PUF2_YEAST
ID PUF2_YEAST Reviewed; 1075 AA.
AC Q12221; D6W451; Q02573; Q04142; Q7LH42; Q7LH98;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=mRNA-binding protein PUF2;
DE AltName: Full=Pumilio homology domain family member 2;
GN Name=PUF2; OrderedLocusNames=YPR042C; ORFNames=YP3085.06c, YP9499.01;
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 46191 / IL125-2B;
RX PubMed=9730282;
RX DOI=10.1002/(sici)1097-0061(199808)14:11<1027::aid-yea295>3.0.co;2-s;
RA Waskiewicz-Staniorowska B., Skala J., Jasinski M., Grenson M., Goffeau A.,
RA Ulaszewski S.;
RT "Functional analysis of three adjacent open reading frames from the right
RT arm of yeast chromosome XVI.";
RL Yeast 14:1027-1039(1998).
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 FUNCTION, AND RNA-BINDING.
RX PubMed=11101532; DOI=10.1093/emboj/19.23.6602;
RA Olivas W.M., Parker R.;
RT "The Puf3 protein is a transcript-specific regulator of mRNA degradation in
RT yeast.";
RL EMBO J. 19:6602-6611(2000).
RN [5]
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 [6]
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 [7]
RP RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=15024427; DOI=10.1371/journal.pbio.0020079;
RA Gerber A.P., Herschlag D., Brown P.O.;
RT "Extensive association of functionally and cytotopically related mRNAs with
RT Puf family RNA-binding proteins in yeast.";
RL PLoS Biol. 2:342-354(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
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 [10]
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-198; SER-872 AND
RP SER-876, AND 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).
CC -!- FUNCTION: RNA-binding protein involved in post-transcriptional
CC regulation. Negatively regulates expression of COX17 by binding to the
CC 3'-UTR of COX17 mRNA. Promotes decay of COX17 mRNA by enhancing its
CC rate of deadenylation and subsequent turnover. Predominantly binds to
CC mRNAs encoding membrane-associated proteins with roles in transmembrane
CC transport and vesicular trafficking. {ECO:0000269|PubMed:11101532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15024427}. Note=Localizes to foci enriched near the
CC periphery of the cell.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z73616; CAA97992.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94990.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89163.1; -; Genomic_DNA.
DR EMBL; Z68111; CAA92146.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11467.1; -; Genomic_DNA.
DR PIR; S54067; S54067.
DR RefSeq; NP_015367.1; NM_001184139.1.
DR AlphaFoldDB; Q12221; -.
DR SMR; Q12221; -.
DR BioGRID; 36219; 1284.
DR IntAct; Q12221; 9.
DR MINT; Q12221; -.
DR STRING; 4932.YPR042C; -.
DR iPTMnet; Q12221; -.
DR MaxQB; Q12221; -.
DR PaxDb; Q12221; -.
DR PRIDE; Q12221; -.
DR EnsemblFungi; YPR042C_mRNA; YPR042C; YPR042C.
DR GeneID; 856155; -.
DR KEGG; sce:YPR042C; -.
DR SGD; S000006246; PUF2.
DR VEuPathDB; FungiDB:YPR042C; -.
DR eggNOG; KOG4574; Eukaryota.
DR GeneTree; ENSGT00940000176457; -.
DR HOGENOM; CLU_009728_0_0_1; -.
DR InParanoid; Q12221; -.
DR OMA; INWITAN; -.
DR BioCyc; YEAST:G3O-34198-MON; -.
DR PRO; PR:Q12221; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12221; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00806; PUF; 3.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00025; Pumilio; 6.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50302; PUM; 5.
DR PROSITE; PS50303; PUM_HD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1075
FT /note="mRNA-binding protein PUF2"
FT /id="PRO_0000262754"
FT DOMAIN 316..402
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 511..872
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 574..611
FT /note="Pumilio 1"
FT REPEAT 612..647
FT /note="Pumilio 2"
FT REPEAT 649..683
FT /note="Pumilio 3"
FT REPEAT 684..719
FT /note="Pumilio 4"
FT REPEAT 722..758
FT /note="Pumilio 5"
FT REPEAT 760..800
FT /note="Pumilio 6"
FT REGION 38..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1075 AA; 119508 MW; CD3E4D5FE9B2F47D CRC64;
MDNKRLYNGN LSNIPEVIDP GITIPIYEED IRNDTRMNTN ARSVRVSDKR GRSSSTSPQK
IGSYRTRAGR FSDTLTNLLP SISAKLHHSK KSTPVVVVPP TSSTPDSLNS TTYAPRVSSD
SFTVATPLSL QSTTTRTRTR NNTVSSQITA SSSLTTDVGN ATSANIWSAN AESNTSSSPL
FDYPLATSYF EPLTRFKSTD NYTLPQTAQL NSFLEKNGNP NIWSSAGNSN TDHLNTPIVN
RQRSQSQSTT NRVYTDAPYY QQPAQNYQVQ VPPRVPKSTS ISPVILDDVD PASINWITAN
QKVPLVNQIS ALLPTNTISI SNVFPLQPTQ QHQQNAVNLT STSLATLCSQ YGKVLSARTL
RGLNMALVEF STVESAICAL EALQGKELSK VGAPSTVSFA RVLPMYEQPL NVNGFNNTPK
QPLLQEQLNH GVLNYQLQQS LQQPELQQQP TSFNQPNLTY CNPTQNLSHL QLSSNENEPY
PFPLPPPSLS DSKKDILHTI SSFKLEYDHL ELNHLLQNAL KNKGVSDTNY FGPLPEHNSK
VPKRKDTFDA PKLRELRKQF DSNSLSTIEM EQLAIVMLDQ LPELSSDYLG NTVIQKLFEN
SSNIIRDIML RKCNKYLTSM GVHKNGTWVC QKIIKMANTP RQINLVTSGV SDYCTPLFND
QFGNYVIQGI LKFGFPWNSF IFESVLSHFW TIVQNRYGSR AVRACLEADS IITQCQLLTI
TSLIIVLSPY LATDTNGTLL ITWLLDTCTL PNKNLILCDK LVNKNLVKLC CHKLGSLTVL
KILNLRGGEE EALSKNKIIH AIFDGPISSD SILFQILDEG NYGPTFIYKV LTSRILDNSV
RDEAITKIRQ LILNSNINLQ SRQLLEEVGL SSAGISPKQS SKNHRKQHPQ GFHSPGRARG
VSVSSVRSSN SRHNSVIQMN NAGPTPALNF NPAPMSEINS YFNNQQVVYS GNQNQNQNGN
SNGLDELNSQ FDSFRIANGT NLSLPIVNLP NVSNNNNNYN NSGYSSQMNP LSRSVSHNNN
NNTNNYNNND NDNNNNNNNN NNNNNNNNNN NNNSNNSNNN NNNDTSLYRY RSYGY
