TBB4_CAEEL
ID TBB4_CAEEL Reviewed; 444 AA.
AC P41937;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tubulin beta-4 chain;
DE AltName: Full=Beta-4-tubulin;
GN Name=tbb-4; ORFNames=B0272.1;
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).
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; Z46240; CAA86310.1; -; Genomic_DNA.
DR PIR; T18683; T18683.
DR RefSeq; NP_509585.1; NM_077184.4.
DR AlphaFoldDB; P41937; -.
DR SMR; P41937; -.
DR BioGRID; 46086; 9.
DR IntAct; P41937; 2.
DR STRING; 6239.B0272.1; -.
DR EPD; P41937; -.
DR PaxDb; P41937; -.
DR PeptideAtlas; P41937; -.
DR PRIDE; P41937; -.
DR EnsemblMetazoa; B0272.1.1; B0272.1.1; WBGene00006538.
DR GeneID; 181170; -.
DR KEGG; cel:CELE_B0272.1; -.
DR UCSC; B0272.1; c. elegans.
DR CTD; 181170; -.
DR WormBase; B0272.1; CE00850; WBGene00006538; tbb-4.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154394; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P41937; -.
DR OMA; MASHAHV; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P41937; -.
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:P41937; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006538; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005879; C:axonemal microtubule; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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: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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..444
FT /note="Tubulin beta-4 chain"
FT /id="PRO_0000048288"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
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 444 AA; 49800 MW; BAAB14ABE312B209 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGAYNGDS DLQLERINVY YNEASGGKYV
PRACLVDLEP GTMDSVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDNVLDVV
RKEAESCDCL QGFQMTHSLG GGTGSGMGTL LISKIREEYP DRIMMTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETF CIDNEALYDI CFRTLKLTTP TYGDLNHLVS MTMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRSLTVPELT QQMFDAKNMM
AACDPRHGRY LTVAAMFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
VKMAATFVGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEATA DDEGEFDEHD QDVE
