ID   UBCP1_XENLA             Reviewed;         318 AA.
AC   Q641F1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC082386; AAH82386.1; -; mRNA.
DR   RefSeq; NP_001087860.1; NM_001094391.1.
DR   AlphaFoldDB; Q641F1; -.
DR   SMR; Q641F1; -.
DR   MaxQB; Q641F1; -.
DR   PRIDE; Q641F1; -.
DR   GeneID; 447721; -.
DR   KEGG; xla:447721; -.
DR   CTD; 447721; -.
DR   Xenbase; XB-GENE-5892757; ublcp1.S.
DR   OMA; DSNAMIS; -.
DR   OrthoDB; 1376145at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 447721; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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_0000242646"
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;  36740 MW;  170DD5F968C32891 CRC64;
     MTLSLIIKWG GQEFPLSALS EEDTVLDLKH SLKSLTGVLP ERMKLLGLKY KGKPAENDVK
     LGVLRLKPNT KIMMMGTREE SLEEMMAPPP DNDEVVNDFD IDEEVVEVEN REENLAKISR
     RVKDYKVEVL NPPREGKKLL VLDVDYTLFD HRSCAETGQE LMRPYLHEFL SSAYEDYDIV
     IWSATSMKWI EAKMKELGVT TNANYKITFM LDSAAMITVH TPRRGLVDVK PLGVIWGKYG
     EFYSKNNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELVKLSQY LKEIAQLDDL
     SELNHKHWER YLAKKQGQ