ID   FCP1_YEAST              Reviewed;         732 AA.
AC   Q03254; D6W0A4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase;
DE            EC=3.1.3.16;
DE   AltName: Full=CTD phosphatase FCP1;
GN   Name=FCP1; OrderedLocusNames=YMR277W; ORFNames=YM8021.03;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
RP   CHARACTERIZATION.
RX   PubMed=8798710; DOI=10.1074/jbc.271.40.24498;
RA   Chambers R.S., Kane C.M.;
RT   "Purification and characterization of an RNA polymerase II phosphatase from
RT   yeast.";
RL   J. Biol. Chem. 271:24498-24504(1996).
RN   [4]
RP   FUNCTION.
RX   PubMed=10445027; DOI=10.1016/s1097-2765(00)80187-2;
RA   Kobor M.S., Archambault J., Lester W., Holstege F.C.P., Gileadi O.,
RA   Jansma D.B., Jennings E.G., Kouyoumdjian F., Davidson A.R., Young R.A.,
RA   Greenblatt J.;
RT   "An unusual eukaryotic protein phosphatase required for transcription by
RT   RNA polymerase II and CTD dephosphorylation in S. cerevisiae.";
RL   Mol. Cell 4:55-62(1999).
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-701, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718 AND SER-720, 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).
RN   [8]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-74, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the
CC       heptad repeats YSPTSPS in the C-terminal domain of the largest RNA
CC       polymerase II subunit (RPB1). This promotes the activity of RNA
CC       polymerase II. {ECO:0000269|PubMed:10445027}.
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   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 6550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z49704; CAA89775.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10178.1; -; Genomic_DNA.
DR   PIR; S54584; S54584.
DR   RefSeq; NP_014004.1; NM_001182784.1.
DR   AlphaFoldDB; Q03254; -.
DR   SMR; Q03254; -.
DR   BioGRID; 35456; 595.
DR   DIP; DIP-2330N; -.
DR   IntAct; Q03254; 12.
DR   MINT; Q03254; -.
DR   STRING; 4932.YMR277W; -.
DR   iPTMnet; Q03254; -.
DR   MaxQB; Q03254; -.
DR   PaxDb; 4932-YMR277W; -.
DR   PeptideAtlas; Q03254; -.
DR   EnsemblFungi; YMR277W_mRNA; YMR277W; YMR277W.
DR   GeneID; 855320; -.
DR   KEGG; sce:YMR277W; -.
DR   AGR; SGD:S000004890; -.
DR   SGD; S000004890; FCP1.
DR   VEuPathDB; FungiDB:YMR277W; -.
DR   eggNOG; KOG0323; Eukaryota.
DR   GeneTree; ENSGT00390000015641; -.
DR   HOGENOM; CLU_007683_0_0_1; -.
DR   InParanoid; Q03254; -.
DR   OMA; DQTVIHC; -.
DR   OrthoDB; 73422at2759; -.
DR   BioCyc; YEAST:G3O-32948-MONOMER; -.
DR   Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   BioGRID-ORCS; 855320; 4 hits in 10 CRISPR screens.
DR   PRO; PR:Q03254; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03254; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   CDD; cd17729; BRCT_CTDP1; 1.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR039189; Fcp1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR011947; FCP1_euk.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR02250; FCP1_euk; 1.
DR   PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR   PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein; Protein phosphatase;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..732
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase"
FT                   /id="PRO_0000212568"
FT   DOMAIN          170..363
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   DOMAIN          499..593
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          50..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..673
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..715
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..732
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         701
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         718
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         720
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CROSSLNK        74
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   732 AA;  83441 MW;  EACA2A7D33A983C6 CRC64;
     MTTQIRSPQG LPYPIQIDKL IPSVGSYLHE GDRLLVYKFW YLVERASDTG DDDNEHDVSP
     GGSAGSNGVS PPTKQLRESI EFFESPYEGD LISWNVDVGD EVATANQVIC EIKRPCNHDI
     VYGGLCTQCG KEVSADAFDG VPLDVVGDVD LQISETEAIR TGKALKEHLR RDKKLILVVD
     LDQTIIHCGV DPTIAEWKND PNNPNFETLR DVKSFTLDEE LVLPLMYMND DGSMLRPPPV
     RKCWYYVKVR PGLKEFFAKV APLFEMHIYT MATRAYALQI AKIVDPTGEL FGDRILSRDE
     NGSLTTKSLA KLFPTDQSMV VVIDDRGDVW NWCPNLIKVV PYNFFVGVGD INSNFLPKQS
     TGMLQLGRKT RQKSQESQEL LTDIMDNEKK LQEKIDKEVK RQEEKLNHQL ATAEEPPANE
     SKEELTKKLE YSASLEVQQQ NRPLAKLQKH LHDQKLLVDD DDELYYLMGT LSNIHKTYYD
     MLSQQNEPEP NLMEIIPSLK QKVFQNCYFV FSGLIPLGTD IQRSDIVIWT STFGATSTPD
     IDYLTTHLIT KNPSTYKARL AKKFNPQIKI VHPDWIFECL VNWKKVDEKP YTLIVDSPIS
     DEELQNFQTQ LQKRQEYLEE TQEQQHMLTS QENLNLFAAG TSWLNNDDDE DIPDTASDDD
     EDDDHDDESD DENNSEGIDR KRSIEDNHDD TSQKKTKAEP SQDGPVQHKG EGDDNEDSDS
     QLEEELMDML DD
//