ID G3QLD1_GORGO Unreviewed; 790 AA.
AC G3QLD1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 72.
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:ENSGGOP00000003280.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000003280.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000003280.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000003280.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000003280.3}
RP IDENTIFICATION.
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 EMBL; CABD030048040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004044791.1; XM_004044743.2.
DR RefSeq; XP_018885553.1; XM_019030008.1.
DR AlphaFoldDB; G3QLD1; -.
DR STRING; 9593.ENSGGOP00000003280; -.
DR MEROPS; C64.003; -.
DR Ensembl; ENSGGOT00000003354.3; ENSGGOP00000003280.3; ENSGGOG00000003334.3.
DR GeneID; 101149274; -.
DR KEGG; ggo:101149274; -.
DR CTD; 7128; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158448; -.
DR HOGENOM; CLU_019606_0_0_1; -.
DR InParanoid; G3QLD1; -.
DR OMA; NAKCSGY; -.
DR OrthoDB; 2909231at2759; -.
DR TreeFam; TF323312; -.
DR Proteomes; UP000001519; Chromosome 6.
DR Bgee; ENSGGOG00000003334; Expressed in testis and 5 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
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:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
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:0030177; P:positive regulation of Wnt signaling pathway; IBA:GO_Central.
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; 1.20.5.4770; -; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR Gene3D; 4.10.240.30; -; 3.
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; 4.
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:UP000001519};
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 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 89678 MW; 10C837E375622E76 CRC64;
MAEQVLPQAL YLSNMRKAVK IRERTPEDIF KPTNGIIHHF KTMHRYTLEM FRTCQFCPQF
REIIHKALID RNIQATLESQ KKLNWCREVR KLVALKTNGD GNCLMHATSQ YMWGVQDTDL
VLRKVLFSTL KETDTRNFKF RWQLESLKSQ EFVETGLCYD TRNWNDEWDN LIKMASTDTP
MARSGLQYNS LEEIHIFVLC NILRRPIIVI SDKMLRSLES GSNFAPLKVG GIYLPLHWPA
QECYRYPIVL GYDSHHFVPL VTLKDSGPEI RAVPLVNRDR GRFEDLKVHF LTDPENEMKE
KLLKEYLMVI EIPVQGWDHG TTHLINAAKL DEANLPKEIN LVDDYFELVQ HEYKKWQENS
EQGRREGHAQ NPMEPSLPQL SLMDVKCETP NCPFFMSVNT QPLCHECSER RQKNQNKLPK
LNSKPGPEGL PGMALGASRG EAYEPLAWNP EESTGGPHSA PPTAPSPFLF SETTAMKCRS
PGCPFTLNVQ HNGFCERCHN ARQLHASHAP DHTRHLHPGK CQACLQDVTR TFNGICSTCF
KRTTAEATSS LSTSLPPSCH QRSKSDPSQL IRSPSPHSCH RAGNDAPAGC LSQAARTPGD
RTGTSKCRKA GCVYFGTPEN KGFCTLCFIE YRENKHFAAA SGKVSPTASR FQNTIPCLGR
ECGTLGSTMF EGYCQKCFIE AQNQRFHEAK RTEEQLRSSQ RRDVPRTTQS TSRPKCARAS
CKNILACRSE ELCMECQHPN QRMGPGAHRG EPAPEDPPKQ RCRAPACDHF GNAKCNGYCN
ECFQFKQMYG
//
