TBA2_SCHPO
ID TBA2_SCHPO Reviewed; 449 AA.
AC P04689; Q9HGL7;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Tubulin alpha-2 chain;
GN Name=tub1; Synonyms=alp2, atb2; ORFNames=SPBC800.05c;
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).
RN [3]
RP MUTAGENESIS OF GLY-246 AND CYS-356.
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).
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; K02842; AAA35351.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC01520.1; -; Genomic_DNA.
DR PIR; B25072; B25072.
DR RefSeq; NP_595106.1; NM_001021013.2.
DR AlphaFoldDB; P04689; -.
DR SMR; P04689; -.
DR BioGRID; 277452; 188.
DR IntAct; P04689; 12.
DR MINT; P04689; -.
DR STRING; 4896.SPBC800.05c.1; -.
DR MaxQB; P04689; -.
DR PaxDb; P04689; -.
DR PRIDE; P04689; -.
DR EnsemblFungi; SPBC800.05c.1; SPBC800.05c.1:pep; SPBC800.05c.
DR GeneID; 2540936; -.
DR KEGG; spo:SPBC800.05c; -.
DR PomBase; SPBC800.05c; -.
DR VEuPathDB; FungiDB:SPBC800.05c; -.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P04689; -.
DR OMA; KVGICYQ; -.
DR PhylomeDB; P04689; -.
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:P04689; -.
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:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005874; C:microtubule; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:PomBase.
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: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:0051659; P:maintenance of mitochondrion location; EXP:PomBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048311; P:mitochondrion distribution; IMP:PomBase.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:PomBase.
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; IPR013838; Beta-tubulin_BS.
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..449
FT /note="Tubulin alpha-2 chain"
FT /id="PRO_0000048226"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 449
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT MUTAGEN 246
FT /note="G->D: Temperature sensitive."
FT /evidence="ECO:0000269|PubMed:9658169"
FT MUTAGEN 356
FT /note="C->Y: Temperature sensitive."
FT /evidence="ECO:0000269|PubMed:9658169"
FT CONFLICT 81
FT /note="G -> D (in Ref. 1; AAA35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="A -> G (in Ref. 1; AAA35351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 50536 MW; D5FBA90418FC8493 CRC64;
MREIISIHVG QAGTQIGNAC WELYCLEHGI QPNGYMNPET ASQNSDGGFS TFFSETGQGK
YVPRSIYVDL EPNVIDQVRT GPYRDLFHPE QLITGKEDAS NNYARGHYTV GKELVDEVTD
KIRRIADNCS GLQGFLVFHS FGGGTGSGFG ALLLERLAME YTKKSKLQFS VYPAPQVSTS
VVEPYNSVLT THATLDLADC TFMVDNESCY DICRRNLDIE RPSYENLNRL IAQVVSSITA
SLRFEGSLNV DLAEFQTNLV PYPRIHFPLV TYAPIVSAAK AFHESNSVQE ITNQCFEPYN
QMVKCDPRAG RYMATCLLYR GDVIPRDVQA AVTTIKAKRT IQFVDWCPTG FKIGICDRPP
QHIEGSEIAK VDRAVCMLSN TTSIAEAWSR LDHKFDLMYS KRAFVHWYVG EGMEEGEFSE
AREDLAALER DYEEVGQDSM EVDYMEEEY
