ID   ALP6_SCHPO              Reviewed;         832 AA.
AC   Q9USQ2; O94366; Q9P954;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   25-MAY-2022, entry version 149.
DE   RecName: Full=Spindle pole body component alp6;
DE   AltName: Full=Altered polarity protein 6;
GN   Name=alp6; ORFNames=SPBC428.20c, SPBC902.01c;
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], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11080156; DOI=10.1093/emboj/19.22.6098;
RA   Vardy L., Toda T.;
RT   "The fission yeast gamma-tubulin complex is required in G(1) phase and is a
RT   component of the spindle assembly checkpoint.";
RL   EMBO J. 19:6098-6111(2000).
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   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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
RN   [5]
RP   INTERACTION WITH MZT1.
RX   PubMed=24006493; DOI=10.1091/mbc.e13-05-0253;
RA   Dhani D.K., Goult B.T., George G.M., Rogerson D.T., Bitton D.A.,
RA   Miller C.J., Schwabe J.W., Tanaka K.;
RT   "Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of
RT   the gamma-tubulin complex and directly interacts with GCP3(Alp6).";
RL   Mol. Biol. Cell 24:3337-3349(2013).
CC   -!- FUNCTION: Component of the gamma tubule complex that is required for
CC       the regulation of both interphase microtubules and mitotic bipolar
CC       spindles. {ECO:0000269|PubMed:11080156}.
CC   -!- SUBUNIT: Part of the gamma-tubulin complex. Interacts directly with
CC       mzt1. {ECO:0000269|PubMed:11080156, ECO:0000269|PubMed:24006493}.
CC   -!- INTERACTION:
CC       Q9USQ2; Q9Y705: alp4; NbExp=3; IntAct=EBI-9549762, EBI-1562228;
CC       Q9USQ2; P0CF96: mzt1; NbExp=6; IntAct=EBI-9549762, EBI-9549556;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:11080156}. Note=Localizes
CC       to the SPB and also to the equatorial MTOC.
CC   -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA94097.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB040811; BAA94097.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CU329671; CAA22295.3; -; Genomic_DNA.
DR   PIR; T50382; T50382.
DR   RefSeq; XP_001713121.2; XM_001713069.2.
DR   AlphaFoldDB; Q9USQ2; -.
DR   SMR; Q9USQ2; -.
DR   BioGRID; 277215; 15.
DR   IntAct; Q9USQ2; 3.
DR   STRING; 4896.SPBC428.20c.1; -.
DR   iPTMnet; Q9USQ2; -.
DR   MaxQB; Q9USQ2; -.
DR   PaxDb; Q9USQ2; -.
DR   EnsemblFungi; SPBC428.20c.1; SPBC428.20c.1:pep; SPBC428.20c.
DR   PomBase; SPBC428.20c; alp6.
DR   VEuPathDB; FungiDB:SPBC428.20c; -.
DR   eggNOG; KOG2000; Eukaryota.
DR   HOGENOM; CLU_003736_0_0_1; -.
DR   InParanoid; Q9USQ2; -.
DR   OMA; MRMMSVC; -.
DR   PhylomeDB; Q9USQ2; -.
DR   PRO; PR:Q9USQ2; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
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: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: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:0071957; C:old mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR   GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007020; P:microtubule nucleation; IC:PomBase.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:PomBase.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   Gene3D; 1.20.120.1900; -; 1.
DR   InterPro; IPR007259; GCP.
DR   InterPro; IPR040457; GCP_C.
DR   InterPro; IPR042241; GCP_C_sf.
DR   InterPro; IPR041470; GCP_N.
DR   PANTHER; PTHR19302; PTHR19302; 1.
DR   Pfam; PF04130; GCP_C_terminal; 1.
DR   Pfam; PF17681; GCP_N_terminal; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..832
FT                   /note="Spindle pole body component alp6"
FT                   /id="PRO_0000078133"
FT   REGION          1..186
FT                   /note="Interaction with mzt1"
FT   MOD_RES         286
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   832 AA;  95997 MW;  C92771C3DBF5C01A CRC64;
     MSEIHVKTAL SRLADKYLQN SKNPSVPYTI ETIVSFFQEI IHSISPDTFQ LDIDDILYKI
     YSKIPPEENN DALFSKLSNL VSRLKSQTVI HNKSQILYFL YLLSPISQSS RDVSSHLLDE
     SISNPINIPS TEVESSNFGQ TRYDQVPENP QITDWDEGLE NESSISIAHD SSRLNRSTET
     SSVQHTLITE ADLLSSISYV LQGISTEYVQ FKNELALLSK RIPVQYLLQM RALSETGLLY
     QELKVFSNYD PSVSQSIDGD NVSKAFINDQ SLALQSLKSV ISKELTNFLA LIASLDSQIR
     ADASLEKPMV TIRRCIAWTQ VAKLKLRILS SVVNDNMNQE NKKRLIQVVS KYNVHGDPLI
     QELSDKILTE ITGPLYEMIE NWIYKGELVD PYQEFFVKEK NGSESHDHQG QGDVVWKGKY
     FLDKELIPSF LSEELVDKIF LIGKSLNFAR YGCGDFDWAQ EHYQKLVKKL SYRDPHSLET
     VVDKAYTESI NHLVYLMEEV FHLTDHLKAI KKYLLLGQGD FVDLLMESLG NSLDQPANTL
     FRHNLTASLE SAIRSSNASY EPEYVLKRLD ARLLELSHGE TGWDVFTLEY KVDSPINVII
     TPYCSRQYLK IFNFLWRLKR IEFALAHSWR RVNLGERNVF RNLDYTKFEW HFVSCHLAEM
     IHFVCQLQYY ILFEVIEISW QELQLAMEKP NATLDTYIEA HEKYVTSITH KGLLGGGKSR
     NEDSFLHQLH DILKVILNFH DAIELLYNFS CSLSNRIRIN VPISTDALAA QYTPIKNELS
     NFTEEFQVRL QKLLHGLASH KDPEMRFLSV RLNYNEFYVS HRRRHDKDVT SQ