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Database: UniProt
Entry: H9FW52_MACMU
LinkDB: H9FW52_MACMU
Original site: H9FW52_MACMU 
ID   H9FW52_MACMU            Unreviewed;      1048 AA.
AC   H9FW52;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:AFE78861.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE78861.1};
RN   [1] {ECO:0000313|EMBL:AFE78861.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE78861.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
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; JU335108; AFE78861.1; -; mRNA.
DR   AlphaFoldDB; H9FW52; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
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   PROSITE; PS50802; OTU; 1.
PE   2: Evidence at transcript level;
FT   DOMAIN          1..90
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   REGION          257..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          848..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..986
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  117006 MW;  EB3BE57E0D075D1D CRC64;
     MACIHYLREN REKFEAFIEG SFEEYLKRLE NPQEWVGQVE ISALSLMYRK DFIIYREPNV
     SPSQVTENNF PEKVLLCFSN GNHYDIVYPI KYKESSAMCQ SLLYELLYEK VFKTDVSKIV
     MGLDTLEVAD EDNSEISDSE DDSCKSKTAA AADVNGFKPL SDNEQLKNNG NSTSLPLSRK
     VLKSLNPSVY RNVEYEIWLK SKQAQQKRDY SIAAGLQYEV GDKCQVRLDH NGKFLNADVQ
     GVHSENGPVL VEELGKKHTS KNLKAPPPES WNTVSGKKMK KPSTSGQNFH SDMDYRGPKN
     PSKPIKAPSA LPPRLQHPSG VRQHAFSSHS SGSQSQKFSS EHKNLSRTPS QIIRKPDRER
     VEDFDHTSRE SNYFGLSPEE RREKQAIEES RLLYEIQNRD EQAFPALSSS SVSQSASQSS
     NPCVQRKSSH VSDRKGSRRR MDTEERKDKD SIHGHSQLDK KPEPSTLENI TDDKYATVSS
     PSKSKKLECP SPAEQKPAEH VSLSNPAPLL VSPEVHLTPA VPSLPATVPA WPSEPTTFGP
     TGVPAPIPVL SVTQTLTTGP DSAVSQAHLT PSPVPVSIQA VNQPLMPLPQ TLSLYQDPLY
     PGFPCNEKGD RAIVPPYSLC QTGEDLPKDK NILRFFFNLG VKAYSCPMWA PHSYLYPLHQ
     AYLAACRMYP KVPVPVYPHN PWFQEAPAAQ NESDCTCTDA HFPMQTEASV NGQMPQPEIG
     PPTFSSPLVI PPSQVSESHG QLSYQADLES ETPGQLLHAD YEESLSGKNM FPQPSFGPNP
     FLGPVPIAPP FFPHVWYGYP FQGFIENPVM RQNIVLPSDE KGELDLSLEN LDLSKDCGSV
     STVDEFPEAR GEHVHSLPEA SVSSKPEEGR TEQSSQTRKA DMALASVPPV AEGKAHPPTQ
     ILNRERETVP VELEPKRTIQ SLKEKTEKVK DPKTAADVVS PGANSVDSRV QRPKEESSED
     ENEVSNILRS GRSKQFYNQT YGSRKYKSDW GYSGRGGYQH VRGEESWKGQ PSRSRDEGYQ
     YHRNVRGRPF RGDRRRSGMG DGHRGQHT
//
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