ID   SSU72_BOVIN             Reviewed;         194 AA.
AC   Q17QI2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC118344; AAI18345.1; -; mRNA.
DR   RefSeq; NP_001069817.1; NM_001076349.1.
DR   AlphaFoldDB; Q17QI2; -.
DR   SMR; Q17QI2; -.
DR   STRING; 9913.ENSBTAP00000003331; -.
DR   PaxDb; Q17QI2; -.
DR   PRIDE; Q17QI2; -.
DR   Ensembl; ENSBTAT00000003331; ENSBTAP00000003331; ENSBTAG00000002575.
DR   GeneID; 614837; -.
DR   KEGG; bta:614837; -.
DR   CTD; 29101; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002575; -.
DR   eggNOG; KOG2424; Eukaryota.
DR   GeneTree; ENSGT00390000010165; -.
DR   HOGENOM; CLU_062463_2_2_1; -.
DR   InParanoid; Q17QI2; -.
DR   OMA; PNCYEFG; -.
DR   OrthoDB; 1304061at2759; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000002575; Expressed in oocyte and 107 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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_0000330011"
FT   COILED          160..186
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   194 AA;  22588 MW;  CA252E57BD278A77 CRC64;
     MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD KPNVYDFKTT
     YDQMYNDLLR KDKELYTQNG ILHMLDRNKR IKPRPERFQN CKDLFDLILT CEERVYDQVV
     EDLNSREQET CQPVHVINVD IQDNHEEATL GAFLICELCQ CIQHTEDMEN EIDELLQEFE
     EKSGRTFLHT VCFY