SSU72_CAEEL
ID SSU72_CAEEL Reviewed; 197 AA.
AC Q22453;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 4.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase ssup-72 {ECO:0000305};
DE Short=CTD phosphatase ssup-72 {ECO:0000250|UniProtKB:Q9NP77};
DE EC=3.1.3.16 {ECO:0000269|PubMed:26588990};
GN Name=ssup-72 {ECO:0000312|WormBase:T13C2.4};
GN ORFNames=T13C2.4 {ECO:0000312|WormBase:T13C2.4};
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, INTERACTION WITH SYDN-1 AND AMA-1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF CYS-13; GLY-47 AND ASP-145.
RX PubMed=26588990; DOI=10.1101/gad.266650.115;
RA Chen F., Zhou Y., Qi Y.B., Khivansara V., Li H., Chun S.Y., Kim J.K.,
RA Fu X.D., Jin Y.;
RT "Context-dependent modulation of Pol II CTD phosphatase SSUP-72 regulates
RT alternative polyadenylation in neuronal development.";
RL Genes Dev. 29:2377-2390(2015).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-47.
RX PubMed=28087624; DOI=10.1242/dev.146001;
RA Chen F., Chisholm A.D., Jin Y.;
RT "Tissue-specific regulation of alternative polyadenylation represses
RT expression of a neuronal ankyrin isoform in C. elegans epidermal
RT development.";
RL Development 144:698-707(2017).
RN [4]
RP PHOSPHORYLATION AT SER-39, AND MUTAGENESIS OF SER-39.
RX PubMed=31910362; DOI=10.1016/j.devcel.2019.12.005;
RA LaBella M.L., Hujber E.J., Moore K.A., Rawson R.L., Merrill S.A.,
RA Allaire P.D., Ailion M., Hollien J., Bastiani M.J., Jorgensen E.M.;
RT "Casein Kinase 1delta Stabilizes Mature Axons by Inhibiting Transcription
RT Termination of Ankyrin.";
RL Dev. Cell 52:88-103(2020).
CC -!- FUNCTION: Protein phosphatase that dephosphorylates 'Ser-5' of the
CC heptad repeats YSPTSPS in the C-terminal domain of the large RNA
CC polymerase II subunit ama-1 (PubMed:26588990). By regulating the
CC phosphorylation status of ama-1 and thus ama-1 binding to specific
CC polyadenylation sites, regulates alternative polyadenylation of pre-
CC mRNAs, including unc-44 and dlk-1 mRNAs (PubMed:26588990,
CC PubMed:28087624). This results in the tissue-specific expression of
CC unc-44 isoforms (PubMed:28087624). {ECO:0000269|PubMed:26588990,
CC ECO:0000269|PubMed:28087624}.
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:0000269|PubMed:26588990};
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:0000250|UniProtKB:Q9NP77};
CC -!- SUBUNIT: May interact with synd-1 (via C-terminus); the interaction may
CC prevent ssup-72 binding to RNA polymerase II ama-1 (PubMed:26588990).
CC May interact with RNA polymerase II ama-1 (Probable).
CC {ECO:0000269|PubMed:26588990, ECO:0000305|PubMed:9851916}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26588990}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermis, intestine and nervous
CC system. {ECO:0000269|PubMed:26588990}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults.
CC {ECO:0000269|PubMed:26588990}.
CC -!- PTM: May be phosphorylated by kin-20. {ECO:0000305|PubMed:31910362}.
CC -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR EMBL; BX284602; CCD70326.1; -; Genomic_DNA.
DR RefSeq; NP_495386.3; NM_062985.3.
DR AlphaFoldDB; Q22453; -.
DR SMR; Q22453; -.
DR STRING; 6239.T13C2.4; -.
DR EPD; Q22453; -.
DR PaxDb; Q22453; -.
DR PeptideAtlas; Q22453; -.
DR EnsemblMetazoa; T13C2.4.1; T13C2.4.1; WBGene00020480.
DR EnsemblMetazoa; T13C2.4.2; T13C2.4.2; WBGene00020480.
DR GeneID; 188472; -.
DR KEGG; cel:CELE_T13C2.4; -.
DR UCSC; T13C2.4; c. elegans.
DR CTD; 188472; -.
DR WormBase; T13C2.4; CE39774; WBGene00020480; ssup-72.
DR eggNOG; KOG2424; Eukaryota.
DR GeneTree; ENSGT00390000010165; -.
DR HOGENOM; CLU_062463_2_1_1; -.
DR InParanoid; Q22453; -.
DR OMA; PNCYEFG; -.
DR OrthoDB; 1304061at2759; -.
DR PhylomeDB; Q22453; -.
DR Reactome; R-CEL-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:Q22453; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00020480; Expressed in embryo and 3 other tissues.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0040012; P:regulation of locomotion; IGI:UniProtKB.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR InterPro; IPR006811; RNA_pol_II_suA.
DR PANTHER; PTHR20383; PTHR20383; 1.
DR Pfam; PF04722; Ssu72; 1.
PE 1: Evidence at protein level;
KW Hydrolase; mRNA processing; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..197
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase ssup-72"
FT /id="PRO_0000447207"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:31910362"
FT MUTAGEN 13
FT /note="C->S: No obvious phenotype. Fails to suppress
FT abnormal synapse and axon formation in a sydn-1 and syd-2
FT mutant background."
FT /evidence="ECO:0000269|PubMed:26588990"
FT MUTAGEN 39
FT /note="S->A: Does not suppress the locomotion defect of the
FT kin-20 ox423 mutant."
FT /evidence="ECO:0000269|PubMed:31910362"
FT MUTAGEN 39
FT /note="S->F,E: Suppresses the locomotion defect of the kin-
FT 20 ox423 mutant."
FT /evidence="ECO:0000269|PubMed:31910362"
FT MUTAGEN 47
FT /note="G->E: In ju924; increases ama-1 'Ser-5'
FT phosphorylation, alters usage of internal polyadenylation
FT sites (PAS) in unc-44 and dlk-1 pre-mRNAs. Restores ama-1
FT binding to neuron-specific PASs, expression of unc-44 in
FT neurons and vulva, and suppresses abnormal synapse and axon
FT formation in a sydn-1 (ju541) mutant background."
FT /evidence="ECO:0000269|PubMed:26588990,
FT ECO:0000269|PubMed:28087624"
FT MUTAGEN 145
FT /note="D->A: No obvious phenotype. Fails to suppress
FT abnormal synapse and axon formation in a sydn-1 and syd-2
FT mutant background."
FT /evidence="ECO:0000269|PubMed:26588990"
SQ SEQUENCE 197 AA; 22775 MW; AB2214165FA041BC CRC64;
MEYSSKLRFA VSCSSNMNRS MEAHGILKKR GFNIESYGSG NQVKMPGPTV DKPNCYEFGP
TTYEDIYADL TNKDLHLYTQ NGLLHMVDRN RRIKSRPQRF QAETREFDIV LCLEERVFDQ
VVDFLNRSVG KSGNPVHVIN IDIEDNAEEA TFGAFFVADL CEKLERSEDF EEDIDQIITD
LEENNPKRNL LHTICFY
