TBB1_VOLCA
ID TBB1_VOLCA Reviewed; 443 AA.
AC P11482;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUBB1;
GN and
GN Name=TUBB2;
OS Volvox carteri (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3067;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TUBB1).
RC STRAIN=f. Nagariensis;
RX PubMed=3185505; DOI=10.1007/bf00339597;
RA Harper J.F., Mages W.;
RT "Organization and structure of Volvox beta-tubulin genes.";
RL Mol. Gen. Genet. 213:315-324(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TUBB2).
RC STRAIN=f. Nagariensis / HK10;
RX PubMed=7628715; DOI=10.1016/0378-1119(95)00178-9;
RA Mages W., Cresnar B., Harper J.F., Bruederlein M., Schmitt R.;
RT "Volvox carteri alpha 2- and beta 2-tubulin-encoding genes: regulatory
RT signals and transcription.";
RL Gene 160:47-54(1995).
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; X12855; CAA31334.1; -; Genomic_DNA.
DR EMBL; L24547; AAA99439.1; -; Genomic_DNA.
DR PIR; JC4178; JC4178.
DR PIR; S04695; S04695.
DR RefSeq; XP_002953617.1; XM_002953571.1.
DR RefSeq; XP_002956358.1; XM_002956312.1.
DR AlphaFoldDB; P11482; -.
DR SMR; P11482; -.
DR PRIDE; P11482; -.
DR GeneID; 9616181; -.
DR GeneID; 9619310; -.
DR KEGG; vcn:VOLCADRAFT_75910; -.
DR KEGG; vcn:VOLCADRAFT_77081; -.
DR OMA; ECMILDN; -.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..443
FT /note="Tubulin beta chain"
FT /id="PRO_0000048384"
FT REGION 423..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; 49662 MW; 50F7934FCA8FDB8C 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 EEN
