TBB2_CAEEL
ID TBB2_CAEEL Reviewed; 450 AA.
AC P52275;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Tubulin beta-2 chain;
DE AltName: Full=Beta-2-tubulin;
GN Name=tbb-2; ORFNames=C36E8.5;
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 [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 [2]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-404; ASP-417 AND ASP-435.
RX PubMed=17371877; DOI=10.1074/jbc.m611051200;
RA Taylor R.C., Brumatti G., Ito S., Hengartner M.O., Derry W.B., Martin S.J.;
RT "Establishing a blueprint for CED-3-dependent killing through
RT identification of multiple substrates for this protease.";
RL J. Biol. Chem. 282:15011-15021(2007).
RN [3]
RP MUTAGENESIS OF GLU-439.
RX PubMed=22621901; DOI=10.1091/mbc.e12-01-0055;
RA Wilson K.J., Qadota H., Mains P.E., Benian G.M.;
RT "UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the
RT function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans.";
RL Mol. Biol. Cell 23:2623-2634(2012).
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 -!- PTM: Cleaved by caspase ced-3 in vitro. {ECO:0000269|PubMed:17371877}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z35597; CAA84648.1; -; Genomic_DNA.
DR PIR; T19788; T19788.
DR RefSeq; NP_497806.1; NM_065405.5.
DR PDB; 6E88; EM; 4.80 A; B/D/J/K/N/O=1-426.
DR PDBsum; 6E88; -.
DR AlphaFoldDB; P52275; -.
DR SMR; P52275; -.
DR BioGRID; 40756; 21.
DR DIP; DIP-27189N; -.
DR STRING; 6239.C36E8.5.1; -.
DR EPD; P52275; -.
DR PaxDb; P52275; -.
DR PeptideAtlas; P52275; -.
DR PRIDE; P52275; -.
DR EnsemblMetazoa; C36E8.5.1; C36E8.5.1; WBGene00006537.
DR GeneID; 175519; -.
DR KEGG; cel:CELE_C36E8.5; -.
DR UCSC; C36E8.5.1; c. elegans.
DR CTD; 175519; -.
DR WormBase; C36E8.5; CE00913; WBGene00006537; tbb-2.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00970000196484; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P52275; -.
DR OMA; CVDARED; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P52275; -.
DR Reactome; R-CEL-5617833; Cilium Assembly.
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-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR Reactome; R-CEL-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:P52275; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006537; Expressed in embryo and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:WormBase.
DR GO; GO:0045298; C:tubulin complex; ISS:WormBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000212; P:meiotic spindle organization; IGI:WormBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..450
FT /note="Tubulin beta-2 chain"
FT /id="PRO_0000048287"
FT REGION 428..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..450
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"
FT MUTAGEN 404
FT /note="D->E: Partial reduction in ced-3-mediated cleavage;
FT when associated with E-417 and E-435."
FT /evidence="ECO:0000269|PubMed:17371877"
FT MUTAGEN 417
FT /note="D->E: Partial reduction in ced-3-mediated cleavage;
FT when associated with E-404 and E-435."
FT /evidence="ECO:0000269|PubMed:17371877"
FT MUTAGEN 435
FT /note="D->E: Partial reduction in ced-3-mediated cleavage;
FT when associated with E-404 and E-417."
FT /evidence="ECO:0000269|PubMed:17371877"
FT MUTAGEN 439
FT /note="E->K: In sb26; no effect on thick filament
FT organization in body wall muscles. Partially restores thick
FT filament organization in a mel-26 (ct61sb4) mutant
FT background."
FT /evidence="ECO:0000269|PubMed:22621901"
SQ SEQUENCE 450 AA; 50345 MW; 8F04D0D2AB165006 CRC64;
MREIVHVQAG QCGNQIGSKF WEVISDEHGI QPDGTFKGET DLQLERIDVY YNEANNGKYV
PRAVLVDLEP GTMDSVRSGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDNVLDVI
RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMSSFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CYRTLKLTNP TYGDLNHLVS LTMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLSAKGTQA YRALTVAELT QQMFDAKNMM
AACDPRHGRY LTVAAMFRGR MSMREVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMAATFVGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLIS
EYQQYQEATA EDDVDGYAEG EAGETYESEQ
