PMD1_YEAST
ID PMD1_YEAST Reviewed; 1753 AA.
AC P32634; D3DM38;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Negative regulator of sporulation PMD1;
GN Name=PMD1; OrderedLocusNames=YER132C; ORFNames=SYGP-ORF50;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9383076; DOI=10.1093/genetics/147.3.1351;
RA Benni M.L., Neigeborn L.;
RT "Identification of a new class of negative regulators affecting
RT sporulation-specific gene expression in yeast.";
RL Genetics 147:1351-1366(1997).
RN [4]
RP FUNCTION.
RX PubMed=12524333; DOI=10.1093/genetics/162.4.1573;
RA Davis D.A., Bruno V.M., Loza L., Filler S.G., Mitchell A.P.;
RT "Candida albicans Mds3p, a conserved regulator of pH responses and
RT virulence identified through insertional mutagenesis.";
RL Genetics 162:1573-1581(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1664, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1307 AND SER-1356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1664, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP FUNCTION.
RX PubMed=19087957; DOI=10.1534/genetics.108.098434;
RA McDonald C.M., Wagner M., Dunham M.J., Shin M.E., Ahmed N.T., Winter E.;
RT "The Ras/cAMP pathway and the CDK-like kinase Ime2 regulate the MAPK Smk1
RT and spore morphogenesis in Saccharomyces cerevisiae.";
RL Genetics 181:511-523(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-298; SER-838; SER-1289;
RP SER-1307 AND SER-1664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Negatively regulates early sporulation-specific genes. Seems
CC to exert its function by positively regulating the Ras/cAMP pathway.
CC Required for growth under alkaline conditions. Acts synergetically with
CC MDS3. {ECO:0000269|PubMed:12524333, ECO:0000269|PubMed:19087957}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 815 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U18916; AAC03230.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07792.1; -; Genomic_DNA.
DR PIR; S30855; S30855.
DR RefSeq; NP_011058.3; NM_001179022.3.
DR AlphaFoldDB; P32634; -.
DR BioGRID; 36876; 70.
DR DIP; DIP-2381N; -.
DR IntAct; P32634; 12.
DR MINT; P32634; -.
DR STRING; 4932.YER132C; -.
DR iPTMnet; P32634; -.
DR MaxQB; P32634; -.
DR PaxDb; P32634; -.
DR PRIDE; P32634; -.
DR EnsemblFungi; YER132C_mRNA; YER132C; YER132C.
DR GeneID; 856869; -.
DR KEGG; sce:YER132C; -.
DR SGD; S000000934; PMD1.
DR VEuPathDB; FungiDB:YER132C; -.
DR eggNOG; KOG0379; Eukaryota.
DR GeneTree; ENSGT00940000176594; -.
DR HOGENOM; CLU_252311_0_0_1; -.
DR InParanoid; P32634; -.
DR OMA; DFEFITA; -.
DR BioCyc; YEAST:G3O-30295-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR ChiTaRS; PMD1; yeast.
DR PRO; PR:P32634; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32634; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR SUPFAM; SSF117281; SSF117281; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kelch repeat; Meiosis; Phosphoprotein; Reference proteome;
KW Repeat; Sporulation.
FT CHAIN 1..1753
FT /note="Negative regulator of sporulation PMD1"
FT /id="PRO_0000119141"
FT REPEAT 143..198
FT /note="Kelch 1"
FT REPEAT 206..253
FT /note="Kelch 2"
FT REGION 651..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1753 AA; 195383 MW; E4252998C6C2508B CRC64;
MTVLQPPSSV CYPLNLPIVP NPNLDEATRK KLTLECRTGA AVELARSGVF VHGGLTLPLN
LTIINSLQLQ KELILYFGKQ KDRNADFKTL ADWISPEIFF LDLISRTWQR INTTIDTTSE
NELNNGLSFK ERLFHSMCFT ESNIYIFGGL MVSPHNGYEL IATNELWKLD LKTKCWSLIS
ENPQITRRFN HSMHVLNENN ENQDTKLIIV GGLDNMDIPV KKIDIFNLRT SLWESESKSD
ENPASKGSSK ILVNIDGMPI SLSHDSNFSV LIENNQAEIP TLALYYPQRE ANTSRRGTDD
GSFSTYAHDL DDKSKLPKHH HHHHGDLKYF ESDDADENAV KTLMSPIVIL PLLGNSQGAR
MTSNPTQNNK ENSILQVPFH LQYPSGNYFN YNIVVIGFYP DPQPSNLHCF IYNIASGKWI
RVNIACTECS ISMHRFWKLL IWKSHHQALL LGTRTDDFCS PSVQKFDHIL SFSLPMLNGY
NKLVNTKHTR TNNGIANSHN LNVNLSLYDH LPYSNSSTIE HTNPYTVTQG YSLDDSGIPR
LTSTATSQFE NYSRYITVPL EMESTSSIFP PYAMVLGKDA LEIFGKTLSD FEFITADGDS
IGVPVYLLRK RWGRYFDSLL SNGYANTSFN YEFNGDTSNI ISFSPHTASK TTKFGNSSQS
SNGSLEKYFS KNGNSKSNSN TSLKKPHSVD FTSSTSSPKQ RAISHNKLSP SEPILCADEE
DSRSNTLKQH ATGDTGLKET GTSNKRPIST TCSSTGMVFR VPFQDMKNSK LGLSEQSGRS
TRASSVSPPP VYKKSTNDGN DSNCTLSNTP LVYRRASTVG TTTNSSVDDG FSSIRRASHP
LQSYIIAKSS PSSISKASPA EKAFSRRKSS ALRFIASPNQ SRQTSFASTA STASVVSSTS
GRRRNSNQIS HLGSSASLPN SPILPVLNIP LPPQEKIPLE PLPPVPKAPS RRSSSLAEYV
QFGRDSPVAS RRSSHSTRKS SSSDARRISN SSLLRNTLDS QLLSNSYGSD IPYEASIQEY
GMNNGRDEEE DGDNQDYGCI SPSNIRPIFS TINAININGN FKEGEFFSSK SYINNEKSRR
LSYISNPESV ESTNSNNNAI IELEPLLTPR SLYMPWSTAS VRAFAEFFYT AQINGKWLLA
PVTLDLLIMA KIYEIPILYE LITEVLYKII SKKEEGLSVT CEALLNLFQQ KVSRYCNENE
GKIRKQLDSS ESYQDTLEIK RSLANIDNGY VDSYLLRNTS MAQSIHYTDD SNGETEIDMH
HTGISSIGSL ANRAVPTVFA GGPRDSHNSI GSIAFPSNSG VQNIRRSVSL FSPATKKKSS
LSRETDPLDT SDQFTDDVPD SGPVSRQQNF PRRSSSFTET VPTEPTRYNY QNLDSSKSNR
ASDDKEEQNE QATLQDISNF DKYKVETLQK RNSNDGKDLD RTNDPLKNRG TEIPQNSSNL
ETDPFIRDSF DSDSGSSFRS DSDDLDSQLG ILPFTKMNKK LQEQTSQEFD DSIDPLYKIG
SSTPGSSRLH GSFSKYIRPN SQREDGSEYV NISSLENMVS PNALPPVDYV MKSIYRTSVL
VNDSNLMTRT KEAIELSKVL KKLKKKVLQD ISQMDDEMRE TGKPIFARGS SSPTLSRQHS
DVATPLKQQE NTRPALKFAS SSPISEGFRK SSIKFSQAPS TQISPRTSVT DFTASQQRRQ
HMNKRFSTQT THSTSALFMN PAFMPSAVNT GRKESEGHCE DRSATANRTN RKEDATTNDN
DNIAPFPFFG KRR
