ID TBB1_CAEEL Reviewed; 441 AA.
AC P12456;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 27-MAR-2024, entry version 173.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=mec-7; ORFNames=ZK154.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2744465; DOI=10.1101/gad.3.6.870;
RA Savage C., Hamelin M., Culotti J.G., Coulson A., Albertson D.G.,
RA Chalfie M.;
RT "mec-7 is a beta-tubulin gene required for the production of 15-
RT protofilament microtubules in Caenorhabditis elegans.";
RL Genes Dev. 3:870-881(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=1639062; DOI=10.1002/j.1460-2075.1992.tb05357.x;
RA Hamelin M., Scott I.M., Way J.C., Culotti J.G.;
RT "The mec-7 beta-tubulin gene of Caenorhabditis elegans is expressed
RT primarily in the touch receptor neurons.";
RL EMBO J. 11:2885-2893(1992).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19652181; DOI=10.1534/genetics.109.105726;
RA Bounoutas A., Zheng Q., Nonet M.L., Chalfie M.;
RT "mec-15 encodes an F-box protein required for touch receptor neuron
RT mechanosensation, synapse formation and development.";
RL Genetics 183:607-617(2009).
CC -!- FUNCTION: TTubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC GTPase activity of alpha-tubulin. Plays a role in mechanosensory
CC transduction (touch sensitivity) (PubMed:19652181).
CC {ECO:0000269|PubMed:19652181, ECO:0000305}.
CC -!- FUNCTION: Mec-7 beta-tubulin is required for the production of 15-
CC protofilament microtubules.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P68363};
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 -!- TISSUE SPECIFICITY: Expressed primarily in touch receptor neurons.
CC {ECO:0000269|PubMed:1639062}.
CC -!- DISRUPTION PHENOTYPE: Defective touch receptor neuron synaptic
CC transmission with reduced levels of rab-3 at synapses, conferring touch
CC insensitivity. Irregular touch receptor neuron shape. The heterozygous
CC mutant, but not the null mutant, rescues the touch sensitivity defect
CC in the mec-15 single mutant. {ECO:0000269|PubMed:19652181}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X15242; CAA33320.1; -; Genomic_DNA.
DR EMBL; FO080892; CCD67558.1; -; Genomic_DNA.
DR PIR; S05956; S05956.
DR RefSeq; NP_509313.1; NM_076912.3.
DR AlphaFoldDB; P12456; -.
DR SMR; P12456; -.
DR BioGRID; 45960; 9.
DR STRING; 6239.ZK154.3.1; -.
DR EPD; P12456; -.
DR PaxDb; 6239-ZK154-3; -.
DR PeptideAtlas; P12456; -.
DR EnsemblMetazoa; ZK154.3.1; ZK154.3.1; WBGene00003171.
DR GeneID; 181036; -.
DR KEGG; cel:CELE_ZK154.3; -.
DR UCSC; ZK154.3; c. elegans.
DR AGR; WB:WBGene00003171; -.
DR WormBase; ZK154.3; CE15257; WBGene00003171; mec-7.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000170651; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P12456; -.
DR OMA; HSAYFVE; -.
DR OrthoDB; 3124041at2759; -.
DR PhylomeDB; P12456; -.
DR Reactome; R-CEL-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:P12456; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003171; Expressed in larva and 26 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:WormBase.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:WormBase.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IGI:UniProtKB.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:WormBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1905789; P:positive regulation of detection of mechanical stimulus involved in sensory perception of touch; IGI:UniProtKB.
DR GO; GO:1905792; P:positive regulation of mechanosensory behavior; IGI:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:WormBase.
DR CDD; cd02187; beta_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR PANTHER; PTHR11588:SF484; TUBULIN BETA-2 CHAIN-RELATED; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Magnesium; Metal-binding;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..441
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048286"
FT BINDING 11
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
FT BINDING 69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
FT BINDING 143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
FT BINDING 144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
FT BINDING 204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
FT BINDING 226
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
SQ SEQUENCE 441 AA; 49260 MW; F01403CFD069F4D4 CRC64;
MREIVHIQAG QCGNQIGSKF WEVISDEHGI DPSGQYVGDS DLQLERINVY YNEAGSNKYV
PRAVLVDLEP GTMDSVRSGP FGQLFRPDNY VFGQSGAGNN WAKGHYTEGA ELVDNVLDVV
RKEAESTDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDSTF CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRSNQQ YRAITVPELT QQCFDAKNMM
AACDPRHGRY LTAAAIFRGR MSMKEVDEQM LNIQNKNSSY FVDWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEAAA DEDAAEAFDG E
//
