ID   UBCP1_XENTR             Reviewed;         318 AA.
AC   Q28EX9; A4IHX3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ubiquitin-like domain-containing CTD phosphatase 1;
DE            EC=3.1.3.16;
DE   AltName: Full=Nuclear proteasome inhibitor UBLCP1;
GN   Name=ublcp1; ORFNames=TGas135j05.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing
CC       their proteolytic activity. The dephosphorylation may prevent assembly
CC       of the core and regulatory particles (CP and RP) into mature 26S
CC       proteasome (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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC       nuclear proteasomes. {ECO:0000250}.
CC   -!- DOMAIN: The Ubiquitin-like domain mediates interaction with
CC       proteasomes. {ECO:0000250}.
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DR   EMBL; CR762286; CAJ83586.1; -; mRNA.
DR   EMBL; BC135735; AAI35736.1; -; mRNA.
DR   RefSeq; NP_001016061.1; NM_001016061.2.
DR   AlphaFoldDB; Q28EX9; -.
DR   SMR; Q28EX9; -.
DR   STRING; 8364.ENSXETP00000027925; -.
DR   PaxDb; Q28EX9; -.
DR   DNASU; 548815; -.
DR   GeneID; 548815; -.
DR   KEGG; xtr:548815; -.
DR   CTD; 134510; -.
DR   Xenbase; XB-GENE-5892709; ublcp1.
DR   eggNOG; KOG1605; Eukaryota.
DR   eggNOG; KOG1872; Eukaryota.
DR   HOGENOM; CLU_1317152_0_0_1; -.
DR   InParanoid; Q28EX9; -.
DR   OrthoDB; 1376145at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000016360; Expressed in skeletal muscle tissue and 13 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR011943; HAD-SF_hydro_IIID.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF03031; NIF; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02245; HAD_IIID1; 1.
DR   PROSITE; PS50969; FCP1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Ubiquitin-like domain-containing CTD phosphatase 1"
FT                   /id="PRO_0000242647"
FT   DOMAIN          3..81
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          133..294
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          133..294
FT                   /note="Phosphatase"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  36854 MW;  6544E1EF04FE4633 CRC64;
     MTLSLIIKWG GQEFPLSALS EEDTVLDLKH SLKSLTGVLP ERMKLLGLKY KGKPAENDVK
     LGVLKLKPNT KIMMMGTREE SLEEMMAPPP ENDEVVNDFD IEEEVVEVEN REENLAKISR
     RVKDYKIEIL NPPREGKKLL VLDVDYTLFD HRSCAETGQE LMRPYLHEFL TSAYEDYDIV
     IWSATSMKWI EAKMKELGVS TNSNYKITFM LDSAAMITVH TPRRGLVDVK PLGVIWGKYG
     EFYNKNNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELLKLSQY LKEIAQLDDL
     SELNHKHWER YLVKKQGQ