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RGI1_YEAST
ID   RGI1_YEAST              Reviewed;         161 AA.
AC   P40043; D3DLX2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Respiratory growth induced protein 1;
GN   Name=RGI1; OrderedLocusNames=YER067W;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   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   INDUCTION.
RX   PubMed=10770760; DOI=10.1128/aac.44.5.1255-1265.2000;
RA   Bammert G.F., Fostel J.M.;
RT   "Genome-wide expression patterns in Saccharomyces cerevisiae: comparison of
RT   drug treatments and genetic alterations affecting biosynthesis of
RT   ergosterol.";
RL   Antimicrob. Agents Chemother. 44:1255-1265(2000).
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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [7]
RP   INDUCTION.
RX   PubMed=15870279; DOI=10.1128/mcb.25.10.4075-4091.2005;
RA   Lai L.C., Kosorukoff A.L., Burke P.V., Kwast K.E.;
RT   "Dynamical remodeling of the transcriptome during short-term anaerobiosis
RT   in Saccharomyces cerevisiae: differential response and role of Msn2 and/or
RT   Msn4 and other factors in galactose and glucose media.";
RL   Mol. Cell. Biol. 25:4075-4091(2005).
RN   [8]
RP   INDUCTION.
RX   PubMed=18756096;
RA   Seo H.Y., Chang Y.J., Chung Y.J., Kim K.S.;
RT   "Proteomic analysis of recombinant Saccharomyces cerevisiae upon iron
RT   deficiency induced via human H-ferritin production.";
RL   J. Microbiol. Biotechnol. 18:1368-1376(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-161, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=20567505; DOI=10.1371/journal.pone.0011163;
RA   Domitrovic T., Kozlov G., Freire J.C., Masuda C.A., da Silva Almeida M.,
RA   Montero-Lomeli M., Atella G.C., Matta-Camacho E., Gehring K.,
RA   Kurtenbach E.;
RT   "Structural and functional study of YER067W, a new protein involved in
RT   yeast metabolism control and drug resistance.";
RL   PLoS ONE 5:E11163-E11163(2010).
CC   -!- FUNCTION: Involved in the control of energetic metabolism and
CC       significantly contribute to cell fitness, especially under respiratory
CC       growth conditions. {ECO:0000269|PubMed:20567505}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20567505};
CC       Peripheral membrane protein {ECO:0000269|PubMed:20567505}.
CC   -!- INDUCTION: Up-regulated by a wide range of conditions, such as
CC       intracellular iron depletion, carbon source restriction, high
CC       temperature, high osmotic stress, cold stress, unfolded protein
CC       response, and high hydrostatic pressure. The promoter contains several
CC       binding sites for the stress response transcription factors MSN2, MSN4
CC       and HSF1. Down-regulated when treated with different antifungal drugs
CC       from the azole class. {ECO:0000269|PubMed:10770760,
CC       ECO:0000269|PubMed:15870279, ECO:0000269|PubMed:18756096}.
CC   -!- MISCELLANEOUS: Present with 8450 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the RGI1 family. {ECO:0000305}.
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DR   EMBL; U18813; AAB64603.1; -; Genomic_DNA.
DR   EMBL; AY692724; AAT92743.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07726.1; -; Genomic_DNA.
DR   PIR; S50570; S50570.
DR   RefSeq; NP_010990.1; NM_001178958.1.
DR   PDB; 3BCY; X-ray; 1.70 A; A=11-161.
DR   PDBsum; 3BCY; -.
DR   AlphaFoldDB; P40043; -.
DR   SMR; P40043; -.
DR   BioGRID; 36810; 49.
DR   DIP; DIP-5346N; -.
DR   IntAct; P40043; 2.
DR   MINT; P40043; -.
DR   STRING; 4932.YER067W; -.
DR   iPTMnet; P40043; -.
DR   MaxQB; P40043; -.
DR   PaxDb; P40043; -.
DR   PRIDE; P40043; -.
DR   EnsemblFungi; YER067W_mRNA; YER067W; YER067W.
DR   GeneID; 856797; -.
DR   KEGG; sce:YER067W; -.
DR   SGD; S000000869; RGI1.
DR   VEuPathDB; FungiDB:YER067W; -.
DR   eggNOG; ENOG502RZ9F; Eukaryota.
DR   GeneTree; ENSGT00940000176408; -.
DR   HOGENOM; CLU_118207_0_0_1; -.
DR   InParanoid; P40043; -.
DR   OMA; YAEETEY; -.
DR   BioCyc; YEAST:G3O-30241-MON; -.
DR   ChiTaRS; RGI1; yeast.
DR   EvolutionaryTrace; P40043; -.
DR   PRO; PR:P40043; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40043; protein.
DR   GO; GO:0071944; C:cell periphery; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006112; P:energy reserve metabolic process; IMP:SGD.
DR   Gene3D; 3.40.1000.40; -; 1.
DR   InterPro; IPR022554; RGI1.
DR   InterPro; IPR038235; RGI1_sf.
DR   Pfam; PF10843; RGI1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Isopeptide bond; Membrane; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..161
FT                   /note="Respiratory growth induced protein 1"
FT                   /id="PRO_0000202633"
FT   CROSSLNK        68
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   STRAND          17..27
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   HELIX           28..40
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   HELIX           56..60
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   TURN            61..64
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   HELIX           78..90
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   HELIX           92..99
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   STRAND          108..114
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   STRAND          116..129
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   STRAND          132..145
FT                   /evidence="ECO:0007829|PDB:3BCY"
FT   STRAND          149..159
FT                   /evidence="ECO:0007829|PDB:3BCY"
SQ   SEQUENCE   161 AA;  18989 MW;  31C2929EBB19BF37 CRC64;
     MTKKDKKEVK VQTVTTEDGE TVKVFEDLQG FETFIANETE DDDFDHLHCK LNYYPPFVLH
     ESHEDPEKIS DAANSHSKKF VRHLHQHIEK HLLKDIKQAV RKPELKFHEK SKEETFDKIT
     WHYGEETEYH GRPFKIDVQV VCTHEDAMVF VDYKTHPVGA N
 
 
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