SRO9_YEAST
ID SRO9_YEAST Reviewed; 434 AA.
AC P25567; D6VQX8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=RNA-binding protein SRO9;
DE AltName: Full=Suppressor of RHO3 protein 9;
GN Name=SRO9; OrderedLocusNames=YCL037C; ORFNames=YCL37C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 PROTEIN SEQUENCE OF 24-44; 43-65; 137-157; 192-219; 227-248 AND 342-364,
RP FUNCTION, IDENTIFICATION IN HMC COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11689685; DOI=10.1128/mcb.21.23.7923-7932.2001;
RA Hon T., Lee H.C., Hach A., Johnson J.L., Craig E.A., Erdjument-Bromage H.,
RA Tempst P., Zhang L.;
RT "The Hsp70-Ydj1 molecular chaperone represses the activity of the heme
RT activator protein Hap1 in the absence of heme.";
RL Mol. Cell. Biol. 21:7923-7932(2001).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9383048; DOI=10.1093/genetics/147.3.1003;
RA Kagami M., Toh-e A., Matsui Y.;
RT "SRO9, a multicopy suppressor of the bud growth defect in the Saccharomyces
RT cerevisiae RHO3-deficient cells, shows strong genetic interactions with
RT tropomyosin genes, suggesting its role in organization of the actin
RT cytoskeleton.";
RL Genetics 147:1003-1016(1997).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10564276; DOI=10.1091/mbc.10.11.3849;
RA Sobel S.G., Wolin S.L.;
RT "Two yeast La motif-containing proteins are RNA-binding proteins that
RT associate with polyribosomes.";
RL Mol. Biol. Cell 10:3849-3862(1999).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-422, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-156; LYS-301; LYS-342 AND
RP LYS-352, AND IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: May overlap in function with tropomyosin and may be involved
CC in organization of actin filaments. Acts as a multicopy suppressor of
CC RHO3 mutation. RNA-binding protein which may modulate mRNA translation.
CC Involved in heme regulation of HAP1, as a component of the high-
CC molecular-weight complex (HMC). {ECO:0000269|PubMed:10564276,
CC ECO:0000269|PubMed:11689685}.
CC -!- SUBUNIT: Interacts with HAP1. Component of the HMC including HAP1, SRO9
CC and YDJ1. {ECO:0000269|PubMed:11689685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10564276,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9383048}.
CC Note=Associates with translating ribosome.
CC -!- MISCELLANEOUS: Present with 8430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42379.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X59720; CAA42379.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006937; DAA07447.1; -; Genomic_DNA.
DR PIR; S19365; S19365.
DR RefSeq; NP_009893.2; NM_001178682.1.
DR AlphaFoldDB; P25567; -.
DR BioGRID; 30946; 968.
DR ComplexPortal; CPX-1276; HMC complex.
DR ComplexPortal; CPX-1882; HAP1 transcriptional repressor complex, SSA1 variant.
DR ComplexPortal; CPX-1883; HAP1 transcriptional repressor complex, SSA2 variant.
DR DIP; DIP-6638N; -.
DR IntAct; P25567; 56.
DR MINT; P25567; -.
DR STRING; 4932.YCL037C; -.
DR iPTMnet; P25567; -.
DR MaxQB; P25567; -.
DR PaxDb; P25567; -.
DR PRIDE; P25567; -.
DR EnsemblFungi; YCL037C_mRNA; YCL037C; YCL037C.
DR GeneID; 850320; -.
DR KEGG; sce:YCL037C; -.
DR SGD; S000000542; SRO9.
DR VEuPathDB; FungiDB:YCL037C; -.
DR eggNOG; KOG2590; Eukaryota.
DR GeneTree; ENSGT00940000176708; -.
DR HOGENOM; CLU_039873_0_0_1; -.
DR InParanoid; P25567; -.
DR OMA; YRIVNMS; -.
DR BioCyc; YEAST:G3O-29296-MON; -.
DR PRO; PR:P25567; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25567; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; IC:ComplexPortal.
DR GO; GO:0097322; F:7SK snRNA binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IMP:SGD.
DR GO; GO:0070482; P:response to oxygen levels; IC:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..434
FT /note="RNA-binding protein SRO9"
FT /id="PRO_0000207615"
FT DOMAIN 255..351
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 1..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..190
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 434 AA; 48060 MW; B1B720D40C7B9914 CRC64;
MSAETAAANT ATAPVPEVQE QESSKSKQVN LTPAPLPTSS PWKLAPTEIP VSTISIEDLD
ATRKKKNRTP TPKSSTATKW VPIKASITVS GTKRSGSKNG ASNGNSNKSK NNKTAASSTS
SSNANRKKKH HQHNAKKQQQ MKKDGFESAV GEEDSKDATS QENGQSTQQQ QPPHHRNHHH
SHHHNSNGPQ RRKFHNSNNA GMPQNQGFPP QFKPYQGRNA RNNNNNRSKY HNHFHHNQQH
PQQPMVKLQQ QFYPVQPVLM AINNIARQIE YYFSEENLTV DNYLRSKLSK DGFAPLSLIS
KFYRVVNMSF GGDTNLILAA LREIVANEAA TVNVAEGTLA AKEGDNVTGE AKEPSPLDKY
FVRSKSWSNW LPETFETEIN IEKELVGDAL DQFMISLPPV PQQEEESSTE LASQEQETKE
DSAPVAAGES ESSL
