ID A0A3Q0DEI4_MESAU Unreviewed; 934 AA.
AC A0A3Q0DEI4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=Otud7a {ECO:0000313|RefSeq:XP_021091183.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021091183.1};
RN [1] {ECO:0000313|RefSeq:XP_021091183.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_021091183.1}
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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 RefSeq; XP_021091183.1; XM_021235524.1.
DR AlphaFoldDB; A0A3Q0DEI4; -.
DR STRING; 10036.ENSMAUP00000004668; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd22773; OTU_OTUD7A; 1.
DR CDD; cd14347; UBA_Cezanne_like; 1.
DR Gene3D; 1.20.5.4770; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF9; OTU DOMAIN-CONTAINING PROTEIN 7A; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00451}.
FT DOMAIN 201..384
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 892..927
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 461..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 101787 MW; D99B068C79DD81D0 CRC64;
MVSSLLPNPP SAECWAVLLH DPMTLDMDAV LSDFVRSTGA EPGLARDLLE GKNWDLTAAL
SDYEQLRQVH TANLPHVFNE GRCAKQPDRE LPQPGHKVER PCLQRQEEIA QAEKRLSRGI
SHASSAIVSL ARSHVANECN NEQFPLEMPI YTFQLPDLSV YSEDFRSFIE RDLIEQATMV
ALEQAGRLNW WSTVCTSCKR LLPLATTGDG NCLLHAASLG MWGFHDRDLV LRKALYTMMR
TGAEREALKR RWRWQQTQQN KESGLVYTEE EWEREWTELL KLASSEPRTH LSKNGSGTGG
GVDNSEDPVY ESLEEFHVFV LAHILRRPIV VVADTMLRDS GGEAFAPIPF GGIYLPLEVP
PNRCHCSPLV LAYDQAHFSA LVSMEQRDQQ REQAVIPLTD SEHKLLPLHF AVDPGKDWEW
GKDDNDNARL AHLILSLEAK LNLLHSYMNV TWIRIPSETR APLAQPESPT ASAGEDVQSL
TESLDSDRDS VCSNSNSNNG KNGKDKEKEK PRKDKDKTRA DSVANKLGSF SKTLGIKLKK
NMGGLGGLVH GKMGRANSAN GKNGDGNERS KEKKSKSRKG SKEDSGASAS TSPSEKTTPS
PTDKAAGASP ADKGSGPRSD AWKYSTDVKL SLNILRAAMQ GERKFIFAGL LLTSHRHQFH
EEMIGYYLTS AQERFSAEQE QRRRDAAAAA ATATATATTK RPARRPEAEG PPGPERASPG
PPAAPPTQLV LKLKERPSPG TGVNARATRA VGGAASPGPG GGTRRAGTGT GGPAPGRSPP
APARQSVIHV QAAARDEACA PAVGALRPCA TYPQQNRSLW SQSYSPARGA LRTVNTVESL
APGGGDSPGP AEQKSQTYSN GFSAARGDGL EFADADAPVA RSNAECARGG PGPAQRRCQR
ENCAFYGRAE TEHFCSYCYR EELRRRREAR AARP
//
