ID Q0IHU0_XENTR Unreviewed; 1051 AA.
AC Q0IHU0;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=otud4 {ECO:0000313|EMBL:AAI22972.1,
GN ECO:0000313|RefSeq:NP_001072598.1,
GN ECO:0000313|Xenbase:XB-GENE-5900161};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI22972.1};
RN [1] {ECO:0000313|RefSeq:NP_001072598.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI22972.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testes {ECO:0000313|EMBL:AAI22972.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001072598.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
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DR EMBL; BC122971; AAI22972.1; -; mRNA.
DR RefSeq; NP_001072598.1; NM_001079130.1.
DR MEROPS; C85.002; -.
DR GeneID; 780053; -.
DR KEGG; xtr:780053; -.
DR AGR; Xenbase:XB-GENE-5900161; -.
DR CTD; 54726; -.
DR Xenbase; XB-GENE-5900161; otud4.
DR OMA; FFPPVWY; -.
DR OrthoDB; 5406292at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd22794; OTU_OTUD4; 1.
DR CDD; cd20448; Tudor_OTUD4; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12419:SF9; OTU DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000008143}.
FT DOMAIN 28..149
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 278..338
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 346..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1051 AA; 117068 MW; E704431184DBB825 CRC64;
MDGQGGKGTV AHSKDEAAMD SYLRSEGLYR KKIAKDGSCL FRAVAEQVMH SQSEHLKIRK
SCINYLRKNR GQYEALIEGS FEDYLKSLEN PQEWVGQVEI SALSLMFKKD FIIYQEPNVP
PACVTENGFS EKIMLCFSNG NHYDIIYPIG FAESAAMCQS IIYELLYEKV MGVNVGKYMV
EQDTCGPNAT GEVYCSDGSG SEGEDVSKNI KTNFADMNGF KPHKDDKCPQ KKKEEPTMLP
SVLRSLHTTQ YRNVEYEVWL KTQRDQQKLD FSIAAGMQYS VGDKCQVRVE PGGKFYNAHI
QEVGTETGPV IVFVEELGEK HAVQLKHLKP IPQTIISTEG WNTVAGKKQK KALPSGTNAQ
TEKDYRGQKG FGKPVKQQAA QPLRQQQAAG NKQYGLSSQL SDQAPQSENK GRSKTPPKVP
GRKVERERSE NVTFGLTVEE RKEKEAIEES KSLYEMQSMD KDAFPALSSL PIGERAVQNT
EVFPVKRIPN VITENTRRKS EGEDQRDKAS TAQATKGRDQ KCCDETVKQL TSSDADDLPS
MPVLRTSAEH QASPIVPSTP SVVTSWPGIP AQIPSMSATG SDSSVLQPQV TSSPYPPLPV
SVPAVNQPLL PLPQTLSALQ DPLYPGFPLN EKGERATVPS YSFCKNGGDL PDDKSILRFF
FNLGLKAYTY PMWPPHTHLY PLHQAYLNMC RMYPNIPVYP QGSWVQETSE NQSEVDPSLL
SHPSEVRMES QGSQPLTVSS SPVQVPGIVG QIPNQSESGV INQALHTNVD FEDPATSKTI
FPQPPFAQSS YMGAVPIATP YFPHFWYGYP YQGYIESPVI RHNVYIPPQD RDLPENLSSE
AVENNSSNQI AIRQSLDLQE QCKPDLPLAS STGGTSSELI SNASTVQSEQ RMNVNIPQVL
TGHKSLPSKM KDNLVPPLAS TPIETKETAY GSSEDKERSE VNAVALGSTQ ANVSEEKALR
AREESSEDER EVSNMLSSGR SKNFYSQSYS TRRPRSEKYY QPNRGGYQHP RGEEGWRGQR
GRDDGFQHHR SYRGRPYRRR PMGDSYRAQQ E
//
