MBO1_SCHPO
ID MBO1_SCHPO Reviewed; 1115 AA.
AC O94488;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Microtubule organizer protein 1;
DE AltName: Full=Morphology defective protein 20;
GN Name=mbo1; Synonyms=mod20, mto1; ORFNames=SPCC417.07c;
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, INTERACTION WITH MCP6, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15120067; DOI=10.1016/j.cub.2004.03.042;
RA Sawin K.E., Lourenco P.C.C., Snaith H.A.;
RT "Microtubule nucleation at non-spindle pole body microtubule-organizing
RT centers requires fission yeast centrosomin-related protein mod20p.";
RL Curr. Biol. 14:763-775(2004).
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, AND SUBCELLULAR LOCATION.
RX PubMed=15004232; DOI=10.1091/mbc.e03-10-0728;
RA Venkatram S., Tasto J.J., Feoktistova A., Jennings J.L., Link A.J.,
RA Gould K.L.;
RT "Identification and characterization of two novel proteins affecting
RT fission yeast gamma-tubulin complex function.";
RL Mol. Biol. Cell 15:2287-2301(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-94; SER-1005 AND SER-1009,
RP 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 cytoplasmic astral microtubule growth during
CC mitosis. Involved in localizing components of the gamma-tubulin complex
CC to the non-spindle pole body (non-SPB) microtubule organizing centers
CC (MTOCs). Required for new microtubule nucleation from non-SPB sites
CC during interphase. {ECO:0000269|PubMed:15004232,
CC ECO:0000269|PubMed:15120067}.
CC -!- SUBUNIT: Interacts with mcp6. {ECO:0000269|PubMed:15120067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:15004232,
CC ECO:0000269|PubMed:15120067, ECO:0000269|PubMed:16823372}.
CC Note=Localizes at the interphase MTOC (iMTOC) and at the equatorial
CC MTOC (eMTOC) at the end of mitosis.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAA22653.1; -; Genomic_DNA.
DR PIR; T41342; T41342.
DR RefSeq; NP_588284.1; NM_001023274.2.
DR AlphaFoldDB; O94488; -.
DR SMR; O94488; -.
DR BioGRID; 276030; 96.
DR IntAct; O94488; 1.
DR STRING; 4896.SPCC417.07c.1; -.
DR iPTMnet; O94488; -.
DR MaxQB; O94488; -.
DR PaxDb; O94488; -.
DR PRIDE; O94488; -.
DR EnsemblFungi; SPCC417.07c.1; SPCC417.07c.1:pep; SPCC417.07c.
DR GeneID; 2539467; -.
DR KEGG; spo:SPCC417.07c; -.
DR PomBase; SPCC417.07c; -.
DR VEuPathDB; FungiDB:SPCC417.07c; -.
DR eggNOG; ENOG502QU0H; Eukaryota.
DR HOGENOM; CLU_279796_0_0_1; -.
DR InParanoid; O94488; -.
DR OMA; IGNILFW; -.
DR PhylomeDB; O94488; -.
DR PRO; PR:O94488; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IDA:PomBase.
DR GO; GO:0061496; C:half bridge of mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0031021; C:interphase microtubule organizing center; IDA:PomBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:PomBase.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0061499; C:outer plaque of mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0099070; C:static microtubule bundle; IDA:PomBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:PomBase.
DR GO; GO:0030954; P:astral microtubule nucleation; EXP:PomBase.
DR GO; GO:0072766; P:centromere clustering at the mitotic interphase nuclear envelope; IMP:PomBase.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IMP:PomBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; EXP:PomBase.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0051415; P:microtubule nucleation by interphase microtubule organizing center; IMP:PomBase.
DR GO; GO:0140405; P:spindle pole body-led chromosome movement during mitotic interphase; IMP:PomBase.
DR InterPro; IPR012943; Cnn_1N.
DR InterPro; IPR024545; Mto2p-binding.
DR Pfam; PF07989; Cnn_1N; 1.
DR Pfam; PF12808; Mto2_bdg; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1115
FT /note="Microtubule organizer protein 1"
FT /id="PRO_0000356169"
FT REGION 25..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 445..915
FT /evidence="ECO:0000255"
FT COILED 1072..1102
FT /evidence="ECO:0000255"
FT COMPBIAS 30..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1115 AA; 128469 MW; 8CA5503EC141E3E0 CRC64;
MEENSSELDS NNFNVLVDNL AGLSLTDEEV RRILSPRKEG SRQLPSSTSK DEDSEEASHK
YDFEIDRDSL KSDSGSPRLH QNATAPTSST PLQSPDESVN KLNSEDEEGN SSVAPFFLDT
TNFDRLNDNI TTDDEQLSPV LTANQGFQSQ EQYEEDSYNN YDYTSDPSSP NYISSSLDQL
PHLDDEDDLQ LTPIKEERNY LHSQDAPTTN ALSKKISDIL IPASAMKDLK DRKNALAKEF
EESQPGSSLT LKEQANVIDN LRKEVFGLKL KCYFLYDQLN KFHDQEVQDI MKQNIDLKTL
TMELQRAVAG YEKKISGLES RIKPDQSFNL STPSPAPSNL ITLQSRYSQA LSELETTKRA
FAALRKEKSK KTNYSVGAYN EDRNVLSNML DNERREKEAL LQELESLRVQ LSKKVPMPAK
NTDERVIETL QRSNELLRMD ISMQNEALLL RKQENDRLVK QVEELTVALN SGKMNAIVEA
ESSKNELWDS MMVSRMKTQE QSIELTRLYK QLQDIEEDYE NKLMRMEQQW REDVDQLQEY
VEEITQELQD TKEVLSKSSK ESDDYEEVVG KLRTEAEREI EKFEKTIREN EESISLFKEE
VEKLTDEITQ LSERYNDKCH EFDELQKRLQ TLEEENNKAK EDSTSKTSNL LEQLKMTEAE
VDSLRKENEE NKQVIALKES ELVKSNDNKL LLNEQIESLN DQLSQLKTEM ESVTTSKESL
ADYLSNLKER HNDELDSLNK KLREFEGILS SNSSLKSEIE ERNNQYVTLR ENFDSLQNAI
METFDKQVTH CSVNHLVQQI RKLKDENKKD QSGTDKLMKK IYHCEQSLKE KTNSLETLVS
EKKELKNLLD AERRSKKAIQ LELENLSSQA FRRNLSGSSS PSERSQSREL KLLQASEKRL
KEQVEERNSL IKNIVTRFTQ LNTGSKPVNT NVEALTTISS MNQAVNMNFR ELDKSIQEFK
RKCQSMEREF KTELRKLDGV LEARSKRLSQ LEERVKLLGA GSTSSIPNSP RASKRVSLDS
EDKKLVPASP DKSAVQRGIT ALKRDAEGMS HIWQLRLREM EFQLKAEQEG RKRDKLGARE
RLQDLIRQNR SLSRQIKTDK ESNSRSPSIS SQEHK
