ALP7_SCHPO
ID ALP7_SCHPO Reviewed; 474 AA.
AC Q9URY2; Q9UU56;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Microtubule protein alp7;
DE AltName: Full=Altered polarity protein 7;
DE AltName: Full=Transforming acidic coiled-coil protein mia1;
DE Short=TACC protein mia1;
GN Name=alp7; Synonyms=mia1; ORFNames=SPAC890.02c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 104-273, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, INTERACTION WITH ALP14, AND SUBCELLULAR LOCATION.
RX PubMed=14742702; DOI=10.1091/mbc.e03-11-0837;
RA Sato M., Vardy L., Angel Garcia M., Koonrugsa N., Toda T.;
RT "Interdependency of fission yeast Alp14/TOG and coiled coil protein Alp7 in
RT microtubule localization and bipolar spindle formation.";
RL Mol. Biol. Cell 15:1609-1622(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16481403; DOI=10.1091/mbc.e05-08-0811;
RA Zheng L., Schwartz C., Wee L., Oliferenko S.;
RT "The fission yeast transforming acidic coiled coil-related protein
RT Mia1p/Alp7p is required for formation and maintenance of persistent
RT microtubule-organizing centers at the nuclear envelope.";
RL Mol. Biol. Cell 17:2212-2222(2006).
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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).
CC -!- FUNCTION: Required for bipolar spindle formation and proper chromosome
CC segregation. Has an indirect role in connecting the kinetochores and
CC the plus end of pole to chromosome microtubules by targeting alp14 to
CC the spindle pole body. Involved in the emergence of large microtubule
CC organizing centers (MTOC) in interphase cells. Attaches to the minus
CC ends of microtubules and associates with the sites of microtubule
CC attachment on the nuclear envelope. This leads to the stabilzation of
CC the microtubule bundles. {ECO:0000269|PubMed:14742702,
CC ECO:0000269|PubMed:16481403}.
CC -!- SUBUNIT: Interacts with alp14. {ECO:0000269|PubMed:14742702}.
CC -!- INTERACTION:
CC Q9URY2; O94534: alp14; NbExp=13; IntAct=EBI-1556697, EBI-1556727;
CC Q9URY2; Q10173: nuf2; NbExp=3; IntAct=EBI-1556697, EBI-1002565;
CC Q9URY2; Q92351: pcp1; NbExp=3; IntAct=EBI-1556697, EBI-7633620;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
CC spindle. Chromosome, centromere, kinetochore. Note=Associated with the
CC equatorial MTOC, spindle midzones, spindle pole body and mitotic
CC kinetochore periphery. Spindle and kinetochore localization is alp14-
CC dependent.
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DR EMBL; CU329670; CAB63493.1; -; Genomic_DNA.
DR EMBL; AB027802; BAA87106.1; -; Genomic_DNA.
DR PIR; T50258; T50258.
DR RefSeq; NP_594820.1; NM_001020249.2.
DR AlphaFoldDB; Q9URY2; -.
DR SMR; Q9URY2; -.
DR BioGRID; 279804; 31.
DR DIP; DIP-39987N; -.
DR IntAct; Q9URY2; 7.
DR MINT; Q9URY2; -.
DR STRING; 4896.SPAC890.02c.1; -.
DR iPTMnet; Q9URY2; -.
DR MaxQB; Q9URY2; -.
DR PaxDb; Q9URY2; -.
DR PRIDE; Q9URY2; -.
DR EnsemblFungi; SPAC890.02c.1; SPAC890.02c.1:pep; SPAC890.02c.
DR GeneID; 2543382; -.
DR KEGG; spo:SPAC890.02c; -.
DR PomBase; SPAC890.02c; alp7.
DR VEuPathDB; FungiDB:SPAC890.02c; -.
DR eggNOG; ENOG502S2YR; Eukaryota.
DR HOGENOM; CLU_546472_0_0_1; -.
DR InParanoid; Q9URY2; -.
DR OMA; AQYSAKH; -.
DR PRO; PR:Q9URY2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0036449; C:microtubule minus-end; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000940; C:outer kinetochore; IDA:PomBase.
DR GO; GO:0099070; C:static microtubule bundle; IDA:PomBase.
DR GO; GO:0070850; C:TACC/TOG complex; IDA:PomBase.
DR GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR GO; GO:0030953; P:astral microtubule organization; IMP:PomBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
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:1990571; P:meiotic centromere clustering; IMP:PomBase.
DR GO; GO:0051415; P:microtubule nucleation by interphase microtubule organizing center; IMP:PomBase.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IMP:PomBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:PomBase.
DR GO; GO:0061805; P:mitotic spindle elongation (spindle phase three); IMP:PomBase.
DR GO; GO:0061804; P:mitotic spindle formation (spindle phase one); IMP:PomBase.
DR GO; GO:0140210; P:protein transport along microtubule to kinetochore; IMP:PomBase.
DR InterPro; IPR024312; TACC_fungi.
DR Pfam; PF12709; Fungal_TACC; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..474
FT /note="Microtubule protein alp7"
FT /id="PRO_0000064570"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 219..273
FT /evidence="ECO:0000255"
FT COILED 367..471
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 474 AA; 53175 MW; 22B4216C196E310C CRC64;
MSDIVSSSTD YSRRSPSSSS IGTNETDHTG FHEKRQGASS ESLIPPAQRS SEESMPAPKL
FPKLTSKPNP QLNLKDTLNK RVSDRLQALE LNKSFDFSGT PRPMHPISHP LSQHKTPEFK
HRKRNVESIL TPKNPSLFSS SNAASQRGSL NTAPSNFAYS HSSSLQTSAS SRPPVLSNGS
FPRQTNTAPL NPPVHLKDNI RNSATPSTSQ ADIPTQYPIN STQKQQAKYE AEIEGYKAKL
AGTYHEISVL QNTIVNVSGQ LIAVNDQLQQ LRSGKASTSP STKDTNMRLV EGHNEETLAL
QRGKYTQEEV DKLIQERMEK VAEDLHAQYS AKHTQKINAF KANYARKYEA TIQELQNQIG
TAPNAPKISN SNWEEERRAL KADNQTLQKQ LEKAIQERQD MSDFLNNFKA DMAKSDKLLM
QQQSQQTGDL ETLRLQLQAL QEELRVEREE RQQLIQMSED LVIAMDQLNL EQKS
