MOD21_SCHPO
ID MOD21_SCHPO Reviewed; 677 AA.
AC Q9UT52;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Gamma-tubulin complex subunit mod21;
GN Name=mod21; ORFNames=SPAC806.08c;
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 [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 [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP IDENTIFICATION IN THE GAMMA-TUBULIN COMPLEX, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=17021256; DOI=10.1091/mbc.e05-11-1009;
RA Anders A., Lourenco P.C.C., Sawin K.E.;
RT "Noncore components of the fission yeast gamma-tubulin complex.";
RL Mol. Biol. Cell 17:5075-5093(2006).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Component of the gamma-tubulin complex that is required for
CC the regulation of both interphase microtubule organization and
CC nucleation, and mitotic bipolar spindles. Required for correct
CC septation. {ECO:0000269|PubMed:17021256}.
CC -!- SUBUNIT: Component of the gamma-tubulin complex composed of at least
CC alp4, alp6, alp16, ghf1, gtb1 and mod21. {ECO:0000269|PubMed:17021256}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:17021256}. Note=Localizes to the SPB and also to the
CC equatorial MTOC.
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DR EMBL; CU329670; CAB55287.2; -; Genomic_DNA.
DR PIR; T39100; T39100.
DR RefSeq; NP_592858.2; NM_001018259.2.
DR PDB; 6L80; X-ray; 2.00 A; A/C=1-109.
DR PDBsum; 6L80; -.
DR AlphaFoldDB; Q9UT52; -.
DR SMR; Q9UT52; -.
DR BioGRID; 279549; 26.
DR STRING; 4896.SPAC806.08c.1; -.
DR PaxDb; Q9UT52; -.
DR EnsemblFungi; SPAC806.08c.1; SPAC806.08c.1:pep; SPAC806.08c.
DR GeneID; 2543117; -.
DR KEGG; spo:SPAC806.08c; -.
DR PomBase; SPAC806.08c; mod21.
DR VEuPathDB; FungiDB:SPAC806.08c; -.
DR HOGENOM; CLU_406053_0_0_1; -.
DR OMA; DWMEITS; -.
DR PRO; PR:Q9UT52; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA: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:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0051415; P:microtubule nucleation by interphase microtubule organizing center; IMP:PomBase.
DR InterPro; IPR032797; Mod21.
DR Pfam; PF14609; GCP5-Mod21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome; Septation.
FT CHAIN 1..677
FT /note="Gamma-tubulin complex subunit mod21"
FT /id="PRO_0000352819"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:6L80"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:6L80"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:6L80"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:6L80"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:6L80"
SQ SEQUENCE 677 AA; 78427 MW; 5BDFF0AFCAF2E24D CRC64;
MTMSRADQIL QHLLRELIHN DSLVASEWLK HSKKIIQNVP SSTLVFHEMI EHIKGICDKM
GIQGREDLEM PLRNACEVLN RQTVSVKQSI LHAQILKLFL ELSKPPSDIH VPQIPVYKDC
NKNEQEAIIQ LLTSCEGDHW LMPDWSSMPD DETITEDSEE ETFNGNANEI TIPANIHIPI
IEESDNASNN KLCTLFKKSK QPNLDFLQIK PFMFWDSSLN ETVRISERSI IRDSIYMLIG
YPSFFFLKNG SKIETRLSLL PKLHHMSEEI LRSIMTELAD YGSNLEFFRQ KLTSPSDSFF
KSDDQSTKNE PFLSVVFIYP QIKPHLLSCL KNTHQELIKL ETEVYNATKN CTLFQFFQHV
KKFVDPLLCF RFAYEKSATN MWDFVKTLEF IYSTRNYSSQ MFKLYKASAI AMLLWMVNQA
SQITSSMTIA RPLYNILILC KDFPNNFLEK DNIALQLGSI VFDQSPTLNN LLVEMEILIR
SKILKLGKSL DLSFDFQSLM GEFENLIKQQ EEAKKSLWSK RFSRFYYGHY VFVNTCHNFF
LTLYQSFTEV DENSIFNGVF ETLNNDVDDE SVIGEKEKLI LKQKQKCLSE FFVDDIKKLL
NEELLNCQKQ ELPDVMENTY QISTVSGIKN DPLFTLDQTC NIIAKLADNL IHPSVPIGSS
AYRCRRNLAD LLFLIMP
