ID G3W9V9_SARHA Unreviewed; 792 AA.
AC G3W9V9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:ENSSHAP00000012214.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000012214.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000012214.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000012214.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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_012404819.1; XM_012549365.1.
DR AlphaFoldDB; G3W9V9; -.
DR STRING; 9305.ENSSHAP00000012214; -.
DR Ensembl; ENSSHAT00000012313.2; ENSSHAP00000012214.1; ENSSHAG00000010469.2.
DR GeneID; 100919524; -.
DR CTD; 7128; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158448; -.
DR HOGENOM; CLU_019606_0_0_1; -.
DR InParanoid; G3W9V9; -.
DR OMA; NAKCSGY; -.
DR OrthoDB; 2909231at2759; -.
DR TreeFam; TF323312; -.
DR Proteomes; UP000007648; 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; 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 Protease {ECO:0000256|ARBA:ARBA00022807};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00451}.
FT DOMAIN 93..264
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 382..417
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 470..505
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 598..633
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 648..683
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 758..792
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 547..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 90828 MW; 9FC0B1EC90B6E260 CRC64;
MAEQQVLPQA LYLSNMRKAV KIRERTPEDI IKPTNGIIYH FKTMHRYTME MFRTCQFCPQ
FREFILVALI DRSIQNSLEN QRKLNWCREV RKLVALKTNG DGNCLMHATS QYMWGVQDTD
LVLRKALYST LKETDIRNFK FRWQLESLKS QEFVETGLRY DTRNWNEEWD NLIKMASTDT
SVARGGLQYH SLEEIHVFVL SNILRRPIII IADKMLRSLE SGSNFAPLKV GGIYLPLHWP
AQECYRYPIV LGYDSQHFAP LVTLKNSGPE IRAVPLVHRE KGRFEDLKVH FLTEPEAEMK
EKLLKEYLTV VEIPVQGWDH GTIHLINAAK LDEANLPKEI NLVEDYFELV QHEYKKWQEN
TELNHGEAHA RNGLEPHLPQ FSLMEVKCET PNCPFFMSVN TQPFCHECFE RRQNTQNKPR
KQNSKPGVEK LKGIGLGEAC EPTGWKPEEL PAMGPHSAPP TAPSLFLFSE TTAMKCKNPG
CPFTLNVQHN GFCERCHNTR QLNPGCDLSN HRHLDTGKCQ ACHQDVTRTF NGICSTCFKR
TTESSPITSS SFPPSCHQRS FSDPSQLSQS IHQHPCHRTG HEAASGTISQ SGRNLENRTG
TSKCRKAGCM YFGTPENQGF CTLCFIEYRE NKRDLPASGQ TDPSASRFQN AIPCLGRECG
TLGSTLFEGY CQKCFIEAQN LRFREAKRTE EQLVRQSERS NQCRDIQRTI QSSQRKKCAK
ATCKNFVAHR GEELCPECQR HNQRLGPGIP RGEPIKEEVP KQRCRAPACD HFGNTKCNGY
CNECYQFKQL YG
//