SGD1_YEAST
ID SGD1_YEAST Reviewed; 899 AA.
AC Q06132; D6VYX6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Suppressor of glycerol defect protein 1;
GN Name=SGD1; OrderedLocusNames=YLR336C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11042259; DOI=10.1016/s0014-5793(00)02087-1;
RA Akhtar N., Paahlman A.-K., Larsson K., Corbett A.H., Adler L.;
RT "SGD1 encodes an essential nuclear protein of Saccharomyces cerevisiae that
RT affects expression of the GPD1 gene for glycerol 3-phosphate
RT dehydrogenase.";
RL FEBS Lett. 483:87-92(2000).
RN [4]
RP FUNCTION, AND INTERACTION WITH PLC1.
RX PubMed=12073033; DOI=10.1007/s00438-002-0647-8;
RA Lin H., Nguyen P.H., Vancura A.;
RT "Phospholipase C interacts with Sgd1p and is required for expression of
RT GPD1 and osmoresistance in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 267:313-320(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-736, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in osmoregulatory glycerol response, probably
CC through its interaction with PLC1 which regulates the expression of
CC GDP1. {ECO:0000269|PubMed:11042259, ECO:0000269|PubMed:12073033}.
CC -!- SUBUNIT: Interacts with PLC1. {ECO:0000269|PubMed:12073033}.
CC -!- INTERACTION:
CC Q06132; Q12099: FAL1; NbExp=4; IntAct=EBI-34377, EBI-6776;
CC Q06132; P32383: PLC1; NbExp=3; IntAct=EBI-34377, EBI-13485;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11042259,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
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DR EMBL; U19028; AAB67262.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09642.1; -; Genomic_DNA.
DR PIR; S51341; S51341.
DR RefSeq; NP_013440.1; NM_001182225.1.
DR AlphaFoldDB; Q06132; -.
DR SMR; Q06132; -.
DR BioGRID; 31600; 91.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR ComplexPortal; CPX-242; FAL1-SGD1 complex.
DR DIP; DIP-6333N; -.
DR IntAct; Q06132; 28.
DR MINT; Q06132; -.
DR STRING; 4932.YLR336C; -.
DR iPTMnet; Q06132; -.
DR MaxQB; Q06132; -.
DR PaxDb; Q06132; -.
DR PRIDE; Q06132; -.
DR EnsemblFungi; YLR336C_mRNA; YLR336C; YLR336C.
DR GeneID; 851049; -.
DR KEGG; sce:YLR336C; -.
DR SGD; S000004328; SGD1.
DR VEuPathDB; FungiDB:YLR336C; -.
DR eggNOG; KOG2141; Eukaryota.
DR GeneTree; ENSGT00940000153458; -.
DR HOGENOM; CLU_006786_2_0_1; -.
DR InParanoid; Q06132; -.
DR OMA; MQYYAKK; -.
DR BioCyc; YEAST:G3O-32415-MON; -.
DR PRO; PR:Q06132; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06132; protein.
DR GO; GO:0097078; C:FAL1-SGD1 complex; IDA:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0032774; P:RNA biosynthetic process; IMP:ComplexPortal.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51366; MI; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..899
FT /note="Suppressor of glycerol defect protein 1"
FT /id="PRO_0000269652"
FT DOMAIN 335..540
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 644..781
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 24..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 899 AA; 102853 MW; 8EEFDB8258407FF3 CRC64;
MQKTDGIRIP GVILDELKTL DYSQDERFSI SEGKKRRRGN GKHLSRKEKR KMERADKKRK
IISTREINSS RLKSAPTSEK RSANAGVKNV GKQANGKNPI SSDESESNEN WDSDEVLTDE
VAEESGEQAM SAEETMKKLE SLKRKAKGIQ GAENSGEIKG NSYEKKHIRN RDTNENFVSY
PLAPSDRSAF ERDEMDMQYY AKKLGLKGER KAIHAKDEFD AIGGLLEGLE YFENYGKSDE
EYGDFATETN SMRKDDEASE KAFSSDDDLS ASDFEDSDGL SESDNDSVAD SDDNYRREKE
NPYVAPTQSV ESYVPPSLRK KLDDSENNST LSEISKKVNS SLNKLSDSNI TIIITDLNRL
YDSLPRQYVT ESLTKGILNI ISQNQKLLDG FIMNYAALAY TLSKLRGIEV GAFFIQKTVE
AFLHHYEEEM ENILKDQQSK ISSKICINIA TLLSYCYNFG FVSCRLIYDI IRIFVADPNE
FTTELLLRII SISGQLIRGD DPSALRDIRS ELLKNAKNLK EQSPRLRFLM DTMSDLKNNR
LKPSILATDH HPLKKNLQSI LNSSSSWEPL QVSLEDIKNI DSKGKWWLVG ASWRGNMENA
FEVSINNEND ASKSKKSKIS IEDDLLDDIP DWNIIARQQR MNTDIRRAIF ISIMSAQDYL
DAFSKLEKLS LKNKQVLEIP RIVLHCLLAD SGSNGYNHYY ALVANKICER YSHLSKSFQF
LFWDVIKKFE DKEFDSESDT DEEDDLDDKE KLLRISNQGR FFGSLLANDI LKLDVFKHVP
FMGGLNTEGM LFMEILLFQL FLTVAKKSEK KLKMDESGNK RIIYSDDYLR DVLTKNVKSE
NMLFILKGLK WFINKKFRYH NFLAGKKGDK AFDRDERRLA WASKAAKSII DKELENIDS
