ID   SSU72_RAT               Reviewed;         194 AA.
AC   Q4KLK9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase SSU72;
DE            Short=CTD phosphatase SSU72;
DE            EC=3.1.3.16;
GN   Name=Ssu72;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of
CC       the C-terminal domain of RNA polymerase II. Plays a role in RNA
CC       processing and termination. Plays a role in pre-mRNA polyadenylation
CC       via its interaction with SYMPK (By similarity). {ECO:0000250}.
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: Interacts with GTF2B (via C-terminus); this interaction is
CC       inhibited by SYMPK. Interacts with RB1. Interacts with CD226. Interacts
CC       with SYMPK. {ECO:0000250|UniProtKB:Q9NP77}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly in the cytosol. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR   EMBL; BC099142; AAH99142.1; -; mRNA.
DR   RefSeq; NP_001020828.1; NM_001025657.1.
DR   AlphaFoldDB; Q4KLK9; -.
DR   SMR; Q4KLK9; -.
DR   STRING; 10116.ENSRNOP00000024349; -.
DR   iPTMnet; Q4KLK9; -.
DR   PhosphoSitePlus; Q4KLK9; -.
DR   PaxDb; Q4KLK9; -.
DR   PRIDE; Q4KLK9; -.
DR   Ensembl; ENSRNOT00000024349; ENSRNOP00000024349; ENSRNOG00000017829.
DR   GeneID; 298681; -.
DR   KEGG; rno:298681; -.
DR   CTD; 29101; -.
DR   RGD; 1307854; Ssu72.
DR   eggNOG; KOG2424; Eukaryota.
DR   GeneTree; ENSGT00390000010165; -.
DR   HOGENOM; CLU_062463_2_1_1; -.
DR   InParanoid; Q4KLK9; -.
DR   OMA; PNCYEFG; -.
DR   OrthoDB; 1304061at2759; -.
DR   PhylomeDB; Q4KLK9; -.
DR   TreeFam; TF300194; -.
DR   Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR   PRO; PR:Q4KLK9; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000017829; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q4KLK9; RN.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR   GO; GO:0006378; P:mRNA polyadenylation; ISS: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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Hydrolase; mRNA processing; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..194
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase SSU72"
FT                   /id="PRO_0000330014"
FT   COILED          160..187
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   194 AA;  22544 MW;  DA3B3157A2388A77 CRC64;
     MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD KPNVYDFKTT
     YDQMYNDLLR KDKELYTQNG ILHMLDRNKR IKPRPERFQN CKDLFDLILT CEERVYDQVV
     EDLNSREQET CQPVHVVNVD IQDNHEEATL GAFLICELCQ CIQHTEDMEN EIDELLQEFE
     EKSGRAFLHT VCFY