ID   NSG1_YEAST              Reviewed;         291 AA.
AC   P38837; D3DL82; Q6Q5G1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Protein NSG1;
DE   AltName: Full=INSIG homolog 1;
GN   Name=NSG1; OrderedLocusNames=YHR133C;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HMG2.
RX   PubMed=16270032; DOI=10.1038/sj.emboj.7600855;
RA   Flury I., Garza R., Shearer A., Rosen J., Cronin S., Hampton R.Y.;
RT   "INSIG: a broadly conserved transmembrane chaperone for sterol-sensing
RT   domain proteins.";
RL   EMBO J. 24:3917-3926(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, 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   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, 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: Stabilizes the HMG-CoA reductase HMG2 by preventing its HRD1-
CC       dependent degradation. Binds directly to the sterol-sensing domain
CC       (SSD)-containing transmembrane region of HMG2, promoting its folding to
CC       protect it from degradation. {ECO:0000269|PubMed:16270032}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16270032}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16270032}.
CC   -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the INSIG family. {ECO:0000305}.
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DR   EMBL; U10398; AAB68416.1; -; Genomic_DNA.
DR   EMBL; AY558109; AAS56435.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06826.1; -; Genomic_DNA.
DR   PIR; S48977; S48977.
DR   RefSeq; NP_012001.1; NM_001179263.1.
DR   AlphaFoldDB; P38837; -.
DR   SMR; P38837; -.
DR   BioGRID; 36566; 79.
DR   DIP; DIP-2775N; -.
DR   IntAct; P38837; 9.
DR   MINT; P38837; -.
DR   STRING; 4932.YHR133C; -.
DR   iPTMnet; P38837; -.
DR   MaxQB; P38837; -.
DR   PaxDb; 4932-YHR133C; -.
DR   PeptideAtlas; P38837; -.
DR   EnsemblFungi; YHR133C_mRNA; YHR133C; YHR133C.
DR   GeneID; 856535; -.
DR   KEGG; sce:YHR133C; -.
DR   AGR; SGD:S000001175; -.
DR   SGD; S000001175; NSG1.
DR   VEuPathDB; FungiDB:YHR133C; -.
DR   eggNOG; ENOG502QX4Q; Eukaryota.
DR   GeneTree; ENSGT00580000081600; -.
DR   HOGENOM; CLU_088332_0_0_1; -.
DR   InParanoid; P38837; -.
DR   OMA; PMISECL; -.
DR   OrthoDB; 1982254at2759; -.
DR   BioCyc; YEAST:G3O-31171-MONOMER; -.
DR   BioGRID-ORCS; 856535; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38837; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38837; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR   GO; GO:0016126; P:sterol biosynthetic process; IMP:SGD.
DR   InterPro; IPR025929; INSIG_fam.
DR   PANTHER; PTHR15301; INSULIN-INDUCED GENE 1; 1.
DR   PANTHER; PTHR15301:SF3; PROTEIN NSG1-RELATED; 1.
DR   Pfam; PF07281; INSIG; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..291
FT                   /note="Protein NSG1"
FT                   /id="PRO_0000202918"
FT   TOPO_DOM        1..96
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..156
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..261
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        8
FT                   /note="N -> T (in Ref. 3; AAS56435)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   291 AA;  32214 MW;  D0A634938AAD118E CRC64;
     MGKKKSKNQL NTGGVPNGVH NTKKEAALPP LGNKLGSASF TAINTLTKPA LFSFYDDDIT
     KNEGNVYDKA LLSNASQLEM VPPSATARHE RSLYAKIINT IAAFFILFIA GILFPMISEC
     LFDNDQLAKG DIVSFLKHGI EIKNKIVAEP DMVPDWAVFG TEGVIFGSIV PFIDSFVRYQ
     HQPKTRSSVY KNTLGSFIRC ANTLLGLIFG IRKLEWSSSL QAAGAWSLLN IVLWLFFDGT
     LTVFFPGLVI GALSAFTCSQ CFSQLSLALY FIDFYFFGFL MFSKLGRYLF N
//