ID   UBCP1_PONAB             Reviewed;         318 AA.
AC   Q5R4C4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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; CR861328; CAH93392.1; -; mRNA.
DR   RefSeq; NP_001126990.1; NM_001133518.1.
DR   AlphaFoldDB; Q5R4C4; -.
DR   BMRB; Q5R4C4; -.
DR   SMR; Q5R4C4; -.
DR   STRING; 9601.ENSPPYP00000017904; -.
DR   GeneID; 100174013; -.
DR   KEGG; pon:100174013; -.
DR   CTD; 134510; -.
DR   eggNOG; KOG1605; Eukaryota.
DR   eggNOG; KOG1872; Eukaryota.
DR   InParanoid; Q5R4C4; -.
DR   OrthoDB; 1376145at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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   Acetylation; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WVY7"
FT   CHAIN           2..318
FT                   /note="Ubiquitin-like domain-containing CTD phosphatase 1"
FT                   /id="PRO_0000242642"
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"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WVY7"
FT   MOD_RES         117
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WVY7"
SQ   SEQUENCE   318 AA;  36675 MW;  23A6DDB17A0E6E0F CRC64;
     MALPIIVKWG GQEYSVTTLS EDDTVLDLKQ FLKTLTGVLP ERQKLLGLKV KGKPAENDVK
     LGALKLKPNT KIMMMGTREE SLEDVLGPPP DNDDVVNDFD IEDEVVEVEN REENLLKISR
     RVKEYKVEIL NPPREGKKLL VLDVDYTLFD HRSCAETGVE LMRPYLHEFL TSAYEDYDIV
     IWSATNMKWI EAKMKELGVS TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS
     EFYSKKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKGLLKLTQY LKEIAKLDDF
     LGLNHKYWER YLSKKQGQ