ALP14_SCHPO
ID ALP14_SCHPO Reviewed; 809 AA.
AC O94534;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Spindle pole body component alp14;
DE AltName: Full=Altered polarity protein 14;
GN Name=alp14; Synonyms=mtc1; ORFNames=SPCC895.07;
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, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11432827; DOI=10.1093/emboj/20.13.3389;
RA Garcia M.A., Vardy L., Koonrugsa N., Toda T.;
RT "Fission yeast ch-TOG/XMAP215 homologue Alp14 connects mitotic spindles
RT with the kinetochore and is a component of the Mad2-dependent spindle
RT checkpoint.";
RL EMBO J. 20:3389-3401(2001).
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, INTERACTION WITH ALP7, 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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543; SER-548; SER-697 AND
RP SER-720, AND IDENTIFICATION BY 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 a role in connecting the kinetochores and the plus end
CC of pole to chromosome microtubules. Also required for the activation of
CC the spindle checkpoint pathway. {ECO:0000269|PubMed:11432827,
CC ECO:0000269|PubMed:14742702}.
CC -!- SUBUNIT: Interacts with alp14. {ECO:0000269|PubMed:14742702}.
CC -!- INTERACTION:
CC O94534; Q9URY2: alp7; NbExp=13; IntAct=EBI-1556727, EBI-1556697;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Chromosome, centromere, kinetochore.
CC Note=Kinetochore periphery. Spindle localization is alp7-dependent.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000305}.
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DR EMBL; AB032409; BAA84527.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA22843.1; -; Genomic_DNA.
DR PIR; T41645; T41645.
DR RefSeq; NP_588048.1; NM_001023040.2.
DR AlphaFoldDB; O94534; -.
DR SMR; O94534; -.
DR BioGRID; 276060; 143.
DR DIP; DIP-39988N; -.
DR IntAct; O94534; 1.
DR MINT; O94534; -.
DR STRING; 4896.SPCC895.07.1; -.
DR iPTMnet; O94534; -.
DR MaxQB; O94534; -.
DR PaxDb; O94534; -.
DR PRIDE; O94534; -.
DR EnsemblFungi; SPCC895.07.1; SPCC895.07.1:pep; SPCC895.07.
DR GeneID; 2539497; -.
DR KEGG; spo:SPCC895.07; -.
DR PomBase; SPCC895.07; alp14.
DR VEuPathDB; FungiDB:SPCC895.07; -.
DR eggNOG; KOG1820; Eukaryota.
DR HOGENOM; CLU_008401_1_0_1; -.
DR InParanoid; O94534; -.
DR OMA; HMGSRFE; -.
DR PhylomeDB; O94534; -.
DR PRO; PR:O94534; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR GO; GO:1904511; C:cytoplasmic microtubule plus-end; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0072687; C:meiotic spindle; EXP:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA: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:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0061863; F:microtubule plus end polymerase; IDA:PomBase.
DR GO; GO:0051010; F:microtubule plus-end binding; TAS:PomBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; EXP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; EXP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IBA:GO_Central.
DR GO; GO:1990571; P:meiotic centromere clustering; IMP:PomBase.
DR GO; GO:0051417; P:microtubule nucleation by spindle pole body; IMP:PomBase.
DR GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:PomBase.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:PomBase.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0140210; P:protein transport along microtubule to kinetochore; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR PANTHER; PTHR12609; PTHR12609; 1.
DR SMART; SM01349; TOG; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinetochore; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..809
FT /note="Spindle pole body component alp14"
FT /id="PRO_0000064566"
FT REPEAT 127..164
FT /note="HEAT 1"
FT REPEAT 167..204
FT /note="HEAT 2"
FT REGION 233..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 637..697
FT /evidence="ECO:0000255"
FT COMPBIAS 236..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 809 AA; 89446 MW; 78B2027F0EC9A939 CRC64;
MSQDQEEDYS KLPLESRIVH KVWKVRLSAY EECSKSFSLS ADGSDNCFEL WNNQSELWKS
VLTDSNVAAQ EAGTAAFVAY CRFSDPSHLL KAREISVLSI SEKCLTSPRA GTRENALEAL
MLLVEADSAA PVIESIIPSL SARSPKVIAS NVAAIASLVE QFGAKVIPSK MIIPHISNLF
GHADKNVRKE ASRLTVNIYR WTGDPLKDLL FKDLRPVQTK ELESLFAELP TEPPKQTRFL
KSQQPTSEPN VETQVEEQPA LENEESEPEP SDDQFDLVEE VDVLPNVDPN LETLMASSKW
KDRKEALDKL LPVLSQPKIK DNDFFNLVAI LTKSVSKDAN IMVVINAAHC IQAMAKGLRS
NFSKYASTSI NALLERSKEK KANVIESLSS AMDAVLATSS LDDLAELIAS FAGNKNPQIK
SSCFSLFSRS FSNMTSLPSK FTVDTCAKAC VPGVSDTFEP VRSAAAEALG VLMKLVGERA
INQYLSPLDD IRKSKIRSFY ETATVKAKAP TKKSKVKPSK QEESKVVVPS NAKAVKKSVV
PSSPVVPSPR KATNKSLSMD VSKGNAFENG PLLPRPTTRP VSRGLSRGTS SSLQQKVKAS
TPLNSGALNE TVQNLKNMEL DDPAPQPAKH SRVDRYEHPK VLEDNDSTIS SLESLKRENE
ELREQLKVEH EENISMQKQL SELKGELNTL RSARKASPIG DRKPAFMRRA NTDFLELSTS
PSFQRSVREF EPTRPKLYSS IDVNQRSPLA SAKTNGNFTF HAELPRSPFS SRANNINPDW
TKAIDLAAKL KQKITEMKQT DQRHQGLIH
