ID   SGM1_YEAST              Reviewed;         707 AA.
AC   P47166; D6VWV2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Protein SGM1;
DE   AltName: Full=Slow growth on galactose and mannose protein 1;
GN   Name=SGM1; OrderedLocusNames=YJR134C; ORFNames=J2120;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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.
RX   PubMed=10628851; DOI=10.1007/pl00013817;
RA   Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H.,
RA   Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G., Kramer W.,
RA   Klein S., Koetter P., Kricke J., Launhardt H., Mannhaupt G., Maierl A.,
RA   Meyer P., Mewes W., Munder T., Niedenthal R.K., Ramezani Rad M.,
RA   Roehmer A., Roemer A., Rose M., Schaefer B., Siegler M.-L., Vetter J.,
RA   Wilhelm N., Wolf K., Zimmermann F.K., Zollner A., Hinnen A.;
RT   "Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by
RT   a systematic approach.";
RL   Mol. Gen. Genet. 262:683-702(1999).
RN   [4]
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   [5]
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   [6]
RP   INTERACTION WITH YPT6.
RX   PubMed=16473623; DOI=10.1016/s0076-6879(05)03052-1;
RA   Siniossoglou S.;
RT   "Affinity purification of Ypt6 effectors and identification of TMF/ARA160
RT   as a Rab6 interactor.";
RL   Methods Enzymol. 403:599-607(2005).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-571 AND SER-589, AND
RP   IDENTIFICATION BY 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-549; SER-568;
RP   SER-571 AND SER-576, 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).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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: Required for normal growth rate on galactose and mannose.
CC       {ECO:0000269|PubMed:10628851}.
CC   -!- SUBUNIT: Interacts with YPT6. {ECO:0000269|PubMed:16473623}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SGM1 family. {ECO:0000305}.
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DR   EMBL; Z49634; CAA89665.1; -; Genomic_DNA.
DR   EMBL; Z49635; CAA89667.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08918.1; -; Genomic_DNA.
DR   PIR; S57157; S57157.
DR   RefSeq; NP_012668.3; NM_001181792.3.
DR   AlphaFoldDB; P47166; -.
DR   SMR; P47166; -.
DR   BioGRID; 33889; 99.
DR   DIP; DIP-2973N; -.
DR   IntAct; P47166; 3.
DR   MINT; P47166; -.
DR   STRING; 4932.YJR134C; -.
DR   iPTMnet; P47166; -.
DR   MaxQB; P47166; -.
DR   PaxDb; 4932-YJR134C; -.
DR   PeptideAtlas; P47166; -.
DR   EnsemblFungi; YJR134C_mRNA; YJR134C; YJR134C.
DR   GeneID; 853598; -.
DR   KEGG; sce:YJR134C; -.
DR   AGR; SGD:S000003895; -.
DR   SGD; S000003895; SGM1.
DR   VEuPathDB; FungiDB:YJR134C; -.
DR   eggNOG; KOG4673; Eukaryota.
DR   HOGENOM; CLU_018551_0_0_1; -.
DR   InParanoid; P47166; -.
DR   OMA; WPNGYRI; -.
DR   OrthoDB; 2015082at2759; -.
DR   BioCyc; YEAST:G3O-31751-MONOMER; -.
DR   Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   BioGRID-ORCS; 853598; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P47166; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47166; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:SGD.
DR   GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR   InterPro; IPR022092; TMF_DNA-bd.
DR   InterPro; IPR022091; TMF_TATA-bd.
DR   PANTHER; PTHR46515:SF1; TATA ELEMENT MODULATORY FACTOR; 1.
DR   PANTHER; PTHR46515; TATA ELEMENT MODULATORY FACTOR TMF1; 1.
DR   Pfam; PF12329; TMF_DNA_bd; 1.
DR   Pfam; PF12325; TMF_TATA_bd; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Golgi apparatus; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..707
FT                   /note="Protein SGM1"
FT                   /id="PRO_0000203121"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          122..473
FT                   /evidence="ECO:0000255"
FT   COILED          594..706
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         576
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   707 AA;  81171 MW;  BA47D1A7265BF3D9 CRC64;
     MSKKLSLEER LSLATKKGRK KNKRSTSNLS SPSPVVLSNN EQESARTSID DAAAGVVSID
     NAENIDDPAV RSESTVEGDT GKADSIAVDD VVHPDHNRTD CFDDTMVSLP TWLPKNYTEF
     TVEELVKEIS PEYLRLNKQI DDLTNELNRK SQIETTDSSF FKLIKEKDDL IDQLRKEGAK
     LAETELRQSN QIKALRTKVK DLEYEVSELN DSSAQSVENY NELQSLYHNI QGQLAEATNK
     LKDADKQKES LETLEKNIKE KDDLITILQQ SLDNMRTLLE KEKSEFQTEK KALQEATVDQ
     VTTLETKLEQ LRIELDSSTQ NLDAKSNRDF VDDQQSYEEK QHASFQYNRL KEQLESSKAN
     WDSIEYALNT KIVNLENRFE STMKEKNDIE EKYQTALRSS ETLGKQLEKE KENHSKAVLE
     VKDLERRAET LKSSLQSISD DYNLLKKKYE IQRSQLEQKE NELKPHQENS NEKIIDKIPV
     ELTDSLNSME GNIEDEWTLP QENSMLSLSM SKLGELESDP SLKPIYNESH ETICSEESQH
     FDRKNVDFSI DDIPEEAAAL QAIREGESMN SLNNTSIPYR RASVQLSNSN GHISAHLVNK
     LSTELKRLEG ELSASKELYD NLLKEKTKAN DEILRLLEEN DKFNEVNKQK DDLLKRVEQM
     QSKLETSLQL LGEKTEQVEE LENDVSDLKE MMHQQVQQMV EMQGKMR
//