FCP1_CAEEL
ID FCP1_CAEEL Reviewed; 659 AA.
AC Q95QG8;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase {ECO:0000250|UniProtKB:Q9Y5B0};
DE EC=3.1.3.16 {ECO:0000305|PubMed:17291483, ECO:0000305|PubMed:23903194};
GN Name=fcp-1 {ECO:0000312|WormBase:F36F2.6};
GN ORFNames=F36F2.6 {ECO:0000312|WormBase:F36F2.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17291483; DOI=10.1016/j.ydbio.2006.12.039;
RA Walker A.K., Boag P.R., Blackwell T.K.;
RT "Transcription reactivation steps stimulated by oocyte maturation in C.
RT elegans.";
RL Dev. Biol. 304:382-393(2007).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23903194; DOI=10.1242/dev.095778;
RA Bowman E.A., Bowman C.R., Ahn J.H., Kelly W.G.;
RT "Phosphorylation of RNA polymerase II is independent of P-TEFb in the C.
RT elegans germline.";
RL Development 140:3703-3713(2013).
CC -!- FUNCTION: During the late stages of oogenesis, dephosphorylates 'Ser-5'
CC of the heptad repeats YSPTSPS in the C-terminal domain of the largest
CC RNA polymerase II subunit ama-1 (PubMed:17291483). Similarly,
CC dephosphorylates 'Ser-5' of ama-1 in early embryonic cells prior to the
CC activation of the zygotic transcription program at the 4-cell embryonic
CC stage (PubMed:17291483). May dephosphorylate 'Ser-2' of the ama-1
CC heptad repeats YSPTSPS in embryonic somatic and germline cells
CC (PubMed:23903194). {ECO:0000269|PubMed:17291483,
CC ECO:0000269|PubMed:23903194}.
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 Evidence={ECO:0000305|PubMed:17291483, ECO:0000305|PubMed:23903194};
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 Evidence={ECO:0000305|PubMed:17291483, ECO:0000305|PubMed:23903194};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an arrest at the
CC 100-cell embryonic stage (PubMed:17291483). In developing oocytes,
CC results in an abnormal accumulation of 'Ser-5' phosphorylated ama-1 and
CC a more diffused nuclear localization of phosphorylated ama-1
CC (PubMed:17291483). 'Ser-2' phosphorylated ama-1 is present in
CC diakinetic oocyte but at low levels indicating that transcription is
CC possibly blocked at the elongation stage (PubMed:17291483). Increased
CC levels of 'Ser-2' phosphorylated ama-1 in embryonic and germline nuclei
CC (PubMed:23903194). Simultaneous knockdown of components of the
CC transcription pre-initiation complex including ama-1, rbp-2, cdk-7,
CC rgr-1 or taf-4 abolishes phosphorylation of the ama-1 CTD domain
CC repeats at 'Ser-5' in diakinetic oocytes (PubMed:17291483). A similar
CC abnormal accumulation of 'Ser-5' phosphorylated ama-1 occurs in 1-cell
CC and 2-cell embryos (PubMed:17291483). {ECO:0000269|PubMed:17291483,
CC ECO:0000269|PubMed:23903194}.
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DR EMBL; BX284601; CAC70088.2; -; Genomic_DNA.
DR RefSeq; NP_492423.2; NM_060022.4.
DR AlphaFoldDB; Q95QG8; -.
DR SMR; Q95QG8; -.
DR STRING; 6239.F36F2.6; -.
DR EPD; Q95QG8; -.
DR PaxDb; Q95QG8; -.
DR PeptideAtlas; Q95QG8; -.
DR EnsemblMetazoa; F36F2.6.1; F36F2.6.1; WBGene00009479.
DR GeneID; 172719; -.
DR KEGG; cel:CELE_F36F2.6; -.
DR UCSC; F36F2.6; c. elegans.
DR CTD; 172719; -.
DR WormBase; F36F2.6; CE39366; WBGene00009479; fcp-1.
DR eggNOG; KOG0323; Eukaryota.
DR GeneTree; ENSGT00390000015641; -.
DR HOGENOM; CLU_007683_1_1_1; -.
DR InParanoid; Q95QG8; -.
DR OMA; RVEDQHR; -.
DR OrthoDB; 683531at2759; -.
DR PhylomeDB; Q95QG8; -.
DR Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-CEL-113418; Formation of the Early Elongation Complex.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q95QG8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009479; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IMP:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
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 Differentiation; Hydrolase; Nucleus; Oogenesis; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..659
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase"
FT /id="PRO_0000443529"
FT DOMAIN 139..303
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT DOMAIN 351..443
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 484..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..640
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 74412 MW; B5AC5F46EF102F70 CRC64;
MDIKFEGNDA ECTAGLKKAS EGSFVLKDHV LIEFKINGKV AGKIKTPCEG VVTFGKGLKP
GIVLNKGQVI ATVSECTHAI VIKDMCATCG KDLREKGGRA GQRKEQSTAN VSMIHHVPEL
IVSDTLAKEI GSADENNLIT NRKLVLLVDL DQTIIHTSDK PMTVDTENHK DITKYNLHSR
VYTTKLRPHT TEFLNKMSNM YEMHIVTYGQ RQYAHRIAQI LDPDARLFEQ RILSRDELFS
AQHKTNNLKA LFPCGDNLVV IIDDRSDVWM YSEALIQIKP YRFFKEVGDI NAPKNSKEQM
PVQIEDDAHE DKVLEEIERV LTNIHDKYYE KHDLRGSEEV LLDVKEVIKE ERHKVLDGCV
IVFSGIVPMG EKLERTDIYR LCTQFGAVIV PDVTDDVTHV VGARYGTQKV YQANRLNKFV
VTVQWVYACV EKWLKADENL FQLTKESTPP VGRPLGSKYV NDLANMDTIG KAALADMNNE
VDEALSDDED DGDNEDEDDD GNDVGEDKGD ENLEEKQEKN EEEMDDVEQN GSVENQSGDA
LENETDSTSR GQKRKHCPEM EDEEEESDSD NEDDDTPMSY KALLSDSRKK GRIVPENEDD
AVFDVDDEKG HAPANIDEEE DDEDNEDEEV PESDDDDEFE DMAALIERQI SDAVDEKDQ
