Sternberg E.J., Weeks D.P.;
RT "Repeated consensus sequence and pseudopromoters in the four coordinately
RT regulated tubulin genes of Chlamydomonas reinhardi.";
RL Mol. Cell. Biol. 4:1115-1124(1984).
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 -!- MISCELLANEOUS: The 2 beta-tubulin genes of Chlamydomonas (beta-1 and
CC beta-2) encode the same protein.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M10064; AAA33101.1; -; Genomic_DNA.
DR EMBL; K03281; AAA33102.1; -; Genomic_DNA.
DR EMBL; K01808; AAA33099.1; -; Genomic_DNA.
DR EMBL; K01809; AAA33100.1; -; Genomic_DNA.
DR PIR; A29141; UBKM.
DR RefSeq; XP_001693997.1; XM_001693945.1.
DR RefSeq; XP_001694072.1; XM_001694020.1.
DR PDB; 6U42; EM; 3.40 A; 0A/0C/0E/0G/0I/0K/0M/0O/0Q/0S/0U/0W/0Y/1/1A/1C/1E/1G/1K/1M/1O/1Q/1S/1U/1W/2A/2C/2E/2G/2I=1-443.
DR PDB; 6VE7; EM; 3.60 A; 4/8/9/I/J/K/N/O/Q/R/T/U/V/a/b/i/j/p/q/r/t/u/v/w=1-443.
DR PDB; 7JU4; EM; 3.40 A; 6/8/C/G/I/K/O/Q/S/W/Y/i/k/y=1-443.
DR PDB; 7KZM; EM; 7.50 A; A1/A3/A5/A7/B1/B3/B5/B7=1-443.
DR PDB; 7KZO; EM; 3.30 A; A1/A3/A5/A7/B1/B3/B5/B7=1-443.
DR PDB; 7SOM; EM; 3.70 A; AA/AC/AE/AG/AI/AK/BA/BC/BE/BG/BI/BK/CA/CC/CE/CG/CI/CK/DC/DE/DG/DI/DK/EA/EC/EE/EG/EI/EK/FA=1-443.
DR PDB; 7SQC; EM; 3.80 A; NC/NE/NG/NI/NK/NM/NO/OC/OE/OG/OI/OK/OM/OO/OQ/PC/PE/PG/PI/PK/PM/PO/PQ/QC/QE/QG/QI/QK/QM/QO=1-443.
DR PDBsum; 6U42; -.
DR PDBsum; 6VE7; -.
DR PDBsum; 7JU4; -.
DR PDBsum; 7KZM; -.
DR PDBsum; 7KZO; -.
DR PDBsum; 7SOM; -.
DR PDBsum; 7SQC; -.
DR AlphaFoldDB; P04690; -.
DR SMR; P04690; -.
DR STRING; 3055.EDP02933; -.
DR PRIDE; P04690; -.
DR ProMEX; P04690; -.
DR EnsemblPlants; PNW76052; PNW76052; CHLRE_12g549550v5.
DR EnsemblPlants; PNW76245; PNW76245; CHLRE_12g542250v5.
DR GeneID; 5719519; -.
DR GeneID; 5719644; -.
DR Gramene; PNW76052; PNW76052; CHLRE_12g549550v5.
DR Gramene; PNW76245; PNW76245; CHLRE_12g542250v5.
DR KEGG; cre:CHLRE_12g542250v5; -.
DR KEGG; cre:CHLRE_12g549550v5; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR OMA; ECMILDN; -.
DR OrthoDB; 962471at2759; -.
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; 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 3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding.
FT CHAIN 1..443
FT /note="Tubulin beta-1/beta-2 chain"
FT /id="PRO_0000048335"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Acidic residues"
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 443 AA; 49619 MW; 5967934FCA8FDB8C CRC64;
MREIVHIQGG QCGNQIGAKF WEVVSDEHGI DPTGTYHGDS DLQLERINVY FNEATGGRYV
PRAILMDLEP GTMDSVRSGP YGQIFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAESCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVV PSPKVSDTVV
EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLTTP TFGDLNHLIS AVMSGITCCL
RFPGQLNADL RKLAVNLIPF PRLHFFMVGF TPLTSRGSQQ YRALTVPELT QQMWDAKNMM
CAADPRHGRY LTASALFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK SSVCDIPPKG
LKMSATFIGN STAIQEMFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDASA EEEGEFEGEE EEA
