TBB_EUGGR
ID TBB_EUGGR Reviewed; 442 AA.
AC P12457;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUBB;
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Z 1224 5/25;
RX PubMed=2506525; DOI=10.1093/nar/17.16.6727;
RA Schantz M.-L., Schantz R.;
RT "Sequence of a cDNA clone encoding beta tubulin from Euglena gracilis.";
RL Nucleic Acids Res. 17:6727-6727(1989).
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; X15797; CAA33797.1; -; mRNA.
DR PIR; S05496; S05496.
DR AlphaFoldDB; P12457; -.
DR SMR; P12457; -.
DR PRIDE; P12457; -.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..442
FT /note="Tubulin beta chain"
FT /id="PRO_0000048346"
FT BINDING 138..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 442 AA; 49418 MW; F25CBFA9C7496989 CRC64;
MREIVHIQAG QCGNQIGSKF WEVISDEQGV DPPDIPGDSD LQLERINVYY NEATGGRYVP
AILMDLEPGT MDSVRAGPYG QIFRPDNFVF GQTGAGNNWA KGHYTEGPEL IDSVLDVVRK
EAESCDCLQG FQIAHSLGGG TGSGMGTLLI SKIREEYPDR MMMTFSVIPS PKVSDTVVEP
YNTTLSVHQL VENADEVMCI GNEALYDICL PTLKLTTPTF GHETLVSAVM SGVTCCLRFP
GQLNSDLRKL AVNLIPFPRL HFFLVGFAPL TSRGSQQYRA LTVPELTQQM FDAKNMMAAS
DPAHGRYLTA SAMFRGRMST KEVDEQMLNV QNKNSSYFVE WIPNNIKSSV CDIPPKGLKM
SATFIGNNTA IQEMFKRVSE QFTAMFRRKA FLHWYTGEGM DEMEFTEAES NMNDLVSEYQ
QYQDATVEEE GEFDEEEDVE QY