ID UBCP1_CHICK Reviewed; 318 AA. AC Q5ZJJ8; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Ubiquitin-like domain-containing CTD phosphatase 1; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q8WVY7}; DE AltName: Full=Nuclear proteasome inhibitor UBLCP1; GN Name=UBLCP1; ORFNames=RCJMB04_17j14; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., RA Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:R6.1-R6.9(2005). CC -!- FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing CC their proteolytic activity. Recruited to the 19S regulatory particle of CC the 26S proteasome where it dephosphorylates 19S component PSMC2 which CC impairs PSMC2 ATPase activity and disrupts 26S proteasome assembly. Has CC also been reported to stimulate the proteolytic activity of the 26S CC proteasome. {ECO:0000250|UniProtKB:Q8WVY7}. 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 Evidence={ECO:0000250|UniProtKB:Q8WVY7}; 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 Evidence={ECO:0000250|UniProtKB:Q8WVY7}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q8WVY7}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WVY7}. CC Note=Colocalizes with nuclear proteasomes. CC {ECO:0000250|UniProtKB:Q8WVY7}. CC -!- DOMAIN: The Ubiquitin-like domain mediates interaction with CC proteasomes. {ECO:0000250|UniProtKB:Q8WVY7}. 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; AJ720436; CAG32095.1; -; mRNA. DR RefSeq; NP_001025784.2; NM_001030613.3. DR RefSeq; XP_015149251.1; XM_015293765.1. DR AlphaFoldDB; Q5ZJJ8; -. DR SMR; Q5ZJJ8; -. DR STRING; 9031.ENSGALP00000005808; -. DR PaxDb; 9031-ENSGALP00000040691; -. DR Ensembl; ENSGALT00000005818; ENSGALP00000005808; ENSGALG00000003672. DR Ensembl; ENSGALT00010035864.1; ENSGALP00010020802.1; ENSGALG00010014900.1. DR Ensembl; ENSGALT00015055365; ENSGALP00015033463; ENSGALG00015022639. DR GeneID; 416237; -. DR KEGG; gga:416237; -. DR CTD; 134510; -. DR VEuPathDB; HostDB:geneid_416237; -. DR eggNOG; KOG1605; Eukaryota. DR eggNOG; KOG1872; Eukaryota. DR GeneTree; ENSGT00390000010107; -. DR HOGENOM; CLU_046931_1_0_1; -. DR InParanoid; Q5ZJJ8; -. DR OMA; DSNAMIS; -. DR OrthoDB; 49886at2759; -. DR PhylomeDB; Q5ZJJ8; -. DR TreeFam; TF323786; -. DR PRO; PR:Q5ZJJ8; -. DR Proteomes; UP000000539; Chromosome 13. DR Bgee; ENSGALG00000003672; Expressed in spermatid and 13 other cell types or tissues. DR ExpressionAtlas; Q5ZJJ8; baseline and differential. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:1904855; F:proteasome regulatory particle binding; IEA:Ensembl. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0090364; P:regulation of proteasome assembly; IEA:Ensembl. DR CDD; cd01813; Ubl_UBLCP1; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR02245; HAD_IIID1; 1. DR PANTHER; PTHR48405; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1. DR PANTHER; PTHR48405:SF1; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1. DR Pfam; PF03031; NIF; 1. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00577; CPDc; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50969; FCP1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 2: Evidence at transcript level; KW Hydrolase; Magnesium; Metal-binding; Nucleus; Protein phosphatase; KW Reference proteome. FT CHAIN 1..318 FT /note="Ubiquitin-like domain-containing CTD phosphatase 1" FT /id="PRO_0000242644" 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 BINDING 143 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9XZ16" FT BINDING 145 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9XZ16" FT BINDING 253 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9XZ16" SQ SEQUENCE 318 AA; 36800 MW; FC73F52A7B36668C CRC64; MSLSLIIKWG GQEYTITSLS EEDTVLDLKQ SLKGLTGVLP ERQKLLGLKM KGKPADDDVK LGALKLKPNT KIMMMGTREE SLEDVLGPPP DNDDVINDFD IEEEVVEVEN REENLLKISR RVKEYKVEIL NPPREGKKLL VLDVDYTLFD HRSCAETGVE LMRPYLHEFL TSAYEDYDIV IWSATNMKWI EAKMKELGVS TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS EYYSKKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELLKLTQY LKEIAKLDDF LELNHKHWER YLSKKQGQ //