ID   UBCP1_DANRE             Reviewed;         318 AA.
AC   Q6DI37;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=zgc:86634;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-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}.
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DR   EMBL; BC075753; AAH75753.1; -; mRNA.
DR   RefSeq; NP_001002319.1; NM_001002319.2.
DR   RefSeq; NP_001186304.1; NM_001199375.1.
DR   AlphaFoldDB; Q6DI37; -.
DR   SMR; Q6DI37; -.
DR   STRING; 7955.ENSDARP00000065340; -.
DR   PaxDb; Q6DI37; -.
DR   Ensembl; ENSDART00000065341; ENSDARP00000065340; ENSDARG00000044492.
DR   Ensembl; ENSDART00000076715; ENSDARP00000071186; ENSDARG00000044492.
DR   Ensembl; ENSDART00000162189; ENSDARP00000130882; ENSDARG00000044492.
DR   Ensembl; ENSDART00000185042; ENSDARP00000144720; ENSDARG00000044492.
DR   GeneID; 792145; -.
DR   KEGG; dre:792145; -.
DR   CTD; 134510; -.
DR   ZFIN; ZDB-GENE-040718-3; ublcp1.
DR   eggNOG; KOG1605; Eukaryota.
DR   eggNOG; KOG1872; Eukaryota.
DR   GeneTree; ENSGT00390000010107; -.
DR   InParanoid; Q6DI37; -.
DR   OMA; DSNAMIS; -.
DR   OrthoDB; 1376145at2759; -.
DR   PhylomeDB; Q6DI37; -.
DR   TreeFam; TF323786; -.
DR   PRO; PR:Q6DI37; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 21.
DR   Bgee; ENSDARG00000044492; Expressed in blastula and 20 other tissues.
DR   ExpressionAtlas; Q6DI37; baseline.
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_0000242645"
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;  36822 MW;  ED57FD31B4D25748 CRC64;
     MSVSVIIKWG GQEYSINTLS EEDTVLDLKQ SIKSLTGVLP ERQKLLGLKL KGKPADDNVK
     LGDLKLKPNT KIMMMGTREE SLEDVLAPPP ENDDVVNDFD IEEEVTEVEN REENLAKIAR
     RVKDYKVEEL NPPRPGKRLL VLDIDYTLFD HKSCAETGHE LMRPFLHEFL TSAYEDFDIV
     IWSATSMKWI DAKMKELGVT DNPNYKITFM LDSAAMITVH TPKRGVVEVK PLGVIWGKYS
     EFYNRKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNREK DKELYKLSQY LKEIAKLDDF
     SGLNHKHWER YLSKKQNQ