GAR1_YEAST
ID GAR1_YEAST Reviewed; 205 AA.
AC P28007; D3DL41;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit GAR1 {ECO:0000305};
DE AltName: Full=Glycine/arginine-rich protein 1 {ECO:0000303|PubMed:1531632};
DE AltName: Full=snoRNP protein GAR1;
GN Name=GAR1 {ECO:0000303|PubMed:1531632}; OrderedLocusNames=YHR089C;
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].
RC STRAIN=YNN 281;
RX PubMed=1531632; DOI=10.1002/j.1460-2075.1992.tb05099.x;
RA Girard J.-P., Lehtonen H., Caizergues-Ferrer M., Amalric F., Tollervey D.,
RA Lapeyre B.;
RT "GAR1 is an essential small nucleolar RNP protein required for pre-rRNA
RT processing in yeast.";
RL EMBO J. 11:673-682(1992).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=9303321; DOI=10.1093/emboj/16.15.4770;
RA Bousquet-Antonelli C., Henry Y., Gelugne J.-P., Caizergues-Ferrer M.,
RA Kiss T.;
RT "A small nucleolar RNP protein is required for pseudouridylation of
RT eukaryotic ribosomal RNAs.";
RL EMBO J. 16:4770-4776(1997).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN H/ACA SNORNP
RP COMPLEXES.
RX PubMed=9843512; DOI=10.1093/emboj/17.23.7078;
RA Henras A., Henry Y., Bousquet-Antonelli C., Noaillac-Depeyre J.,
RA Gelugne J.-P., Caizergues-Ferrer M.;
RT "Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs.";
RL EMBO J. 17:7078-7090(1998).
RN [7]
RP INTERACTION WITH H/ACA SNORNAS.
RX PubMed=9556561; DOI=10.1074/jbc.273.18.10868;
RA Bagni C., Lapeyre B.;
RT "Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a
RT nontypical RNA binding element.";
RL J. Biol. Chem. 273:10868-10873(1998).
RN [8]
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 [9]
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 [10]
RP SUBCELLULAR LOCATION, AND METHYLATION BY HMT1.
RX PubMed=12756332; DOI=10.1261/rna.5020803;
RA Xu C., Henry P.A., Setya A., Henry M.F.;
RT "In vivo analysis of nucleolar proteins modified by the yeast arginine
RT methyltransferase Hmt1/Rmt1p.";
RL RNA 9:746-759(2003).
RN [11]
RP CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
RX PubMed=15388873; DOI=10.1261/rna.7770604;
RA Henras A.K., Capeyrou R., Henry Y., Caizergues-Ferrer M.;
RT "Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form
RT a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA
RT snoRNAs.";
RL RNA 10:1704-1712(2004).
RN [12]
RP FUNCTION, AND IDENTIFICATION IN THE H/ACA SNORNP COMPLEX.
RX PubMed=21131909; DOI=10.1038/emboj.2010.316;
RA Wu G., Xiao M., Yang C., Yu Y.T.;
RT "U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81
RT RNP.";
RL EMBO J. 30:79-89(2011).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [14]
RP METHYLATION AT ARG-15; ARG-19; ARG-147; ARG-154 AND ARG-158.
RX PubMed=26081071; DOI=10.1002/pmic.201500075;
RA Yagoub D., Hart-Smith G., Moecking J., Erce M.A., Wilkins M.R.;
RT "Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively
RT methylated and are substrates of the arginine methyltransferase Hmt1p.";
RL Proteomics 15:3209-3218(2015).
RN [15]
RP METHYLATION AT ARG-147.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [16]
RP METHYLATION AT ARG-4; ARG-8; ARG-11; ARG-15; ARG-19; ARG-147; ARG-154;
RP ARG-158; ARG-162; ARG-165; ARG-171; ARG-174; ARG-180; ARG-184; ARG-189;
RP ARG-193; ARG-197 AND ARG-201.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 32-124 IN A COMPLEX WITH CBF5;
RP NOP10 AND SHQ1.
RX PubMed=22117216; DOI=10.1038/emboj.2011.427;
RA Li S., Duan J., Li D., Ma S., Ye K.;
RT "Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA
RT RNP biogenesis and dyskeratosis congenita.";
RL EMBO J. 30:5010-5020(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-124 IN A COMPLEX WITH CBF5 AND
RP NOP10.
RX PubMed=22085967; DOI=10.1101/gad.175299.111;
RA Li S., Duan J., Li D., Yang B., Dong M., Ye K.;
RT "Reconstitution and structural analysis of the yeast box H/ACA RNA-guided
RT pseudouridine synthase.";
RL Genes Dev. 25:2409-2421(2011).
CC -!- FUNCTION: Non-catalytic component of the H/ACA small nucleolar
CC ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of
CC rRNA and is required for ribosome biogenesis (PubMed:9303321,
CC PubMed:9843512). This involves the isomerization of uridine such that
CC the ribose is subsequently attached to C5, instead of the normal N1
CC (PubMed:9303321, PubMed:9843512). Pseudouridine ('psi') residues may
CC serve to stabilize the conformation of rRNAs (PubMed:9843512). The
CC H/ACA snoRNP complex also mediates pseudouridylation of other types of
CC RNAs (PubMed:21131909). The H/ACA snoRNP complex mediates
CC pseudouridylation at position 93 in U2 snRNA (PubMed:21131909).
CC Essential for growth (PubMed:9303321). {ECO:0000269|PubMed:21131909,
CC ECO:0000269|PubMed:9843512}.
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs) (PubMed:9556561,
CC PubMed:9843512, PubMed:21131909). The protein component of the H/ACA
CC snoRNP contains CBF5, GAR1, NHP2 and NOP10 (PubMed:9556561,
CC PubMed:9843512, PubMed:21131909). The complex contains a stable core
CC composed of CBF5 and NOP10, to which GAR1 and NHP2 subsequently bind.
CC Interacts with snoRNAs (PubMed:9556561, PubMed:9843512).
CC {ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:9556561,
CC ECO:0000269|PubMed:9843512}.
CC -!- INTERACTION:
CC P28007; P32495: NHP2; NbExp=3; IntAct=EBI-7321, EBI-12014;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12756332,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9843512}.
CC -!- PTM: Methylated by HMT1, forming asymmetric dimethylarginines (DMA)
CC within a domain referred to as an RGG box, made up of repeated Gly-Gly
CC dipeptides interspersed with Arg and aromatic residues.
CC {ECO:0000269|PubMed:12756332}.
CC -!- MISCELLANEOUS: Present with 5730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GAR1 family. {ECO:0000305}.
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DR EMBL; X63617; CAA45162.1; -; Genomic_DNA.
DR EMBL; U00060; AAB68929.1; -; Genomic_DNA.
DR EMBL; AY558284; AAS56610.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06785.1; -; Genomic_DNA.
DR PIR; S19634; S19634.
DR RefSeq; NP_011957.1; NM_001179219.1.
DR PDB; 3U28; X-ray; 1.90 A; C=32-124.
DR PDB; 3UAI; X-ray; 3.06 A; C=32-124.
DR PDBsum; 3U28; -.
DR PDBsum; 3UAI; -.
DR AlphaFoldDB; P28007; -.
DR SMR; P28007; -.
DR BioGRID; 36524; 231.
DR ComplexPortal; CPX-737; Box H/ACA ribonucleoprotein complex.
DR DIP; DIP-4484N; -.
DR IntAct; P28007; 83.
DR MINT; P28007; -.
DR STRING; 4932.YHR089C; -.
DR iPTMnet; P28007; -.
DR MaxQB; P28007; -.
DR PaxDb; P28007; -.
DR PRIDE; P28007; -.
DR EnsemblFungi; YHR089C_mRNA; YHR089C; YHR089C.
DR GeneID; 856489; -.
DR KEGG; sce:YHR089C; -.
DR SGD; S000001131; GAR1.
DR VEuPathDB; FungiDB:YHR089C; -.
DR eggNOG; KOG3262; Eukaryota.
DR GeneTree; ENSGT00730000111223; -.
DR HOGENOM; CLU_080002_1_0_1; -.
DR InParanoid; P28007; -.
DR OMA; HSCEGEM; -.
DR BioCyc; MetaCyc:G3O-31136-MON; -.
DR BioCyc; YEAST:G3O-31136-MON; -.
DR PRO; PR:P28007; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P28007; protein.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IPI:SGD.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IDA:ComplexPortal.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IDA:UniProtKB.
DR Gene3D; 2.40.10.230; -; 1.
DR InterPro; IPR038664; Gar1/Naf1_Cbf5-bd_sf.
DR InterPro; IPR007504; H/ACA_rnp_Gar1/Naf1.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF04410; Gar1; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Methylation; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; Ribosome biogenesis; RNA-binding;
KW rRNA processing; Ubl conjugation.
FT CHAIN 1..205
FT /note="H/ACA ribonucleoprotein complex subunit GAR1"
FT /id="PRO_0000208566"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4..21
FT /note="RGG-box 1"
FT REGION 124..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..205
FT /note="RGG-box 2"
FT MOD_RES 4
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 8
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 8
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 11
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 15
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 15
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071"
FT MOD_RES 19
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 147
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071"
FT MOD_RES 147
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 154
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 154
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 158
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 158
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:26081071,
FT ECO:0000269|PubMed:33856219, ECO:0000305|PubMed:12756332"
FT MOD_RES 162
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 165
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 165
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 171
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 174
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 180
FT /note="Omega-N-methylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 184
FT /note="Omega-N-methylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 189
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 189
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 193
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 197
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT MOD_RES 201
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0000305|PubMed:12756332"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3U28"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3U28"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3U28"
SQ SEQUENCE 205 AA; 21480 MW; C197FE85644DD0F8 CRC64;
MSFRGGNRGG RGGFRGGFRG GRTGSARSFQ QGPPDTVLEM GAFLHPCEGD IVCRSINTKI
PYFNAPIYLE NKTQVGKVDE ILGPLNEVFF TIKCGDGVQA TSFKEGDKFY IAADKLLPIE
RFLPKPKVVG PPKPKNKKKR SGAPGGRGGA SMGRGGSRGG FRGGRGGSSF RGGRGGSSFR
GGSRGGSFRG GSRGGSRGGF RGGRR
