MUG79_SCHPO
ID MUG79_SCHPO Reviewed; 1318 AA.
AC Q92349;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Meiotically up-regulated gene 79 protein;
GN Name=mug79; ORFNames=SPAC6G9.04;
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 SPORULATION.
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).
CC -!- FUNCTION: Appears to have a role in sporulation.
CC {ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB03606.1; -; Genomic_DNA.
DR PIR; T39066; T39066.
DR RefSeq; NP_594113.1; NM_001019537.2.
DR AlphaFoldDB; Q92349; -.
DR BioGRID; 277959; 48.
DR STRING; 4896.SPAC6G9.04.1; -.
DR PaxDb; Q92349; -.
DR PRIDE; Q92349; -.
DR EnsemblFungi; SPAC6G9.04.1; SPAC6G9.04.1:pep; SPAC6G9.04.
DR GeneID; 2541456; -.
DR KEGG; spo:SPAC6G9.04; -.
DR PomBase; SPAC6G9.04; -.
DR VEuPathDB; FungiDB:SPAC6G9.04; -.
DR HOGENOM; CLU_260108_0_0_1; -.
DR OMA; MDIQETF; -.
DR PRO; PR:Q92349; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IMP:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0031322; P:ascospore-type prospore-specific spindle pole body remodeling; IMP:PomBase.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0070583; P:spore membrane bending pathway; IMP:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Meiosis; Nucleus; Reference proteome; Sporulation.
FT CHAIN 1..1318
FT /note="Meiotically up-regulated gene 79 protein"
FT /id="PRO_0000116628"
FT DOMAIN 1049..1158
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 177..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1318 AA; 150943 MW; 24DEF138A95FBDD0 CRC64;
MDFRITEGSS PTSLSVSEKI AKLESCNDSR ITCRPVRESK PTYTSGQKHS ALLSKLKRSK
VTTDFCKLEE SKGIICQENL HTEGAKSKTE NISGEDKSSQ RRTRLKQIQE FISHRRSFLN
SNANSVESEK ILAENNHMFN VKSKLSNKES FIKTRRPRTN GELSDLSLQP KRIFSEPVNS
HPSQSMFGNG VRASSGSYSL KRDLKDYEEE LPSSKKRQRT PPPIVVTNFP QEIFPSKKIS
LSAKRRIQGK YSGENVRARI ELARERNRKR DYVSNLSKGH TTNALEENPF NLGPNYRAST
RKCNRIKEAI NLFAAKNGSM EVPPKVSVGD SVLTTSQKFL QVIREKTALL MNQDSNSVQP
QALAAAESPT TKAPTTKAPT SEAPPKGHVK QLAKQLGNIY MPQSINNVEP TSHSSISKVV
NPSEKVISKI ERACLAGNGN VHPSIKMEKN LELNPHPRTL NATEHKINSR IQVSKLNTKN
ELANADPKMY LLENLSDRLY FCKLAKLLLR KYPLDIAEHQ FALVYSRFQR IPLKQISCLK
QSLVAYYSVL SEVGITNEIM LRENRFSSPK TPEGLVSISK LLLDDREHLS HDERSYIQQL
QSQIKSQSVH HENAAEEIRK MRNLRNSRIN SQQVGEKVFV NPDVKTMDIQ ETFLQDYEDE
TFANEGLSAS KFKEEFLLIS DSKSDLNSEE IATPNSLEFK NNPRIKVPRS LLTILNLHDR
SQLKLFEVCH NSEFKDPINL SNCLRNLLEK QLLSYNFTDW FASLGSEYEN VYVKFISHYD
FSSLNVYASF QKLCCDLYYG SDDYIHSPIL QVFASCWLKQ NSNYGFLNED IIVKIVLILI
DLHKSTYSKK LNSYVVPMET FVKYALEKLR PLISPDSVCI LSKEDKKHWL KYKKNRSTFA
KLLFSTWSNL PSDIGFILEC MLKEYYDTFL KSPFAVPNAV QAQLHNQVRG DLTPKRNRSS
LISELMKSSK LLKQESSGNK NSTSLESDAF KESSFVLNEE NGGIYAGKEI DLPEPSVIDG
RPHFSVFNYT HHMQEEKTHN RLPWHRRGMI SYKKMVLSKN NRWVAGYWKK KYCIVDSGKL
IFYKSDHLDP NACSNVSPIH REFGLQSCLA SPNLPPSINS NRNNVFYLNI PGNECYLFEA
PSVLAMNEWI HSLNFNAAMI TCPPLPENIT NTEYGWGYIL TRAEKKAYYT AADGTKTFVG
DLAQLTRWSP MDIQGLQDIP RPLRDKVHIL RDCVPSLLET CLLFQSLPEK MEKCFAAGSK
NYLKAMDNWN RKMKFLYERS MMYKEYQRVL ECEYEYRKSH DFYPTLSPVR YPYDFKGL
