ID E3TE20_ICTPU Unreviewed; 318 AA.
AC E3TE20;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Ubiquitin-like domain-containing CTD phosphatase 1 {ECO:0000256|ARBA:ARBA00014187};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE AltName: Full=Nuclear proteasome inhibitor UBLCP1 {ECO:0000256|ARBA:ARBA00032039};
GN Name=UBCP1 {ECO:0000313|EMBL:ADO28556.1};
GN Synonyms=ubcp1 {ECO:0000313|RefSeq:NP_001187369.1,
GN ECO:0000313|RefSeq:XP_017347266.1}, ublcp1
GN {ECO:0000313|RefSeq:NP_001187369.1,
GN ECO:0000313|RefSeq:XP_017347266.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:ADO28556.1};
RN [1] {ECO:0000313|EMBL:ADO28556.1, ECO:0000313|RefSeq:NP_001187369.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20634964; DOI=10.1371/journal.pone.0011546;
RA Chen F., Lee Y., Jiang Y., Wang S., Peatman E., Abernathy J., Liu H.,
RA Liu S., Kucuktas H., Ke C., Liu Z.;
RT "Identification and characterization of full-length cDNAs in channel
RT catfish (Ictalurus punctatus) and blue catfish (Ictalurus furcatus).";
RL PLoS ONE 5:E11546-E11546(2010).
RN [2] {ECO:0000313|RefSeq:NP_001187369.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27307075;
RA Zeng Q., Liu S., Yao J., Zhang Y., Yuan Z., Jiang C., Chen A., Fu Q.,
RA Su B., Dunham R., Liu Z.;
RT "Transcriptome Display During Testicular Differentiation of Channel Catfish
RT (Ictalurus punctatus) as Revealed by RNA-Seq Analysis.";
RL Biol. Reprod. 95:19-19(2016).
RN [3] {ECO:0000313|RefSeq:NP_001187369.1, ECO:0000313|RefSeq:XP_017347266.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017347266.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001512};
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:0000256|ARBA:ARBA00001482};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GU588600; ADO28556.1; -; mRNA.
DR RefSeq; NP_001187369.1; NM_001200440.1.
DR RefSeq; XP_017347266.1; XM_017491777.3.
DR RefSeq; XP_017347268.1; XM_017491779.1.
DR STRING; 7998.ENSIPUP00000014808; -.
DR Ensembl; ENSIPUT00000015430; ENSIPUP00000014808; ENSIPUG00000009968.
DR GeneID; 100528170; -.
DR KEGG; ipu:100528170; -.
DR CTD; 134510; -.
DR OMA; DSNAMIS; -.
DR OrthoDB; 49886at2759; -.
DR Proteomes; UP000221080; Chromosome 18.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADO28556.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 3..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 133..294
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT COILED 101..128
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 318 AA; 36650 MW; 091B569D0951D493 CRC64;
MSLSVIIKWG GQEYSISALS EDDTVLDLKQ SIKSLTGVLP ERQKLLGLKI RGKPADDGTK
LGLLKLKPNT KIMMMGSREE SLEDILAPPP ESDDVINDFD IEEEVIEVEN REENLAKIAR
RVKEYKVEEL NPPREGKRLL VLDVDYTLFD HKSCAETGQE LMRPFLHEFL ASAYEDYDIV
IWSATSMKWI DAKMKELGVS DNSNYKITFM LDSGAMITVH TPKRGVVEVK PLGVIWGKYG
EFYNRKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRER DKELLKLSHY LKEIAKLDDF
SALNHKHWER YLSKKQSQ
//
