ID   TBA1_SCHPO              Reviewed;         455 AA.
AC   P04688; O42920;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Tubulin alpha-1 chain;
GN   Name=nda2; ORFNames=SPBC16A3.15c;
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].
RX   PubMed=6327053; DOI=10.1016/0092-8674(84)90319-2;
RA   Toda T., Adachi Y., Hiraoka Y., Yanagida M.;
RT   "Identification of the pleiotropic cell division cycle gene NDA2 as one of
RT   two different alpha-tubulin genes in Schizosaccharomyces pombe.";
RL   Cell 37:233-242(1984).
RN   [2]
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).
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; K02841; AAA35350.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA16866.1; -; Genomic_DNA.
DR   PIR; A25072; A25072.
DR   PIR; T39537; T39537.
DR   RefSeq; NP_596774.1; NM_001023795.2.
DR   PDB; 5MJS; EM; 4.60 A; E/F/G/H=1-444.
DR   PDB; 5MLV; EM; 4.50 A; B/E/H/K/M/Q=1-455.
DR   PDB; 6S8M; EM; 4.50 A; A=1-455.
DR   PDBsum; 5MJS; -.
DR   PDBsum; 5MLV; -.
DR   PDBsum; 6S8M; -.
DR   AlphaFoldDB; P04688; -.
DR   SMR; P04688; -.
DR   BioGRID; 276411; 22.
DR   DIP; DIP-37976N; -.
DR   IntAct; P04688; 5.
DR   STRING; 4896.SPBC16A3.15c.1; -.
DR   iPTMnet; P04688; -.
DR   MaxQB; P04688; -.
DR   PaxDb; P04688; -.
DR   PRIDE; P04688; -.
DR   EnsemblFungi; SPBC16A3.15c.1; SPBC16A3.15c.1:pep; SPBC16A3.15c.
DR   GeneID; 2539864; -.
DR   KEGG; spo:SPBC16A3.15c; -.
DR   PomBase; SPBC16A3.15c; nda2.
DR   VEuPathDB; FungiDB:SPBC16A3.15c; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   HOGENOM; CLU_015718_1_1_1; -.
DR   InParanoid; P04688; -.
DR   OMA; VDNEACY; -.
DR   PhylomeDB; P04688; -.
DR   Reactome; R-SPO-114608; Platelet degranulation.
DR   Reactome; R-SPO-5617833; Cilium Assembly.
DR   Reactome; R-SPO-9646399; Aggrephagy.
DR   Reactome; R-SPO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   PRO; PR:P04688; -.
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:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; 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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0000280; P:nuclear division; IBA:GO_Central.
DR   GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; IDA:PomBase.
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   3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..455
FT                   /note="Tubulin alpha-1 chain"
FT                   /id="PRO_0000048225"
FT   BINDING         146..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            455
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        155
FT                   /note="A -> T (in Ref. 1; AAA35350)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   455 AA;  51152 MW;  924EAAB0C53CED41 CRC64;
     MREVISVHVG QAGVQIGNAC WELYCLEHGI GPDGFPTENS EVHKNNSYLN DGFGTFFSET
     GQGKFVPRSI YVDLEPNVID QVRTGPYKDL FHPEQMVTGK EDASNNYARG HYTVGKEMID
     SVLERIRRMA DNCSGLQGFL VFHSFGGGTG SGLGALLLER LNMEYGKKSN LQFSVYPAPQ
     VSTSVVEPYN SVLTTHATLD NSDCTFMVDN EACYDICRRN LDIERPTYEN LNRLIAQVVS
     SITASLRFAG SLNVDLNEFQ TNLVPYPRIH FPLVTYSPIV SAAKAFHESN SVQEITNQCF
     EPYNQMVKCD PRTGRYMATC LLYRGDVIPR DVQAAVTSIK SRRTIQFVDW CPTGFKIGIC
     YEPPQHVPGS GIAKVNRAVC MLSNTTSIAE AWSRLDHKFD LMYSKRAFVH WYVGEGMEEG
     EFSEAREDLA ALERDYEEVG QDSMDNEMYE ADEEY