FCP1_YEAST
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 03-AUG-2022, entry version 169.
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; 593.
DR DIP; DIP-2330N; -.
DR IntAct; Q03254; 12.
DR MINT; Q03254; -.
DR STRING; 4932.YMR277W; -.
DR iPTMnet; Q03254; -.
DR MaxQB; Q03254; -.
DR PaxDb; Q03254; -.
DR PRIDE; Q03254; -.
DR EnsemblFungi; YMR277W_mRNA; YMR277W; YMR277W.
DR GeneID; 855320; -.
DR KEGG; sce:YMR277W; -.
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; IHACIDP; -.
DR BioCyc; YEAST:G3O-32948-MON; -.
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 Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
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:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.40.50.10190; -; 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 PANTHER; PTHR23081; PTHR23081; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02250; FCP1_euk; 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
