MPE1_YEAST
ID MPE1_YEAST Reviewed; 441 AA.
AC P35728; D6VXM8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein MPE1;
GN Name=MPE1; OrderedLocusNames=YKL059C; ORFNames=YKL316;
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;
RX PubMed=8091862; DOI=10.1002/yea.320100008;
RA Rasmussen S.W.;
RT "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT TOA2 genes, an open reading frame (ORF) similar to a translationally
RT controlled tumour protein, one ORF containing motifs also found in plant
RT storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL Yeast 10:S63-S68(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=12819204; DOI=10.1074/jbc.m304454200;
RA Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T.,
RA Buratowski S., Moore C.L., Greenblatt J.;
RT "Organization and function of APT, a subcomplex of the yeast cleavage and
RT polyadenylation factor involved in the formation of mRNA and small
RT nucleolar RNA 3'-ends.";
RL J. Biol. Chem. 278:33000-33010(2003).
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 SER-221, 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).
CC -!- FUNCTION: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which plays a key role in polyadenylation-dependent pre-mRNA
CC 3'-end formation and cooperates with cleavage factors including the
CC CFIA complex and NAB4/CFIB.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2,
CC PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1.
CC {ECO:0000269|PubMed:12819204}.
CC -!- INTERACTION:
CC P35728; Q06632: CFT1; NbExp=5; IntAct=EBI-26710, EBI-32872;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204}.
CC -!- MISCELLANEOUS: Present with 1130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X75781; CAA53413.1; -; Genomic_DNA.
DR EMBL; Z28059; CAA81896.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09098.1; -; Genomic_DNA.
DR PIR; S37881; S37881.
DR RefSeq; NP_012864.1; NM_001179625.1.
DR PDB; 6I1D; X-ray; 2.28 A; B=1-160.
DR PDBsum; 6I1D; -.
DR AlphaFoldDB; P35728; -.
DR SMR; P35728; -.
DR BioGRID; 34074; 241.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR DIP; DIP-6650N; -.
DR IntAct; P35728; 62.
DR MINT; P35728; -.
DR STRING; 4932.YKL059C; -.
DR iPTMnet; P35728; -.
DR MaxQB; P35728; -.
DR PaxDb; P35728; -.
DR PRIDE; P35728; -.
DR EnsemblFungi; YKL059C_mRNA; YKL059C; YKL059C.
DR GeneID; 853806; -.
DR KEGG; sce:YKL059C; -.
DR SGD; S000001542; MPE1.
DR VEuPathDB; FungiDB:YKL059C; -.
DR eggNOG; KOG0314; Eukaryota.
DR GeneTree; ENSGT00940000159365; -.
DR HOGENOM; CLU_019105_0_0_1; -.
DR InParanoid; P35728; -.
DR OMA; MSVIYYK; -.
DR BioCyc; YEAST:G3O-31858-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P35728; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35728; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:SGD.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:ComplexPortal.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IMP:SGD.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IC:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR014891; DWNN_domain.
DR InterPro; IPR033489; RBBP6.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15439; PTHR15439; 1.
DR Pfam; PF08783; DWNN; 1.
DR SMART; SM01180; DWNN; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS51282; DWNN; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..441
FT /note="Protein MPE1"
FT /id="PRO_0000076265"
FT DOMAIN 5..78
FT /note="DWNN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00612"
FT ZN_FING 180..197
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 355..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6I1D"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6I1D"
FT STRAND 16..26
FT /evidence="ECO:0007829|PDB:6I1D"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:6I1D"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:6I1D"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6I1D"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6I1D"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:6I1D"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6I1D"
SQ SEQUENCE 441 AA; 49647 MW; 487567F6FD2C3F61 CRC64;
MSSTIFYRFK SQRNTSRILF DGTGLTVFDL KREIIQENKL GDGTDFQLKI YNPDTEEEYD
DDAFVIPRST SVIVKRSPAI KSFSVHSRLK GNVGAAALGN ATRYVTGRPR VLQKRQHTAT
TTANVSGTTE EERIASMFAT QENQWEQTQE EMSAATPVFF KSQTNKNSAQ ENEGPPPPGY
MCYRCGGRDH WIKNCPTNSD PNFEGKRIRR TTGIPKKFLK SIEIDPETMT PEEMAQRKIM
ITDEGKFVVQ VEDKQSWEDY QRKRENRQID GDETIWRKGH FKDLPDDLKC PLTGGLLRQP
VKTSKCCNID FSKEALENAL VESDFVCPNC ETRDILLDSL VPDQDKEKEV ETFLKKQEEL
HGSSKDGNQP ETKKMKLMDP TGTAGLNNNT SLPTSVNNGG TPVPPVPLPF GIPPFPMFPM
PFMPPTATIT NPHQADASPK K
