ID   SSU72_YEAST             Reviewed;         206 AA.
AC   P53538; D6W0W8; Q6Q569;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase SSU72;
DE            Short=CTD phosphatase SSU72;
DE            EC=3.1.3.16;
DE   AltName: Full=Suppressor of SUA7 protein 2;
GN   Name=SSU72; OrderedLocusNames=YNL222W; ORFNames=N1279;
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].
RX   PubMed=8657130; DOI=10.1128/mcb.16.4.1557;
RA   Sun Z.W., Hampsey M.;
RT   "Synthetic enhancement of a TFIIB defect by a mutation in SSU72, an
RT   essential yeast gene encoding a novel protein that affects transcription
RT   start site selection in vivo.";
RL   Mol. Cell. Biol. 16:1557-1566(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION IN SNORNA 3-END FORMATION.
RX   PubMed=12660165; DOI=10.1093/emboj/cdg141;
RA   Ganem C., Devaux F., Torchet C., Jacq C., Quevillon-Cheruel S., Labesse G.,
RA   Facca C., Faye G.;
RT   "Ssu72 is a phosphatase essential for transcription termination of snoRNAs
RT   and specific mRNAs in yeast.";
RL   EMBO J. 22:1588-1598(2003).
RN   [6]
RP   IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION 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   [7]
RP   FUNCTION AS A PHOSPHATASE, AND FUNCTION IN SNORNA 3'-END FORMATION.
RX   PubMed=15125841; DOI=10.1016/s1097-2765(04)00235-7;
RA   Krishnamurthy S., He X., Reyes-Reyes M., Moore C., Hampsey M.;
RT   "Ssu72 Is an RNA polymerase II CTD phosphatase.";
RL   Mol. Cell 14:387-394(2004).
RN   [8]
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   [9]
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: 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. Component of the APT complex, which may be
CC       involved in polyadenylation-independent transcript 3'-end formation.
CC       SSU72 is required for 3'-end formation of snoRNAs.
CC   -!- FUNCTION: Processively dephosphorylates Ser-5 of the heptad repeats
CC       YSPTSPS in the C-terminal domain of the largest RNA polymerase II
CC       subunit (RPB1).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
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       Component of the APT complex, which is a subcomplex of CPF, and is
CC       composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2.
CC       {ECO:0000269|PubMed:12819204}.
CC   -!- INTERACTION:
CC       P53538; Q01329: PTA1; NbExp=6; IntAct=EBI-18134, EBI-14145;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204}.
CC   -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR   EMBL; U20390; AAA86497.1; -; Genomic_DNA.
DR   EMBL; Z71498; CAA96125.1; -; Genomic_DNA.
DR   EMBL; AY558421; AAS56747.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10334.1; -; Genomic_DNA.
DR   PIR; S63180; S63180.
DR   RefSeq; NP_014177.1; NM_001183060.1.
DR   AlphaFoldDB; P53538; -.
DR   SMR; P53538; -.
DR   BioGRID; 35614; 245.
DR   ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR   DIP; DIP-6700N; -.
DR   IntAct; P53538; 16.
DR   MINT; P53538; -.
DR   STRING; 4932.YNL222W; -.
DR   iPTMnet; P53538; -.
DR   MaxQB; P53538; -.
DR   PaxDb; 4932-YNL222W; -.
DR   PeptideAtlas; P53538; -.
DR   EnsemblFungi; YNL222W_mRNA; YNL222W; YNL222W.
DR   GeneID; 855499; -.
DR   KEGG; sce:YNL222W; -.
DR   AGR; SGD:S000005166; -.
DR   SGD; S000005166; SSU72.
DR   VEuPathDB; FungiDB:YNL222W; -.
DR   eggNOG; KOG2424; Eukaryota.
DR   GeneTree; ENSGT00390000010165; -.
DR   HOGENOM; CLU_062463_0_1_1; -.
DR   InParanoid; P53538; -.
DR   OMA; TQPNVYQ; -.
DR   OrthoDB; 63608at2759; -.
DR   BioCyc; YEAST:G3O-33225-MONOMER; -.
DR   BioGRID-ORCS; 855499; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P53538; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53538; Protein.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IGI:SGD.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IGI:SGD.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:SGD.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:SGD.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR   GO; GO:0006378; P:mRNA polyadenylation; IDA:ComplexPortal.
DR   GO; GO:0009302; P:sno(s)RNA transcription; IMP:SGD.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR   GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IMP:SGD.
DR   GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IMP:SGD.
DR   GO; GO:0031564; P:transcription antitermination; IMP:SGD.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IGI:SGD.
DR   GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IMP:SGD.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   InterPro; IPR006811; RNA_pol_II_suA.
DR   PANTHER; PTHR20383; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR   PANTHER; PTHR20383:SF9; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE SSU72; 1.
DR   Pfam; PF04722; Ssu72; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; mRNA processing; Nucleus; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..206
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase SSU72"
FT                   /id="PRO_0000072230"
FT   CONFLICT        199
FT                   /note="S -> P (in Ref. 4; AAS56747)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   206 AA;  23469 MW;  1AE1B29B87C82FE9 CRC64;
     MPSHRNSNLK FCTVCASNNN RSMESHKVLQ EAGYNVSSYG TGSAVRLPGL SIDKPNVYSF
     GTPYNDIYND LLSQSADRYK SNGLLQMLDR NRRLKKAPEK WQESTKVFDF VFTCEERCFD
     AVCEDLMNRG GKLNKIVHVI NVDIKDDDEN AKIGSKAILE LADMLNDKIE QCEKDDIPFE
     DCIMDILTEW QSSHSQLPSL YAPSYY
//