TBA3_YEAST
ID TBA3_YEAST Reviewed; 445 AA.
AC P09734; D6W0G1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Tubulin alpha-3 chain;
GN Name=TUB3; OrderedLocusNames=YML124C; ORFNames=YM7056.02C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3025610; DOI=10.1128/mcb.6.11.3711-3721.1986;
RA Schatz P.J., Pillus L., Grisafi P., Solomon F., Botstein D.;
RT "Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae
RT encode divergent proteins.";
RL Mol. Cell. Biol. 6:3711-3721(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-170.
RX PubMed=2038328; DOI=10.1128/mcb.11.6.3229-3238.1991;
RA Bun-Ya M., Nishimura M., Harashima S., Oshima Y.;
RT "The PHO84 gene of Saccharomyces cerevisiae encodes an inorganic phosphate
RT transporter.";
RL Mol. Cell. Biol. 11:3229-3238(1991).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP INTERACTION WITH NUM1.
RX PubMed=11266443; DOI=10.1083/jcb.152.2.251;
RA Farkasovsky M., Kuentzel H.;
RT "Cortical Num1p interacts with the dynein intermediate chain Pac11p and
RT cytoplasmic microtubules in budding yeast.";
RL J. Cell Biol. 152:251-262(2001).
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. Interacts with NUM1. {ECO:0000269|PubMed:11266443}.
CC -!- INTERACTION:
CC P09734; Q00402: NUM1; NbExp=2; IntAct=EBI-18981, EBI-12386;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- MISCELLANEOUS: Present with 12300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M28428; AAA35181.1; -; mRNA.
DR EMBL; Z49218; CAA89156.1; -; Genomic_DNA.
DR EMBL; D90346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006946; DAA09775.1; -; Genomic_DNA.
DR PIR; B25076; B25076.
DR RefSeq; NP_013582.1; NM_001182487.1.
DR AlphaFoldDB; P09734; -.
DR SMR; P09734; -.
DR BioGRID; 35081; 260.
DR ComplexPortal; CPX-1425; Tubulin alpha-beta heterodimeric complex, TUB3 variant.
DR DIP; DIP-2206N; -.
DR IntAct; P09734; 95.
DR MINT; P09734; -.
DR STRING; 4932.YML124C; -.
DR MaxQB; P09734; -.
DR PaxDb; P09734; -.
DR PRIDE; P09734; -.
DR EnsemblFungi; YML124C_mRNA; YML124C; YML124C.
DR GeneID; 854915; -.
DR KEGG; sce:YML124C; -.
DR SGD; S000004593; TUB3.
DR VEuPathDB; FungiDB:YML124C; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00940000164588; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P09734; -.
DR OMA; ILTCHTT; -.
DR BioCyc; YEAST:G3O-32703-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-5617833; Cilium Assembly.
DR Reactome; R-SCE-9646399; Aggrephagy.
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:P09734; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P09734; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IC:SGD.
DR GO; GO:0005828; C:kinetochore microtubule; IC:SGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005880; C:nuclear microtubule; IC:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; HDA:SGD.
DR GO; GO:0045298; C:tubulin complex; IGI:SGD.
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:0045143; P:homologous chromosome segregation; IC:SGD.
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:0000070; P:mitotic sister chromatid segregation; IC:SGD.
DR GO; GO:0000280; P:nuclear division; IBA:GO_Central.
DR GO; GO:0030473; P:nuclear migration along microtubule; IC:SGD.
DR GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; 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; IPR002452; Alpha_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; PR01162; ALPHATUBULIN.
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.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..445
FT /note="Tubulin alpha-3 chain"
FT /id="PRO_0000048240"
FT BINDING 143..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 49694 MW; 189889B795E72448 CRC64;
MREVISINVG QAGCQIGNAC WELYSLEHGI KEDGHLEDGL SKPKGGEEGF STFFHETGYG
KFVPRAIYVD LEPNVIDEVR TGRFKELFHP EQLINGKEDA ANNYARGHYT VGREIVDEVE
ERIRKMADQC DGLQGFLFTH SLGGGTGSGL GSLLLENLSY EYGKKSKLEF AVYPAPQLST
SVVEPYNTVL TTHTTLEHAD CTFMVDNEAI YDICKRNLGI SRPSFSNLNG LIAQVISSVT
ASLRFDGSLN VDLNEFQTNL VPYPRIHFPL VSYAPILSKK RATHESNSVS EITNACFEPG
NQMVKCDPTK GKYMANCLLY RGDVVTRDVQ RAVEQVKNKK TVQMVDWCPT GFKIGICYEP
PSVIPSSELA NVDRAVCMLS NTTAIADAWK RIDQKFDLMY AKRAFVHWYV GEGMEEGEFT
EAREDLAALE RDYIEVGADS YAEEF
