PUF4_YEAST
ID PUF4_YEAST Reviewed; 888 AA.
AC P25339; D6VUC3;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Pumilio homology domain family member 4;
GN Name=PUF4; OrderedLocusNames=YGL014W; ORFNames=YGL023;
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=1909073; DOI=10.1002/yea.320070314;
RA Chen W., Balzi E., Capieaux E., Goffeau A.;
RT "The YGL023 gene encodes a putative regulatory protein.";
RL Yeast 7:309-312(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 46191 / IL125-2B;
RX PubMed=1882553; DOI=10.1002/yea.320070311;
RA Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.;
RT "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and
RT ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6
RT gene, a new member of the genetic network controlling pleiotropic drug
RT resistance.";
RL Yeast 7:287-299(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-212, 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=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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; THR-252 AND SER-256, 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).
CC -!- FUNCTION: Is not essential for haploid growth, but may affect diploid
CC formation.
CC -!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; S57889; AAB19616.1; -; Genomic_DNA.
DR EMBL; S58126; AAD13898.1; -; Genomic_DNA.
DR EMBL; Z72536; CAA96714.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08084.1; -; Genomic_DNA.
DR PIR; S64016; S64016.
DR RefSeq; NP_011501.1; NM_001180879.1.
DR PDB; 3BWT; X-ray; 2.69 A; A=554-886.
DR PDB; 3BX2; X-ray; 2.84 A; A/B=554-888.
DR PDB; 3BX3; X-ray; 3.00 A; A/B=554-888.
DR PDB; 4DZS; X-ray; 3.14 A; A/B=536-888.
DR PDBsum; 3BWT; -.
DR PDBsum; 3BX2; -.
DR PDBsum; 3BX3; -.
DR PDBsum; 4DZS; -.
DR AlphaFoldDB; P25339; -.
DR SMR; P25339; -.
DR BioGRID; 33232; 687.
DR DIP; DIP-2638N; -.
DR IntAct; P25339; 18.
DR MINT; P25339; -.
DR STRING; 4932.YGL014W; -.
DR iPTMnet; P25339; -.
DR MaxQB; P25339; -.
DR PaxDb; P25339; -.
DR PRIDE; P25339; -.
DR EnsemblFungi; YGL014W_mRNA; YGL014W; YGL014W.
DR GeneID; 852870; -.
DR KEGG; sce:YGL014W; -.
DR SGD; S000002982; PUF4.
DR VEuPathDB; FungiDB:YGL014W; -.
DR eggNOG; KOG2049; Eukaryota.
DR HOGENOM; CLU_016143_0_0_1; -.
DR InParanoid; P25339; -.
DR OMA; FRRQTFH; -.
DR BioCyc; YEAST:G3O-30535-MON; -.
DR EvolutionaryTrace; P25339; -.
DR PRO; PR:P25339; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P25339; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:SGD.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..888
FT /note="Pumilio homology domain family member 4"
FT /id="PRO_0000075925"
FT DOMAIN 539..888
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 563..598
FT /note="Pumilio 1"
FT REPEAT 599..634
FT /note="Pumilio 2"
FT REPEAT 635..671
FT /note="Pumilio 3"
FT REPEAT 672..707
FT /note="Pumilio 4"
FT REPEAT 708..743
FT /note="Pumilio 5"
FT REPEAT 744..783
FT /note="Pumilio 6"
FT REPEAT 784..821
FT /note="Pumilio 7"
FT REPEAT 823..861
FT /note="Pumilio 8"
FT REGION 236..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 595
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT TURN 555..558
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:3BWT"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:3BWT"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:4DZS"
FT HELIX 575..587
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 590..600
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 604..608
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 613..623
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 626..636
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 640..645
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 649..659
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 663..673
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 677..681
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 686..696
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 699..711
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 713..717
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 722..732
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 735..746
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 749..753
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 758..772
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 777..785
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 789..793
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 798..806
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 809..821
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 824..832
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 837..851
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 853..863
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 864..866
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 869..873
FT /evidence="ECO:0007829|PDB:3BWT"
FT HELIX 875..881
FT /evidence="ECO:0007829|PDB:3BWT"
FT STRAND 883..885
FT /evidence="ECO:0007829|PDB:4DZS"
SQ SEQUENCE 888 AA; 97798 MW; 659BA1062439F642 CRC64;
MSTKGLKEEI DDVPSVDPVV SETVNSALEQ LQLDDPEENA TSNAFANKVS QDSQFANGPP
SQMFPHPQMM GGMGFMPYSQ MMQVPHNPCP FFPPPDFNDP TAPLSSSPLN AGGPPMLFKN
DSLPFQMLSS GAAVATQGGQ NLNPLINDNS MKVLPIASAD PLWTHSNVPG SASVAIEETT
ATLQESLPSK GRESNNKASS FRRQTFHALS PTDLINAANN VTLSKDFQSD MQNFSKAKKP
SVGANNTAKT RTQSISFDNT PSSTSFIPPT NSVSEKLSDF KIETSKEDLI NKTAPAKKES
PTTYGAAYPY GGPLLQPNPI MPGHPHNISS PIYGIRSPFP NSYEMGAQFQ PFSPILNPTS
HSLNANSPIP LTQSPIHLAP VLNPSSNSVA FSDMKNDGGK PTTDNDKAGP NVRMDLINPN
LGPSMQPFHI LPPQQNTPPP PWLYSTPPPF NAMVPPHLLA QNHMPLMNSA NNKHHGRNNN
SMSSHNDNDN IGNSNYNNKD TGRSNVGKMK NMKNSYHGYY NNNNNNNNNN NNNNNSNATN
SNSAEKQRKI EESSRFADAV LDQYIGSIHS LCKDQHGCRF LQKQLDILGS KAADAIFEET
KDYTVELMTD SFGNYLIQKL LEEVTTEQRI VLTKISSPHF VEISLNPHGT RALQKLIECI
KTDEEAQIVV DSLRPYTVQL SKDLNGNHVI QKCLQRLKPE NFQFIFDAIS DSCIDIATHR
HGCCVLQRCL DHGTTEQCDN LCDKLLALVD KLTLDPFGNY VVQYIITKEA EKNKYDYTHK
IVHLLKPRAI ELSIHKFGSN VIEKILKTAI VSEPMILEIL NNGGETGIQS LLNDSYGNYV
LQTALDISHK QNDYLYKRLS EIVAPLLVGP IRNTPHGKRI IGMLHLDS
