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ALP4_SCHPO
ID   ALP4_SCHPO              Reviewed;         784 AA.
AC   Q9Y705;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Spindle pole body component alp4;
DE   AltName: Full=Altered polarity protein 4;
GN   Name=alp4; ORFNames=SPBC365.15;
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.
RC   STRAIN=972 / ATCC 24843;
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   FUNCTION.
RX   PubMed=11952833; DOI=10.1046/j.1365-2443.2002.00530.x;
RA   Vardy L., Fujita A., Toda T.;
RT   "The gamma-tubulin complex protein Alp4 provides a link between the
RT   metaphase checkpoint and cytokinesis in fission yeast.";
RL   Genes Cells 7:365-373(2002).
RN   [4]
RP   INTERACTION WITH MCP6, AND SUBCELLULAR LOCATION.
RX   PubMed=16111942; DOI=10.1016/j.cub.2005.07.058;
RA   Tanaka K., Kohda T., Yamashita A., Nonaka N., Yamamoto M.;
RT   "Hrs1p/Mcp6p on the meiotic SPB organizes astral microtubule arrays for
RT   oscillatory nuclear movement.";
RL   Curr. Biol. 15:1479-1486(2005).
RN   [5]
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 tubule complex that is required for
CC       the regulation of both interphase microtubules and mitotic bipolar
CC       spindles. Required for correct septation. {ECO:0000269|PubMed:11080156,
CC       ECO:0000269|PubMed:11952833}.
CC   -!- SUBUNIT: Part of the gamma-tubulin complex. Interacts with mcp6.
CC       {ECO:0000269|PubMed:11080156, ECO:0000269|PubMed:16111942}.
CC   -!- INTERACTION:
CC       Q9Y705; Q9USQ2: alp6; NbExp=3; IntAct=EBI-1562228, EBI-9549762;
CC       Q9Y705; Q10336: mcp6; NbExp=2; IntAct=EBI-1562228, EBI-1562149;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:11080156,
CC       ECO:0000269|PubMed:16111942, ECO:0000269|PubMed:16823372}.
CC       Note=Localizes to the SPB and also to the equatorial MTOC.
CC   -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB44767.1; -; Genomic_DNA.
DR   EMBL; AB026664; BAA77269.1; -; Genomic_DNA.
DR   PIR; T43510; T43510.
DR   RefSeq; NP_596044.1; NM_001021954.2.
DR   AlphaFoldDB; Q9Y705; -.
DR   SMR; Q9Y705; -.
DR   BioGRID; 276920; 21.
DR   IntAct; Q9Y705; 5.
DR   MINT; Q9Y705; -.
DR   STRING; 4896.SPBC365.15.1; -.
DR   iPTMnet; Q9Y705; -.
DR   MaxQB; Q9Y705; -.
DR   PaxDb; Q9Y705; -.
DR   PRIDE; Q9Y705; -.
DR   EnsemblFungi; SPBC365.15.1; SPBC365.15.1:pep; SPBC365.15.
DR   GeneID; 2540392; -.
DR   KEGG; spo:SPBC365.15; -.
DR   PomBase; SPBC365.15; alp4.
DR   VEuPathDB; FungiDB:SPBC365.15; -.
DR   eggNOG; KOG2001; Eukaryota.
DR   HOGENOM; CLU_007738_0_1_1; -.
DR   InParanoid; Q9Y705; -.
DR   OMA; SKLMTCC; -.
DR   PhylomeDB; Q9Y705; -.
DR   PRO; PR:Q9Y705; -.
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:0031021; C:interphase microtubule organizing center; IDA:PomBase.
DR   GO; GO:0035974; C:meiotic 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:1990734; P:astral microtubule anchoring at mitotic spindle pole body; IMP:PomBase.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:PomBase.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
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:0098863; P:nuclear migration by microtubule mediated pushing forces; 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   Reference proteome; Septation.
FT   CHAIN           1..784
FT                   /note="Spindle pole body component alp4"
FT                   /id="PRO_0000078132"
SQ   SEQUENCE   784 AA;  90158 MW;  E529CE217FFDA2B2 CRC64;
     MVRSISSVLA KEESENGSPI PALEEGSVYH VSLKSEGVSP FSDRIQLNYL YDGKTFSDPS
     NLNIHQQEAC LINELLNAFM GMEGVFVHLQ DMKASSEFET IIMPPSFYIL PGFDLGIKDI
     ASEMLEMGSH YLSITAFIES RSHFEYGFVN HALCAALRKF VMDYVVLIMQ CENQSRIDPN
     FSLQTLRLYT LPTSRSLRQV YLILRDLLLS MEKNASSSDD LGLSNIDDLL EQLNEGNDIS
     HVVNATRSKK KVCKGGQVIS FLTESLTKYA GDPVARKILT YLLREASRPY TKMLNEWIHL
     GLVNDPYDEF MIKIHKGITS MQLDEDYTDE YWEKRYVIRE DQVPPQLLDL QNKVLFAGKY
     LNVVLECRKG VNNLASLNAK DDTQNQLLWP STFDDDNFTL NIMNAYVYAN ESLLQLLQSS
     QSLYAHLYSL KHYFFLDQSD FFTTFLDNAQ HELRKPAKYI SITKLQSQLD LALRQPGTIT
     ATDPHKEYVT VEVNQTSLID WLMHIVSISG LEEGTSSQGN EVWNESITKQ ADVGNETRNF
     ESEHNRSTQG TSKVGSDKDI NGFETMQLCY KVPFPLSLIL SRKAIIRYQL LFRYFLLLRH
     VEMQLENSWV QHSKNSAWRL NSSNAKIEQW KRNSWLLRTR MLSFVQKIIY YTTSEVIETH
     WGKFMGELEN ARTVDNLMQE HIDFLDTCLK ECMLTNSRLL KVQSKLLNTC AMFASYTSTF
     TRSLYLLENS EESFDEGRMD KMEEILRRYE DSFSRHLKSL VNACNYFAST ETAALLSLVM
     KLTG
 
 
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