TBB_SCHPO
ID TBB_SCHPO Reviewed; 448 AA.
AC P05219; O74206; Q9UQZ0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=nda3; Synonyms=alp12; ORFNames=SPBC26H8.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ILE-100.
RX PubMed=6094012; DOI=10.1016/0092-8674(84)90013-8;
RA Hiraoka Y., Toda T., Yanagida M.;
RT "The NDA3 gene of fission yeast encodes beta-tubulin: a cold-sensitive nda3
RT mutation reversibly blocks spindle formation and chromosome movement in
RT mitosis.";
RL Cell 39:349-358(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF TYR-422.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9658169; DOI=10.1091/mbc.9.7.1757;
RA Radcliffe P., Hirata D., Childs D., Vardy L., Toda T.;
RT "Identification of novel temperature-sensitive lethal alleles in essential
RT beta-tubulin and nonessential alpha 2-tubulin genes as fission yeast
RT polarity mutants.";
RL Mol. Biol. Cell 9:1757-1771(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP ANTIBIOTIC RESISTANCE TO RHIZOXIN.
RX PubMed=2274023; DOI=10.1007/bf00633814;
RA Takahashi M., Matsumoto S., Iwasaki S., Yahara I.;
RT "Molecular basis for determining the sensitivity of eucaryotes to the
RT antimitotic drug rhizoxin.";
RL Mol. Gen. Genet. 222:169-175(1990).
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 -!- MISCELLANEOUS: A cold-sensitive nda3 mutation reversibly blocks spindle
CC formation and chromosome movement in mitosis.
CC -!- MISCELLANEOUS: Rhizoxin, an antibiotic that exhibits potent anti-
CC mitotic activity against most eukaryotic cells except for yeasts, binds
CC to beta tubulin.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M10347; AAA35352.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21099.1; -; Genomic_DNA.
DR EMBL; AF042827; AAC21454.1; -; Genomic_DNA.
DR EMBL; AF042828; AAC21455.1; -; Genomic_DNA.
DR PIR; A21649; A21649.
DR PIR; T40019; T40019.
DR PIR; T43624; T43624.
DR RefSeq; NP_596650.1; NM_001022572.2.
DR PDB; 5MJS; EM; 4.60 A; A/B/C/J=1-429.
DR PDB; 5MLV; EM; 4.50 A; C/F/I/L/N/R=1-448.
DR PDB; 6S8M; EM; 4.50 A; B=1-448.
DR PDBsum; 5MJS; -.
DR PDBsum; 5MLV; -.
DR PDBsum; 6S8M; -.
DR AlphaFoldDB; P05219; -.
DR SMR; P05219; -.
DR BioGRID; 277108; 41.
DR DIP; DIP-46363N; -.
DR IntAct; P05219; 2.
DR STRING; 4896.SPBC26H8.07c.1; -.
DR iPTMnet; P05219; -.
DR MaxQB; P05219; -.
DR PaxDb; P05219; -.
DR PRIDE; P05219; -.
DR EnsemblFungi; SPBC26H8.07c.1; SPBC26H8.07c.1:pep; SPBC26H8.07c.
DR GeneID; 2540582; -.
DR KEGG; spo:SPBC26H8.07c; -.
DR PomBase; SPBC26H8.07c; nda3.
DR VEuPathDB; FungiDB:SPBC26H8.07c; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P05219; -.
DR OMA; VCSVAPK; -.
DR PhylomeDB; P05219; -.
DR Reactome; R-SPO-5617833; Cilium Assembly.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-9646399; Aggrephagy.
DR Reactome; R-SPO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:P05219; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000235; C:astral microtubule; NAS:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IMP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:PomBase.
DR GO; GO:0005876; C:spindle microtubule; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:PomBase.
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:1903087; P:mitotic spindle pole body duplication; IMP:PomBase.
DR GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; IDA:PomBase.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Antibiotic resistance; Cytoplasm; Cytoskeleton; GTP-binding;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..448
FT /note="Tubulin beta chain"
FT /id="PRO_0000048430"
FT REGION 429..448
FT /note="Disordered"
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 100
FT /note="I->N: Becomes sensitive to rhizoxin."
FT /evidence="ECO:0000269|PubMed:6094012"
FT MUTAGEN 422
FT /note="Y->H: Temperature sensitive."
FT /evidence="ECO:0000269|PubMed:9658169"
FT CONFLICT 6
FT /note="H -> L (in Ref. 1; AAA35352)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="D -> V (in Ref. 1; AAA35352)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="F -> I (in Ref. 1; AAA35352)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="K -> N (in Ref. 1; AAA35352)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="E -> D (in Ref. 1; AAA35352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 49472 MW; B0A08C9AF23A3846 CRC64;
MREIVHIQAG QCGNQVGAAF WSTIADEHGL DSAGIYHGTS EAQHERLNVY FNEAAGGKYV
PRAVLVDLEP GTMDAVKSGK FGNLFRPDNI IYGQSGAGNI WAKGHYTEGA ELADAVLDVV
RREAEACDAL QGFQLTHSLG GGTGSGMGTL LLSKIREEYP DRMMATFSVA PAPKSSDTVV
EPYNATLSMH QLVENSDETF CIDNEALSSI FANTLKIKSP SYDDLNHLVS AVMAGVTTSF
RFPGELNSDL RKLAVNMVPF PRLHFFMVGF APLAAIGSSS FQAVSVPELT QQMFDANNMM
VAADPRHGRY LTVAALFRGK VSMKEVDEQI RSVQTKNSAY FVEWIPDNVL KAVCSVPPKD
LKMSATFIGN STSIQEIFRR LGDQFSAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEAGI DEGDEDYEIE EEKEPLEY
