MPS2_YEASO
ID MPS2_YEASO Reviewed; 387 AA.
AC E7NHN2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Monopolar spindle protein 2;
GN Name=MPS2; Synonyms=MMC1; ORFNames=FOSTERSO_1678;
OS Saccharomyces cerevisiae (strain FostersO) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=764101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FostersO;
RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "Whole-genome comparison reveals novel genetic elements that characterize
RT the genome of industrial strains of Saccharomyces cerevisiae.";
RL PLoS Genet. 7:E1001287-E1001287(2011).
CC -!- FUNCTION: Component of the spindle pole body (SPB) required for
CC insertion of the nascent SPB into the nuclear envelope and for the
CC proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BBP1, MPS3, and SPC24. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MPS2 family. {ECO:0000305}.
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; AEEZ01000040; EGA62297.1; -; Genomic_DNA.
DR PRIDE; E7NHN2; -.
DR EnsemblFungi; EGA62297; EGA62297; FOSTERSO_1678.
DR HOGENOM; CLU_069890_0_0_1; -.
DR OMA; FIYAKDF; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:0071988; P:protein localization to spindle pole body; IEA:InterPro.
DR GO; GO:0030474; P:spindle pole body duplication; IEA:InterPro.
DR InterPro; IPR031433; Mps2.
DR Pfam; PF17060; MPS2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Nucleus; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..387
FT /note="Monopolar spindle protein 2"
FT /id="PRO_0000409166"
FT TRANSMEM 311..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 216..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..269
FT /evidence="ECO:0000255"
FT COMPBIAS 216..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 44583 MW; BAF5A77132977324 CRC64;
MSNGAFDAIF EYAWGQIDKP ISGDFIYGKD LPKLIEIIEN IFQKAQKSGS YELRLPLFSE
INKDLFRTFS NTKTFFKIHK EEFDDIFFNL VNHPLREILE NAFIGVDSIP SDFIVSMNLN
SPSKFLVENK NKNTEGAGIS TPRKKLTESP IKLLSRXNIG KALEVQVEEL KRELTAKQSL
LQENERQVSE LKIRLETYQE KYASIQQRFS DLQKARQVED NQNSSRTSDP GSPLVTGIDQ
KAILEEFRRR LQRQTDTISF LKDQIRRERG LNCSNDKVSH SKRKHATTDG DGTFKNFISA
VPSNIWVKAT IRIIVCFALL AGVLPYIRKY VYAHDTPSQN SRLQLSWWEN SGILSKIVWF
FEDQTDLETE YRSNANVDDA YSRVFGI