MPT5_YEAST
ID MPT5_YEAST Reviewed; 859 AA.
AC P39016; D6VTX5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Suppressor protein MPT5;
DE AltName: Full=Protein HTR1;
DE AltName: Full=Pumilio homology domain family member 5;
GN Name=MPT5; Synonyms=HTR1, PUF5; OrderedLocusNames=YGL178W; ORFNames=BIC834;
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 96604 / S288c / FY1679;
RX PubMed=7668046; DOI=10.1002/yea.320110808;
RA Coglievina M., Bertani I., Klima R., Zaccaria P., Bruschi C.V.;
RT "The DNA sequence of a 7941 bp fragment of the left arm of chromosome VII
RT of Saccharomyces cerevisiae contains four open reading frames including the
RT multicopy suppressor gene of the pop2 mutation and a putative
RT serine/threonine protein kinase gene.";
RL Yeast 11:767-774(1995).
RN [2]
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 [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] OF 2-859.
RC STRAIN=ATCC 70391;
RX PubMed=7845352; DOI=10.1007/bf00279756;
RA Kikuchi Y., Oka Y., Kobayashi M., Uesono Y., Toh-e A., Kikuchi A.;
RT "A new yeast gene, HTR1, required for growth at high temperature, is needed
RT for recovery from mating pheromone-induced G1 arrest.";
RL Mol. Gen. Genet. 245:107-116(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-859.
RC STRAIN=ATCC 204508 / S288c;
RA Sakai A.;
RT "Multicopy suppressors of the yeast pop2 mutation.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION OF INTRON.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
RN [7]
RP FUNCTION.
RX PubMed=11157761; DOI=10.1093/emboj/20.3.552;
RA Tadauchi T., Matsumoto K., Herskowitz I., Irie K.;
RT "Post-transcriptional regulation through the HO 3'-UTR by Mpt5, a yeast
RT homolog of Pumilio and FBF.";
RL EMBO J. 20:552-561(2001).
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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-834 AND SER-838, 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: RNA-binding protein involved in post-transcriptional
CC regulation. Negatively regulates expression of HO by binding to the 3'-
CC UTR of HO mRNA. Predominantly binds to mRNAs encoding chromatin
CC modifiers and spindle pole body components. Recognizes and binds to 5'-
CC TGTAA[CT]A[AT]TA-3' in the 3'-UTR of target mRNAs. Multicopy suppressor
CC of POP2 mutation. Required for high temperature growth.
CC {ECO:0000269|PubMed:11157761}.
CC -!- INTERACTION:
CC P39016; P31384: CCR4; NbExp=2; IntAct=EBI-2052996, EBI-4396;
CC P39016; P39517: DHH1; NbExp=3; IntAct=EBI-2052996, EBI-158;
CC P39016; P39008: POP2; NbExp=4; IntAct=EBI-2052996, EBI-13629;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15024427}.
CC -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA05172.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA58660.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA58663.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X83690; CAA58660.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X83690; CAA58663.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z72700; CAA96889.1; -; Genomic_DNA.
DR EMBL; D25541; BAA05024.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D26184; BAA05172.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006941; DAA07936.1; -; Genomic_DNA.
DR PIR; S64195; S64195.
DR RefSeq; NP_011337.1; NM_001181043.1.
DR PDB; 5BYM; X-ray; 2.71 A; A=201-600.
DR PDB; 5BZ1; X-ray; 2.15 A; A=201-600.
DR PDB; 5BZ5; X-ray; 2.80 A; A=201-600.
DR PDB; 5BZU; X-ray; 2.50 A; A=201-600.
DR PDB; 5BZV; X-ray; 2.35 A; A=201-600.
DR PDBsum; 5BYM; -.
DR PDBsum; 5BZ1; -.
DR PDBsum; 5BZ5; -.
DR PDBsum; 5BZU; -.
DR PDBsum; 5BZV; -.
DR AlphaFoldDB; P39016; -.
DR SMR; P39016; -.
DR BioGRID; 33076; 1845.
DR DIP; DIP-2271N; -.
DR IntAct; P39016; 17.
DR MINT; P39016; -.
DR STRING; 4932.YGL178W; -.
DR iPTMnet; P39016; -.
DR MaxQB; P39016; -.
DR PaxDb; P39016; -.
DR PRIDE; P39016; -.
DR EnsemblFungi; YGL178W_mRNA; YGL178W; YGL178W.
DR GeneID; 852697; -.
DR KEGG; sce:YGL178W; -.
DR SGD; S000003146; MPT5.
DR VEuPathDB; FungiDB:YGL178W; -.
DR eggNOG; KOG2049; Eukaryota.
DR HOGENOM; CLU_017863_0_0_1; -.
DR InParanoid; P39016; -.
DR OMA; PPLGQMN; -.
DR BioCyc; YEAST:G3O-30665-MON; -.
DR PRO; PR:P39016; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P39016; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR GO; GO:0045947; P:negative regulation of translational initiation; IPI:SGD.
DR GO; GO:1902416; P:positive regulation of mRNA binding; IMP:SGD.
DR GO; GO:1900153; P:positive regulation of 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:1903450; P:regulation of G1 to G0 transition; 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; 6.
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; Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..859
FT /note="Suppressor protein MPT5"
FT /id="PRO_0000075923"
FT DOMAIN 188..596
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 209..247
FT /note="Pumilio 1"
FT REPEAT 248..283
FT /note="Pumilio 2"
FT REPEAT 284..320
FT /note="Pumilio 3"
FT REPEAT 325..362
FT /note="Pumilio 4"
FT REPEAT 363..400
FT /note="Pumilio 5"
FT REPEAT 401..438
FT /note="Pumilio 6"
FT REPEAT 439..474
FT /note="Pumilio 7"
FT REPEAT 503..539
FT /note="Pumilio 8"
FT REGION 85..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:5BZ1"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:5BZ1"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:5BZ1"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 358..365
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 392..404
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:5BZ1"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 444..448
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 453..473
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 488..507
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 509..512
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 518..526
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 554..575
FT /evidence="ECO:0007829|PDB:5BZ1"
FT HELIX 576..579
FT /evidence="ECO:0007829|PDB:5BZ1"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:5BZV"
FT HELIX 585..598
FT /evidence="ECO:0007829|PDB:5BZ1"
SQ SEQUENCE 859 AA; 95422 MW; 6B289BAF3CEA2200 CRC64;
MINNEPFPSA DSASILTTST SNNSLMSYNH QPQLSINSVQ SLLEPVTPPP LGQMNNKRNH
QKAHSLDLSG FNQFISSTQS PLALMNNTST SNSANSFSPN PNAASNSTGL SASMANPPAI
LPLINEFDLE MDGPRRKSSH DFTVVAPSNS GVNTSSLIME TPSSSVTPAA SLRNFSNSNN
AASKCGVDNS SFGLSSSTSS SMVEISALPL RDLDYIKLAT DQFGCRFLQK KLETPSESNM
VRDLMYEQIK PFFLDLILDP FGNYLVQKLC DYLTAEQKTL LIQTIYPNVF QISINQYGTR
SLQKIIDTVD NEVQIDLIIK GFSQEFTSIE QVVTLINDLN GNHVIQKCIF KFSPSKFGFI
IDAIVEQNNI ITISTHKHGC CVLQKLLSVC TLQQIFKISV KIVQFLPGLI NDQFGNYIIQ
FLLDIKELDF YLLAELFNRL SNELCQLSCL KFSSNVVEKF IKKLFRIITG FIVNNNGGAS
QRTAVASDDV INASMNILLT TIDIFTVNLN VLIRDNFGNY ALQTLLDVKN YSPLLAYNKN
SNAIGQNSSS TLNYGNFCND FSLKIGNLIV LTKELLPSIK TTSYAKKIKL KVKAYAEATG
IPFTDISPQV TAMSHNNLQT INNENKNPHN KNSHNHNHNH NHNHAHNNNN NNNQKSHTRH
FSLPANAYHR RSNSSVTNNF SNQYAQDQKI HSPQQIMNFN QNAYPSMGAP SFNSQTNPPL
VSHNSLQNFD NRQFANLMAH PNSAAPIHSF SSSNITNVNP NVSRGFKQPG FMMNETDKIN
ANHFSPYSNA NSQNFNESFV PRMQYQTEGA NWDSSLSMKS QHIGQGPYNQ VNMSRNASIS
NMPAMNTART SDELQFTLP
