ID G3UHZ3_LOXAF Unreviewed; 790 AA.
AC G3UHZ3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=TNFAIP3 {ECO:0000313|Ensembl:ENSLAFP00000027451.1};
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:ENSLAFP00000027451.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000027451.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027451.1,
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:ENSLAFP00000027451.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027451.1};
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 RefSeq; XP_003404055.1; XM_003404007.2.
DR AlphaFoldDB; G3UHZ3; -.
DR STRING; 9785.ENSLAFP00000027451; -.
DR MEROPS; C64.003; -.
DR Ensembl; ENSLAFT00000027333.1; ENSLAFP00000027451.1; ENSLAFG00000011428.3.
DR GeneID; 100670852; -.
DR KEGG; lav:100670852; -.
DR CTD; 7128; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158448; -.
DR InParanoid; G3UHZ3; -.
DR OMA; NAKCSGY; -.
DR OrthoDB; 2909231at2759; -.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001922; P:B-1 B cell homeostasis; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0072666; P:establishment of protein localization to vacuole; IEA:Ensembl.
DR GO; GO:0050869; P:negative regulation of B cell activation; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:2000349; P:negative regulation of CD40 signaling pathway; IEA:Ensembl.
DR GO; GO:0002677; P:negative regulation of chronic inflammatory response; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0070429; P:negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; IEA:Ensembl.
DR GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; IEA:Ensembl.
DR GO; GO:0034148; P:negative regulation of toll-like receptor 5 signaling pathway; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0002634; P:regulation of germinal center formation; IEA:Ensembl.
DR GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0072573; P:tolerance induction to lipopolysaccharide; IEA:Ensembl.
DR CDD; cd22766; OTU_TNFAIP3; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR Gene3D; 4.10.240.30; -; 4.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF3; TUMOR NECROSIS FACTOR ALPHA-INDUCED PROTEIN 3; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 5.
DR SMART; SM00259; ZnF_A20; 7.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 5.
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 92..263
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 381..416
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 472..507
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 601..636
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 651..686
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 756..790
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 545..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 89707 MW; 7118F16540EB8E34 CRC64;
MAEQLLPLAL YLSNMRKAVK IRERTPEDIF KPTNGIIHHF KTMHRYTLEM FRTCQFCPQF
REIIHKALID RNTQASLESQ RKLNWCREVR KLVALKTNGD GNCLMHAVSQ YMWGVQDTDL
VLRKALFSAL KETDTRNFKF RWQLESLKSQ EFVETGLCYD TRNWNDEWDN LIKMASTDTP
GARVGFQYHS LEEIHIFVLC NILRRPVIVI SDKMLRSLES GSNFAPVKVG GIYLPLHWPA
KECYRYPIVL GYDSQHFVPL VTLKDSGPEI RAVPLVNRDR GRFEDLKVHF LTDPENEMKE
KLLKEYLMVI EIPVQGWDVG TTHLINAAKL DEANLPKEIN LVDDYFELVQ HEYKKWQENN
QQGRREAHAP NPLEPSVPQL SLMDVKCETP NCPFFMSVNT QPLCHECSER WQKNKNKPPK
LNSKPGPEVL PGMALGAPRG EACEPLVWIP EEPAGGPHSA PPTAPSLFLF SETTAMKCRT
PGCPFTLNVQ HNGFCERCHN ARQLNTSRNV DSTRHLDPGK CRACLQDATR TFNGICSTCF
KRTTTETSSS LGPTVPSSCH QRSKSDPSQL IQSLSPHSCH RAGSEAQAGC LSQAARTPED
RTGTSKCRKA GCMYFGTPEN KGFCTLCFIE YKENKYFVAA LGKANSTAPR FQNAVPCLGR
ECGTLGSTMF EGYCQKCFIE AQNQRFHEAK RTEEQLRSSQ RRDVLRTTQS SSRPKCARAS
CKNILACCSE ELCMECQRRS QRTVPAPHRG EPAPDESPKQ RCRAPACEHF GNAKCSGYCN
ECFQFKQMYG
//
