TBB1_CYAPA
ID TBB1_CYAPA Reviewed; 447 AA.
AC Q9ZSW1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=TUBB1;
OS Cyanophora paradoxa.
OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Keeling P., Hink-Schauer C., Loeffelhardt W.;
RT "Phylogenetic analysis of beta tubulins.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AF092952; AAD03712.1; -; mRNA.
DR AlphaFoldDB; Q9ZSW1; -.
DR SMR; Q9ZSW1; -.
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..447
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048337"
FT REGION 424..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..447
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 447 AA; 49824 MW; 042B0DD796ADD2A6 CRC64;
MREIVHVQGG QCGNQIGAKF WEVISDEHGV DPTGTYHGDS DLQLERINVY YNEATGGRYV
PRAVLMDLEP GTMDSVRAGP YGQLFRPDNF IFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAEGCDCL QGFQITHSMG GGTGSGMGTL LIAKVREEYP DRMMCTYSVF PSPKVSDTVV
EPYNATLSVH QLVENADEVM VIDNEALYDI CFRTLKLTTP TYGDLNHLVS ACISGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF VPLTSRGSQQ YRALTVPELT QQMFDAKNMM
CAADPRHGRY LTASALFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK ASVCDIPPKG
LKMSATFIGN STAIQEMFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEGDEEE AEGEAAA