ID A0A3Q7TIW2_VULVU Unreviewed; 915 AA.
AC A0A3Q7TIW2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP20 {ECO:0000313|RefSeq:XP_025865286.1,
GN ECO:0000313|RefSeq:XP_025865287.1, ECO:0000313|RefSeq:XP_025865288.1,
GN ECO:0000313|RefSeq:XP_025865289.1, ECO:0000313|RefSeq:XP_025865291.1,
GN ECO:0000313|RefSeq:XP_025865292.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025865286.1};
RN [1]
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025865287.1,
RC ECO:0000313|RefSeq:XP_025865288.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025865287.1,
RC ECO:0000313|RefSeq:XP_025865288.1};
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025865286.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025865286.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025865286.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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 ECO:0000256|RuleBase:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
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DR RefSeq; XP_025865286.1; XM_026009501.1.
DR RefSeq; XP_025865287.1; XM_026009502.1.
DR RefSeq; XP_025865288.1; XM_026009503.1.
DR RefSeq; XP_025865289.1; XM_026009504.1.
DR RefSeq; XP_025865291.1; XM_026009506.1.
DR RefSeq; XP_025865292.1; XM_026009507.1.
DR STRING; 9627.ENSVVUP00000038468; -.
DR Ensembl; ENSVVUT00000050439; ENSVVUP00000038465; ENSVVUG00000027434.
DR Ensembl; ENSVVUT00000050442; ENSVVUP00000038468; ENSVVUG00000027434.
DR KEGG; vvp:112927978; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 6..111
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 145..686
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 688..781
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 790..893
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 259..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 102273 MW; 244E8E65969BD170 CRC64;
MGDSRDFCPH LDSIGEVTKE DLLFKSKGAC QSCGVTGPNL WACLQVACPY VGCGESFADH
STIHAQAKKH NLTVNLTTFR VWCYACEKEV FLEQRLAAHP AGPSPRFSEQ DSPLPSHPLK
AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV
RTDKKPALCK SYQKLVSEVW HRRRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLCCLM
DQLHEELKEP VVAAAAALVE TRDSDSSDTD EKREGDRSPS EDEFLSCDSS SDRGEGDGQG
HGGGGSQAEA ELLIPDEAGR AISEKERMKD RKFSWGQQRT SSEQVDEDAD VDTAMAALDD
QPSEAQPPSL QSPSPSRTPE PDNEAHMWST SRPCSPVHHH EGHTKLASSP PRASPVRMGP
SYVLKKAQVL SAGSRRRKEQ RYRSVISDIF DGSILSLVQC LTCDRVSTTV ETFQDLSLPI
PGKEDLARLH SAIYQNVPAK PGACGDSYAA QGWLAFIMEY IRRFLVSCTP SWFWGPVVTL
EDCLAAFFVA DELKGDNMYS CERCKKLRNG VKYCKVLRLP EILYIHLKRF RHEVMYSFKI
SSHVSFPLEG LDLRPFLAKE CTSQITTYDL LSVICHHGTA GSGHYIAYCQ NVINGQWYEF
DDQYVTEVHE TVVQSAEAYV LFYRKSSEEA VRERQQVVSL AAMREPSLLR FYVSREWLNK
FNTFAEPGPI TNHTFLCSHG GIPPHKYHYI DDLVVILPQN VWEHLYNRFG GGPAVNHLYV
CSICQVEIEA LAKRRQIEID TFIKLNKAFQ AEESPSVIYC ISMQWFREWE AFVKGKDNEP
PGPIDNSRIA QVKGSGHIQL KQGADYGQIS EETWVYLNNL YGGGPEVAIR QSVAQLQDPE
SLHGEQKIEA ETRAV
//
