ID   SNG1_YEAST              Reviewed;         547 AA.
AC   P46950; D6VUX9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Nitrosoguanidine resistance protein SNG1;
GN   Name=SNG1; OrderedLocusNames=YGR197C; ORFNames=G7591;
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 [GENOMIC DNA].
RX   PubMed=7753113; DOI=10.1016/0165-7992(95)90037-3;
RA   Grey M., Pich C.T., Haase E., Brendel M.;
RT   "SNG1 -- a new gene involved in nitrosoguanidine resistance in
RT   Saccharomyces cerevisiae.";
RL   Mutat. Res. 346:207-214(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7502584; DOI=10.1002/yea.320111110;
RA   Guerreiro P., Maia e Silva A., Barreiros T., Arroyo J., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Rodrigues-Pousada C., Nombela C.;
RT   "The complete sequence of a 9000 bp fragment of the right arm of
RT   Saccharomyces cerevisiae chromosome VII contains four previously unknown
RT   open reading frames.";
RL   Yeast 11:1087-1091(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
RP   INDUCTION.
RX   PubMed=12529331; DOI=10.1074/jbc.m208549200;
RA   Hikkel I., Lucau-Danila A., Delaveau T., Marc P., Devaux F., Jacq C.;
RT   "A general strategy to uncover transcription factor properties identifies a
RT   new regulator of drug resistance in yeast.";
RL   J. Biol. Chem. 278:11427-11432(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, AND IDENTIFICATION BY
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, 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).
CC   -!- FUNCTION: May function as a N-methyl-N'nitro-N-nitrosoguanidine (MNNG)
CC       export permease.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Transcriptionally regulated by PDR8.
CC       {ECO:0000269|PubMed:12529331}.
CC   -!- SIMILARITY: To yeast YJR015W. {ECO:0000305}.
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DR   EMBL; X74920; CAA52881.1; -; Genomic_DNA.
DR   EMBL; X82775; CAA58016.1; -; Genomic_DNA.
DR   EMBL; Z72982; CAA97224.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08290.1; -; Genomic_DNA.
DR   PIR; S53920; S53920.
DR   RefSeq; NP_011713.1; NM_001181326.1.
DR   AlphaFoldDB; P46950; -.
DR   SMR; P46950; -.
DR   BioGRID; 33450; 234.
DR   DIP; DIP-8148N; -.
DR   IntAct; P46950; 1.
DR   STRING; 4932.YGR197C; -.
DR   iPTMnet; P46950; -.
DR   PaxDb; 4932-YGR197C; -.
DR   PeptideAtlas; P46950; -.
DR   EnsemblFungi; YGR197C_mRNA; YGR197C; YGR197C.
DR   GeneID; 853111; -.
DR   KEGG; sce:YGR197C; -.
DR   AGR; SGD:S000003429; -.
DR   SGD; S000003429; SNG1.
DR   VEuPathDB; FungiDB:YGR197C; -.
DR   eggNOG; ENOG502QUA0; Eukaryota.
DR   GeneTree; ENSGT00940000176467; -.
DR   HOGENOM; CLU_020178_0_1_1; -.
DR   InParanoid; P46950; -.
DR   OMA; PLENMAM; -.
DR   OrthoDB; 1446922at2759; -.
DR   BioCyc; YEAST:G3O-30883-MONOMER; -.
DR   BioGRID-ORCS; 853111; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P46950; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P46950; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015931; P:nucleobase-containing compound transport; IMP:SGD.
DR   GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR   GO; GO:0061091; P:regulation of phospholipid translocation; IGI:SGD.
DR   InterPro; IPR022703; DUF3533.
DR   PANTHER; PTHR34814; NITROSOGUANIDINE RESISTANCE PROTEIN SNG1; 1.
DR   PANTHER; PTHR34814:SF1; NITROSOGUANIDINE RESISTANCE PROTEIN SNG1; 1.
DR   Pfam; PF12051; DUF3533; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..547
FT                   /note="Nitrosoguanidine resistance protein SNG1"
FT                   /id="PRO_0000072007"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          35..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         91
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   CONFLICT        117
FT                   /note="A -> V (in Ref. 1; CAA52881)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  61293 MW;  D4421BA2DED55420 CRC64;
     MTKSVGDEES QYIEDPSFAA AAAFTGGRDG VSYSNQRFAE GSGHSSDLAK SLEDYRPPDE
     KPSSLSSVGE GGANEEEKGG NDGGPLARIQ TGLFSPRLRN HRKKILSKFV LNNFFIACVC
     VSLISIYWGA CYGTDRYFFK VKNIVVLQDA PSNTSVQSIS AIIPSLLASV PGTWHIYNAT
     SFHRKFGTTN STEIDRKIVD LIYDERYWLA LNVKPNATDT LYNSLISQDA NSEFNSSIFF
     ESVFESGRDP SSVKSTILPL MQQLEVRLQK YYVKEYLPSL MSNITSNDRD LNINMENWAI
     AGQLLFTYND YRPFADRILM APLQVGLIYC ILLTVLQLSL YGKLHGEMAR VLKPKHILIY
     RLLISWATYF LLSIGFCTVS AIFRIDFTPA FGRGGFVVYW MSTWLVMMAV GGANENVLSL
     VIAYCPPYLS IWLMTWIILN ISASFYPMVL NNEFYRYGYI MPIHNAVDIY KVIFLNLTKR
     KMGRNYGILV AWVALNTSLM PFCMKFAGKK MQKNAMQAAE AAVAAATQRA SRPAEANTDK
     NNNPPGN
//