ID G3U7X1_LOXAF Unreviewed; 597 AA.
AC G3U7X1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=OTUD7B {ECO:0000313|Ensembl:ENSLAFP00000023929.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000023929.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000023929.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023929.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000023929.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023929.1};
RG Ensembl;
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}.
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DR AlphaFoldDB; G3U7X1; -.
DR STRING; 9785.ENSLAFP00000023929; -.
DR Ensembl; ENSLAFT00000037447.1; ENSLAFP00000023929.1; ENSLAFG00000026624.1.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000159172; -.
DR HOGENOM; CLU_013263_1_1_1; -.
DR InParanoid; G3U7X1; -.
DR OMA; GHRAFRM; -.
DR TreeFam; TF323312; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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:1990380; F:K48-linked deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002385; P:mucosal immune response; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd22772; OTU_OTUD7B; 1.
DR Gene3D; 1.20.5.4770; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF8; OTU DOMAIN-CONTAINING PROTEIN 7B; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 1.
DR SMART; SM00259; ZnF_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:UP000007646};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00451}.
FT DOMAIN 119..301
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 550..585
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 66732 MW; BAB8FDAACBF41DF6 CRC64;
TPEKGFSDRE STRPPRPTLQ RQDDIVQEKR LSRGISHASS SIVSLARSHV SSNGGGGGSN
EHPLEMPICA FQLPDLTVYN EDFRSFIERD LIEQSMLVAL EQAGRLNWWA SVDPTCQRLL
PLATTGDGNC LLHAASLGMW GFHDRDLMLR KALYALMEKG VEKEALKRRW RWQQTQQNKE
SGLVYTEDEW QKEWNELIKL ASSEPRMHLG TNGANCGGVE SSEEPVYESL EEFHVFVLAH
VLRRPIVVVA DTMLRDSGGE AFAPIPFGGI YLPLEVPANQ CHRSPLVLAY DQAHFSALVS
MEQKENTKEQ GAESVSVPHV SWSALFSLGK IEMRKELSNM QALTVHVDTG LLSWKTHQNC
FKGFKIKKKS LGENMVACSP SSGGHRAFRM MLRYTQLNDF EFSEYILIGK CLVGSHGDQW
PKLYAGWLEK QACLVFNPRN NRFFTGYPGG LVSIGVSGSG NQQKKNPRRQ LAGSIGGGLP
PYATFPQTPP GRPYPHQDSN PSLEPGSHSK DGVHRGALLP PPFRVADSYS NGYREPPEPD
GWTGGPRGLP PTQTKCKQPN CSFYGHPETN NFCSCCYREE LRRREREPGG ELLVHRF
//
