MU190_SCHPO
ID MU190_SCHPO Reviewed; 1188 AA.
AC Q9USG8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Meiotically up-regulated gene 190 protein;
GN Name=mug190; ORFNames=SPCP31B10.06;
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1005, 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: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-
CC pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAB58372.1; -; Genomic_DNA.
DR PIR; T41696; T41696.
DR RefSeq; NP_587862.1; NM_001022855.2.
DR AlphaFoldDB; Q9USG8; -.
DR SMR; Q9USG8; -.
DR BioGRID; 276040; 2.
DR STRING; 4896.SPCP31B10.06.1; -.
DR iPTMnet; Q9USG8; -.
DR MaxQB; Q9USG8; -.
DR PaxDb; Q9USG8; -.
DR PRIDE; Q9USG8; -.
DR EnsemblFungi; SPCP31B10.06.1; SPCP31B10.06.1:pep; SPCP31B10.06.
DR GeneID; 2539477; -.
DR KEGG; spo:SPCP31B10.06; -.
DR PomBase; SPCP31B10.06; mug190.
DR VEuPathDB; FungiDB:SPCP31B10.06; -.
DR eggNOG; KOG1012; Eukaryota.
DR HOGENOM; CLU_002125_2_0_1; -.
DR InParanoid; Q9USG8; -.
DR OMA; WDVGTFE; -.
DR PhylomeDB; Q9USG8; -.
DR PRO; PR:Q9USG8; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; ISM:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IC:PomBase.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; ISO:PomBase.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd04041; C2A_fungal; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037767; C2A_Mug190-like.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR031468; SMP_LBD.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Lipid transport;
KW Lipid-binding; Meiosis; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1188
FT /note="Meiotically up-regulated gene 190 protein"
FT /id="PRO_0000278538"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 228..453
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 451..576
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 636..781
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 544
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 544
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 549
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1188 AA; 133683 MW; 3460BED8B60C8AB1 CRC64;
MSTHSGDSTK QQHYRSSDPY SGRRPIPTIP KFFRDRKQRA EKKEEQQREQ TENEKLFDPI
TQRDVEINDV HFDYAKTYDD PSFTVPNQSI QGSSLPSEKP YLSSNQPTNV YKQHQDDLAP
PEADNQITRD VPISDEKTNI LFFPSPSIDL SYVSKEVKQK TGQYSLFAYI FSLVISWFFT
HSIIISAVLP LAISSCMYLW MQNIYAVAKD AEWGAEQKRG EYARLNLIPE SAEWMNHLLE
KVWPLINPEM FSSVADQIED VMQASIPSFV ENVRVASLDQ GSHPVRVVSI RSLPSGEASE
SFSEKQASEA EHKDEPEQQR KQFYNFELCL AYHAKPVEDA TSTSARASNL HLRIVFYPGI
KGTVGFPLPI WVEIKGFVAR IRFRCELMPE VPFLKNVTFS LMGLPELNVS AVPVAEGGVN
IFGLPLISKF VNDAISAAAN EYVSPKSMTI DLSKTLLGDD IKKEVNALGV IFVHINRAED
LSKQDVNGLS DAYITVGFHK FGKPLYCTRV VKQDLNPIWN EYAFIPVFPD QVKAGEKISI
ELWDSDRFSP DDVVGRTKIG LHLLIQDSGK MHERCDTLTG ISEDTSLPGR VFYEIGYFPR
AEFKPSLKTS GHDITIPRSM RDDPAFQNPH GSLDNKEEEA AVTTAPDEEY PSGILSFTVH
QAVNLQMNHP TGTFGNVSGN YNTSPAQSVG DVTAEEGSEL PSSYVCVDLD DTLVYKTRTK
VFTSNPIYNA GSEKFVKDWR NAMLCFTVRD FKLREHDSIL GVVNIPLATT LTTSSQLTKW
YPIQGGIGFG SVRISILFRS MKLKIPRNLL GWDIGTLEFM DRQIVAEGTG SVSDVSFSSI
RVNIAGVKIT AKSSTSNSSS TAEYHVRSRH AVIPVNNRYR SAVVFEFRKQ LQRKHNVFAM
VWLVDLEDNV EQNIRVPIFT SSKPAHVLQN MIDFDHPDKE SEFKIIGYLS TRICFHRGLD
DSHEQLVDND DEAAIFETYR CLKSMGLRRG YVKDMKNPLA DQRASLDESR ETTTASSKFE
SDDSVDTEDE ETTTDRTPIE CTQTVSMVDP NVNGDIQGRN SLGTMNSNER NLEQEFISLG
YASKNRPKAH AQEGTNQPGA SENVEPVLAD DSDAVTIHSN ISSDDQKRKL VNADDRELEK
RLHRGPYNSK IVRTGEWVKD GAKMGWRNLR RKFALNGRQP DVETEISK
