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UBCP1_CHICK
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   03-AUG-2022, entry version 101.
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=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. 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; 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.ENSGALP00000040691; -.
DR   PaxDb; Q5ZJJ8; -.
DR   Ensembl; ENSGALT00000005818; ENSGALP00000005808; ENSGALG00000003672.
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; 1376145at2759; -.
DR   PhylomeDB; Q5ZJJ8; -.
DR   TreeFam; TF323786; -.
DR   PRO; PR:Q5ZJJ8; -.
DR   Proteomes; UP000000539; Chromosome 13.
DR   Bgee; ENSGALG00000003672; Expressed in spermatid and 13 other 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: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_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   REGION          133..294
FT                   /note="Phosphatase"
FT                   /evidence="ECO:0000250"
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
 
 
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