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Database: UniProt
Entry: G3W9V9_SARHA
LinkDB: G3W9V9_SARHA
Original site: G3W9V9_SARHA 
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
//
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