PUF6_YEAST
ID PUF6_YEAST Reviewed; 656 AA.
AC Q04373; D6VTB8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Pumilio homology domain family member 6;
GN Name=PUF6; OrderedLocusNames=YDR496C; ORFNames=D9719.2;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [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, SUBUNIT, INTERACTION WITH SHE2, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15198983; DOI=10.1101/gad.1189004;
RA Gu W., Deng Y., Zenklusen D., Singer R.H.;
RT "A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and
RT is required for its localization.";
RL Genes Dev. 18:1452-1465(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-35, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP FUNCTION.
RX PubMed=18413716; DOI=10.1101/gad.1611308;
RA Deng Y., Singer R.H., Gu W.;
RT "Translation of ASH1 mRNA is repressed by Puf6p-Fun12p/eIF5B interaction
RT and released by CK2 phosphorylation.";
RL Genes Dev. 22:1037-1050(2008).
RN [9]
RP FUNCTION, INTERACTION WITH FUN12, PHOSPHORYLATION AT SER-31; SER-34 AND
RP SER-35, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-31;
RP SER-34 AND SER-35.
RX PubMed=18791219; DOI=10.1534/genetics.108.095737;
RA Zheng W., Finkel J.S., Landers S.M., Long R.M., Culbertson M.R.;
RT "Nonsense-mediated decay of ash1 nonsense transcripts in Saccharomyces
RT cerevisiae.";
RL Genetics 180:1391-1405(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-35, 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 [11]
RP INTERACTION WITH SHE2.
RX PubMed=19244342; DOI=10.1091/mbc.e08-11-1151;
RA Shen Z., Paquin N., Forget A., Chartrand P.;
RT "Nuclear shuttling of She2p couples ASH1 mRNA localization to its
RT translational repression by recruiting Loc1p and Puf6p.";
RL Mol. Biol. Cell 20:2265-2275(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-35, AND
RP IDENTIFICATION BY 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 [13]
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).
CC -!- FUNCTION: RNA-binding protein involved in post-transcriptional
CC regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA
CC to the distal tip of the bud, where the ASH1 protein is translated and
CC targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR
CC containing the PUF consensus UUGU segment and represses its
CC translation. This silencing of ASH1 mRNA is critical for asymmetric
CC seggregation of ASH1 to the daughter cell nucleus.
CC {ECO:0000269|PubMed:15198983, ECO:0000269|PubMed:18413716,
CC ECO:0000269|PubMed:18791219}.
CC -!- SUBUNIT: Component of the ASH1 mRNP composed of at least PUF6, SHE2,
CC SHE3, SHE1 and the ASH1 mRNA. Interacts with SHE2 and FUN12.
CC {ECO:0000269|PubMed:15198983, ECO:0000269|PubMed:18791219,
CC ECO:0000269|PubMed:19244342}.
CC -!- INTERACTION:
CC Q04373; P36068: SHE2; NbExp=2; IntAct=EBI-33208, EBI-26866;
CC -!- SUBCELLULAR LOCATION: Bud tip. Nucleus, nucleolus.
CC -!- PTM: phosphorylation by CK2 relieves translational repression activity.
CC {ECO:0000269|PubMed:18791219}.
CC -!- MISCELLANEOUS: Present with 21500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PUF6 family. {ECO:0000305}.
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DR EMBL; U33057; AAB64938.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12328.1; -; Genomic_DNA.
DR PIR; S69554; S69554.
DR RefSeq; NP_010784.1; NM_001180804.1.
DR AlphaFoldDB; Q04373; -.
DR SMR; Q04373; -.
DR BioGRID; 32547; 368.
DR DIP; DIP-6579N; -.
DR IntAct; Q04373; 69.
DR MINT; Q04373; -.
DR STRING; 4932.YDR496C; -.
DR iPTMnet; Q04373; -.
DR MaxQB; Q04373; -.
DR PaxDb; Q04373; -.
DR PRIDE; Q04373; -.
DR EnsemblFungi; YDR496C_mRNA; YDR496C; YDR496C.
DR GeneID; 852107; -.
DR KEGG; sce:YDR496C; -.
DR SGD; S000002904; PUF6.
DR VEuPathDB; FungiDB:YDR496C; -.
DR eggNOG; KOG2050; Eukaryota.
DR GeneTree; ENSGT00390000015757; -.
DR HOGENOM; CLU_013994_1_0_1; -.
DR InParanoid; Q04373; -.
DR OMA; WILDDVY; -.
DR BioCyc; YEAST:G3O-30019-MON; -.
DR PRO; PR:Q04373; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04373; protein.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0101031; C:chaperone complex; IMP:SGD.
DR GO; GO:0015934; C:large ribosomal subunit; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:SGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:SGD.
DR GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012959; CPL_dom.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR040059; PUM3.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR PANTHER; PTHR13389; PTHR13389; 1.
DR Pfam; PF08144; CPL; 1.
DR SMART; SM00025; Pumilio; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 5.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW RNA-binding; Translation regulation; Transport.
FT CHAIN 1..656
FT /note="Pumilio homology domain family member 6"
FT /id="PRO_0000075926"
FT DOMAIN 133..483
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 155..191
FT /note="Pumilio 1"
FT REPEAT 192..227
FT /note="Pumilio 2"
FT REPEAT 228..264
FT /note="Pumilio 3"
FT REPEAT 340..376
FT /note="Pumilio 4"
FT REPEAT 377..413
FT /note="Pumilio 5"
FT REPEAT 415..450
FT /note="Pumilio 6"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:18791219"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18791219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 34
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:18791219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18791219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 35
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:18791219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 31
FT /note="S->A: Increases translation repression of ASH1
FT mRNA."
FT /evidence="ECO:0000269|PubMed:18791219"
FT MUTAGEN 34
FT /note="S->A: Increases translation repression of ASH1
FT mRNA."
FT /evidence="ECO:0000269|PubMed:18791219"
FT MUTAGEN 35
FT /note="S->A: Increases translation repression of ASH1
FT mRNA."
FT /evidence="ECO:0000269|PubMed:18791219"
SQ SEQUENCE 656 AA; 75106 MW; 4D172E8854326ECF CRC64;
MAPLTKKTNG KRSAKEVSHS EKKLAKKPRI SIDSSDEESE LSKKEDAVSS SSDDDDLDDL
STSDSEAEEE ADELDISDDS EEHENENEEK EGKDKSEGGE NGNHTEQRKL LKERKMQRKS
GTQVQQIKSV WERLRVKTPP LPKQIREKLS NEIWELSKDC ISDLVLKHDA SRIVQTLVKY
SSKDRREQIV DALKGKFYVL ATSAYGKYLL VKLLHYGSRS SRQTIINELH GSLRKLMRHR
EGAYVVEDLF VLYATHEQRQ QMIKEFWGSE YAVFRETHKD LTIEKVCESS IEKRNIIARN
LIGTITASVE KGSTGFQILH AAMREYVKIA NEKEISEMIE LLHEQFAELV HTPEGSDVAC
TLVARANAKE RKLILKALKN HAEKLIKNEY GNIVFITILN CVDDTVLVFK TFSPTVKEHL
QEFIIDKFGR RPWLYILLGL DGKYFSPIVK NELLRYIELS KATSKKDPLQ RRHELLSKFA
PMFLSTISKD YSSILTENLG CQFIAEVLIN DELYAQLNEK DQEKYQQVLN NILTTFKGDI
TEEEHPIHRA FSTRLLKALI QGGKWNNKEK KVIPLKNVQG LGVPFAEKLY DEIIDSSNLL
EWINNADSSF TIVALYETLK DQKEGKPFLK DLRGVQSKIT TDESNKGSQL LAKLLK
