SCD6_YEAST
ID SCD6_YEAST Reviewed; 349 AA.
AC P45978; D6W4C6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein SCD6 {ECO:0000305};
DE AltName: Full=Suppressor of clathrin deficiency protein 6 {ECO:0000303|Ref.1};
GN Name=SCD6 {ECO:0000303|Ref.1}; OrderedLocusNames=YPR129W;
GN ORFNames=P9659.10;
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=ATCC 204508 / S288c;
RA Lemmon S.K., Otsuka M., Gelperin D.M.;
RT "SCD6, a multicopy suppressor of clathrin deficiency, encodes a novel
RT protein with homologues in humans, C.elegans and plants.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22284680; DOI=10.1016/j.molcel.2011.11.026;
RA Rajyaguru P., She M., Parker R.;
RT "Scd6 targets eIF4G to repress translation: RGG motif proteins as a class
RT of eIF4G-binding proteins.";
RL Mol. Cell 45:244-254(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP METHYLATION AT ARG-288; ARG-294; ARG-298; ARG-306 AND ARG-310.
RX PubMed=27613419; DOI=10.1093/nar/gkw762;
RA Poornima G., Shah S., Vignesh V., Parker R., Rajyaguru P.I.;
RT "Arginine methylation promotes translation repression activity of eIF4G-
RT binding protein, Scd6.";
RL Nucleic Acids Res. 44:9358-9368(2016).
RN [9]
RP METHYLATION AT ARG-310, AND PHOSPHORYLATION AT THR-139.
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).
CC -!- FUNCTION: Involved in regulation of translation and mRNA degradation.
CC Represses translation by binding the eIF4G subunit (TIF4631 or TIF4632)
CC of the eIF4F complex dependent on its RGG domain, forming an mRNP
CC repressed for translation initiation. {ECO:0000269|PubMed:22284680}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:22284680}.
CC Cytoplasm, Stress granule {ECO:0000269|PubMed:22284680}.
CC -!- MISCELLANEOUS: Present with 1280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U30384; AAA74093.1; -; Genomic_DNA.
DR EMBL; U40829; AAB68271.1; -; Genomic_DNA.
DR EMBL; AY693234; AAT93253.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11542.1; -; Genomic_DNA.
DR PIR; S59743; S59743.
DR RefSeq; NP_015454.1; NM_001184226.1.
DR AlphaFoldDB; P45978; -.
DR SMR; P45978; -.
DR BioGRID; 36296; 187.
DR IntAct; P45978; 8.
DR MINT; P45978; -.
DR STRING; 4932.YPR129W; -.
DR iPTMnet; P45978; -.
DR MaxQB; P45978; -.
DR PaxDb; P45978; -.
DR PRIDE; P45978; -.
DR EnsemblFungi; YPR129W_mRNA; YPR129W; YPR129W.
DR GeneID; 856247; -.
DR KEGG; sce:YPR129W; -.
DR SGD; S000006333; SCD6.
DR VEuPathDB; FungiDB:YPR129W; -.
DR eggNOG; KOG1073; Eukaryota.
DR GeneTree; ENSGT00940000168901; -.
DR HOGENOM; CLU_019221_2_1_1; -.
DR InParanoid; P45978; -.
DR OMA; HPRWSPY; -.
DR BioCyc; YEAST:G3O-34266-MON; -.
DR PRO; PR:P45978; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P45978; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:SGD.
DR GO; GO:0033962; P:P-body assembly; IMP:SGD.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR CDD; cd01736; LSm14_N; 1.
DR InterPro; IPR025762; DFDF.
DR InterPro; IPR019050; FDF_dom.
DR InterPro; IPR025761; FFD_box.
DR InterPro; IPR025609; Lsm14-like_N.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR025768; TFG_box.
DR Pfam; PF12701; LSM14; 1.
DR SMART; SM01199; FDF; 1.
DR SMART; SM01271; LSM14; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51513; FFD; 1.
DR PROSITE; PS51536; TFG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Methylation; Phosphoprotein; Reference proteome;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..349
FT /note="Protein SCD6"
FT /id="PRO_0000097622"
FT DOMAIN 193..229
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 89..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 241..257
FT /note="FFD box"
FT MOTIF 260..280
FT /note="TFG box"
FT COMPBIAS 102..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 288
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:27613419"
FT MOD_RES 294
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:27613419"
FT MOD_RES 298
FT /note="Asymmetric dimethylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:27613419"
FT MOD_RES 306
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:27613419"
FT MOD_RES 306
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:27613419"
FT MOD_RES 310
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:27613419"
FT MOD_RES 310
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:27613419,
FT ECO:0000269|PubMed:33856219"
SQ SEQUENCE 349 AA; 39190 MW; 6EE7965858EB36F6 CRC64;
MSQYIGKTIS LISVTDNRYV GLLEDIDSEK GTVTLKEVRC FGTEGRKNWG PEEIYPNPTV
YNSVKFNGSE VKDLSILDAN INDIQPVVPQ MMPPASQFPP QQAQSPPQAQ AQAHVQTNPQ
VPKPESNVPA AVAGYGVYTP TSTETATASM NDKSTPQDTN VNSQSRERGK NGENEPKYQR
NKNRSSNRPP QSNRNFKVDI PNEDFDFQSN NAKFTKGDST DVEKEKELES AVHKQDESDE
QFYNKKSSFF DTISTSTETN TNMRWQEEKM LNVDTFGQAS ARPRFHSRGL GRGRGNYRGN
RGNRGRGGQR GNYQNRNNYQ NDSGAYQNQN DSYSRPANQF SQPPSNVEF
