NSG1_YEAST
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 03-AUG-2022, entry version 144.
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; 67.
DR DIP; DIP-2775N; -.
DR IntAct; P38837; 9.
DR MINT; P38837; -.
DR STRING; 4932.YHR133C; -.
DR iPTMnet; P38837; -.
DR MaxQB; P38837; -.
DR PaxDb; P38837; -.
DR PRIDE; P38837; -.
DR EnsemblFungi; YHR133C_mRNA; YHR133C; YHR133C.
DR GeneID; 856535; -.
DR KEGG; sce:YHR133C; -.
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; SFVRYQH; -.
DR BioCyc; YEAST:G3O-31171-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR15301; 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
