TBB_DICDI
ID TBB_DICDI Reviewed; 455 AA.
AC P32256; O15803; Q55DG9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=tubB; ORFNames=DDB_G0269196;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RX PubMed=8227212; DOI=10.1242/jcs.105.4.903;
RA Trivinos-Lagos L., Ohmachi T., Albrightson C., Burns R.G., Ennis H.L.,
RA Chisholm R.L.;
RT "The highly divergent alpha- and beta-tubulins from Dictyostelium
RT discoideum are encoded by single genes.";
RL J. Cell Sci. 105:903-911(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gonzales S.T., Welker D.L.;
RT "The beta tubulin gene of Dictyostelium discoideum.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
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; L14000; AAC37344.1; -; mRNA.
DR EMBL; AF030823; AAB86429.1; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71948.1; -; Genomic_DNA.
DR RefSeq; XP_646162.1; XM_641070.1.
DR AlphaFoldDB; P32256; -.
DR SMR; P32256; -.
DR IntAct; P32256; 1.
DR STRING; 44689.DDB0191169; -.
DR PaxDb; P32256; -.
DR EnsemblProtists; EAL71948; EAL71948; DDB_G0269196.
DR GeneID; 8617114; -.
DR KEGG; ddi:DDB_G0269196; -.
DR dictyBase; DDB_G0269196; tubB.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; P32256; -.
DR OMA; VCSVAPK; -.
DR PhylomeDB; P32256; -.
DR Reactome; R-DDI-5617833; Cilium Assembly.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-DDI-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:P32256; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:dictyBase.
DR GO; GO:0005874; C:microtubule; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:dictyBase.
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 GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
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 Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..455
FT /note="Tubulin beta chain"
FT /id="PRO_0000048289"
FT REGION 426..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="K -> N (in Ref. 1; AAC37344)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="V -> G (in Ref. 1; AAC37344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 51336 MW; DC00CBF62A8B587E CRC64;
MREIVQIQAG QCGNQIGSKF WEVISEEHGI QSDGFHAGGE DEHLKRLQLE RINVYYNEAR
DGKYVPRSVL VDLEPGTVDT IKASPYGKLF RPDNFIHGQS GAGNNWAKGH YTEGVELVES
VLDVVRRETE GCDCLQGFQV THSIGGGTGS GLGTLLISKI REEFPDRMMC TFSVVPSPKV
SLTVVEPYNA TLSVHQLVEN ADEVMCIDNE ALHDICFRTL KLTQPNYGDL NHLISSVMSG
ITCCLRFPGQ LNSDLRKLAV NLIPFPRLHF FLVGFAPLTA KGASSYNRIT VPELTQQMFD
AKNMMAASDP HNGKYLTASA LFRGKIFTKE VDEQMHNIQT KNSSYFVEWI PHNIKSSICD
IPPKGTPMAV TFIGNNTAIQ DLFKRISIHF QAMFRRKAFL HWYTLEGMEE LEFTEAESNM
NDLVYEYQQY SNQETEEDGG EYQEEHEEHE EQAEN
