TBG_SCHPO
ID TBG_SCHPO Reviewed; 446 AA.
AC P25295;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Tubulin gamma chain;
DE AltName: Full=Gamma-tubulin;
GN Name=tug1; Synonyms=gtb1; ORFNames=SPBC32F12.04;
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=1840506; DOI=10.1016/0092-8674(91)90390-k;
RA Stearns T., Evans L., Kirschner M.;
RT "Gamma-tubulin is a highly conserved component of the centrosome.";
RL Cell 65:825-836(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=1770000; DOI=10.1242/jcs.99.4.693;
RA Horio T., Uzawa S., Jung M.K., Oakley B.R., Tanaka K., Yanagida M.;
RT "The fission yeast gamma-tubulin is essential for mitosis and is localized
RT at microtubule organizing centers.";
RL J. Cell Sci. 99:693-700(1991).
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).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC chain is found at microtubule organizing centers (MTOC) such as the
CC spindle poles or the centrosome, suggesting that it is involved in the
CC minus-end nucleation of microtubule assembly.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M63447; AAA35305.1; -; Genomic_DNA.
DR EMBL; X62031; CAA43976.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19365.1; -; Genomic_DNA.
DR PIR; B39528; UBZPG.
DR RefSeq; NP_596147.1; NM_001022066.2.
DR AlphaFoldDB; P25295; -.
DR SMR; P25295; -.
DR BioGRID; 276756; 37.
DR IntAct; P25295; 4.
DR MINT; P25295; -.
DR STRING; 4896.SPBC32F12.04.1; -.
DR MaxQB; P25295; -.
DR PaxDb; P25295; -.
DR EnsemblFungi; SPBC32F12.04.1; SPBC32F12.04.1:pep; SPBC32F12.04.
DR GeneID; 2540223; -.
DR KEGG; spo:SPBC32F12.04; -.
DR PomBase; SPBC32F12.04; -.
DR VEuPathDB; FungiDB:SPBC32F12.04; -.
DR eggNOG; KOG1374; Eukaryota.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; P25295; -.
DR OMA; EHGINKE; -.
DR PhylomeDB; P25295; -.
DR PRO; PR:P25295; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IDA:PomBase.
DR GO; GO:0000930; C:gamma-tubulin complex; IDA:PomBase.
DR GO; GO:0061496; C:half bridge of mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0061497; C:inner plaque of mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0031021; C:interphase microtubule organizing center; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0071957; C:old mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0061499; C:outer plaque of mitotic spindle pole body; IDA:PomBase.
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:0031122; P:cytoplasmic microtubule organization; IC:PomBase.
DR GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IMP:PomBase.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1902408; P:mitotic cytokinesis, site selection; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IGI:PomBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:PomBase.
DR CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002454; Gamma_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; PR01164; GAMMATUBULIN.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..446
FT /note="Tubulin gamma chain"
FT /id="PRO_0000048480"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 49966 MW; 8A48833EAB3BD469 CRC64;
MGREIITLQA GQCGNQIGSQ FWQQLCLEHG IGPDGTLESF ATEGVDRKDV FFYQSDDTRY
IPRAILIDLE PRVVNNILSD TYGSLYNPEN ILITKNGGGA GNNWANGYSH AERIFEDIMD
MIDREADGSD SLEGFSLLHS IAGGTGSGLG SFLLERLNDR YPKKIIQTYS VFPNSQSVSD
VVVQPYNSLL ALKRLTLNAD SVVVLDNAAL AHIAADRLHT QNPTFHQQNQ LVSTVMSAST
TTLRYPGYMN NDLVSIIASL IPSPRCHFLL TSYTPFTNQQ VEEAKAIRKT TVLDVMRRLL
LPKNQMVSVN PSKKSCFISI LDIIQGEADP ADVHKSLLRI RERRYASFIP WGPASIQVAL
SKKSPYIKTN HRVSGLMLAN HTSIASLFKR TLDQYDRLRK RNAFLEQYKK EAIFEDDLNE
FDSSRDVVAD LINEYEACED PNYLSL
