ID A0A3Q7RPE7_VULVU Unreviewed; 1361 AA.
AC A0A3Q7RPE7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 19 {ECO:0000256|ARBA:ARBA00071653};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 19 {ECO:0000256|ARBA:ARBA00081973};
DE AltName: Full=Ubiquitin thioesterase 19 {ECO:0000256|ARBA:ARBA00075186};
DE AltName: Full=Ubiquitin-specific-processing protease 19 {ECO:0000256|ARBA:ARBA00078778};
GN Name=USP19 {ECO:0000313|RefSeq:XP_025844106.1};
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:UP001652641, ECO:0000313|RefSeq:XP_025844106.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025844106.1}
RP IDENTIFICATION.
RC TISSUE=Cell line {ECO:0000313|RefSeq:XP_025844106.1};
RG RefSeq;
RL Submitted (AUG-2025) 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: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}.
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DR RefSeq; XP_025844106.1; XM_025988321.2.
DR GeneID; 112911665; -.
DR CTD; 10869; -.
DR Proteomes; UP001652641; Chromosome 9.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036503; P:ERAD pathway; IEA:TreeGrafter.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0031647; P:regulation of protein stability; IEA:UniProtKB-ARBA.
DR CDD; cd06466; p23_CS_SGT1_like; 1.
DR CDD; cd06463; p23_like; 1.
DR CDD; cd02674; Peptidase_C19R; 1.
DR FunFam; 3.90.70.10:FF:000012; ubiquitin carboxyl-terminal hydrolase 19 isoform X2; 1.
DR FunFam; 3.90.70.10:FF:000020; ubiquitin carboxyl-terminal hydrolase 19 isoform X4; 1.
DR FunFam; 2.60.40.790:FF:000004; ubiquitin carboxyl-terminal hydrolase 19 isoform X9; 1.
DR FunFam; 6.10.140.2220:FF:000004; ubiquitin carboxyl-terminal hydrolase 19 isoform X9; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR050185; Ub_carboxyl-term_hydrolase.
DR InterPro; IPR028889; USP.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF74; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16602; USP19_linker; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 2.
DR PROSITE; PS51203; CS; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801,
KW ECO:0000313|RefSeq:XP_025844106.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP001652641};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT TRANSMEM 1334..1355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..141
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 323..425
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 540..1257
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 834..876
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..200
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..442
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 150223 MW; FE5FC3308EE9ACE9 CRC64;
MSGGASATGP RRGPPGLEEA TSKKKQKDRA NQESKDGDPR RGSASSREEQ AKEELLLDWR
QSADEVIVKL RVGAGPLRLE EVDAAFTDTD CVVRLPGGRQ WGGVFYAEIE SSCTKVQARK
GGLLQLALPK KVPLLTWPSL LKPLGTQEVV PGLRCQENGQ EPSPIALEPG PEPRRAKQEA
RNQKRAQGRG EVGAGAGPGA QAGPSAKRAV HLRRGPEGEG SRDGPGPRGD APPFLAETAT
QAEAEEQLRV PPLNPQTCLL GSEENLALLA GEKTVSPRND PVSPAMARSR DPEKGDRSKE
EMAVAADAVT LVDGKEPESM VNLAFVKNDS YEKGPDSVVV HVYVKEIRRD TSRVLFREQD
FTLIFQTRDG NFLRLHPGCG PHTLFRWQVK LRNLIEPEQC TFCFTASRID ICLRKRQSQR
WGGLEAPAAR GAVGGAKVAV PTGPTPLDSA PPGGTPHPLT GQEEARAVEK EKPKPRSEDT
GLDGVAARTP MEHVAPKPEP HLASPKPTCM VPPMPHSPVS GDSVEEEEEE EKKVCLPGFT
GLVNLGNTCF MNSVIQSLSN TRELRDFFHD RSFETEINYN NPLGTGGRLA IGFAVLLRAL
WKGTHHAFQP SKLKAIVASK ASQFTGYAQH DAQEFMAFLL DGLHEDLNRI QNKPYTETVD
SDGRPDEVVA EEAWQRHKMR NDSFIVDLFQ GQYKSKLVCP VCAKVSITFD PFLYLPVPLP
QKQKVLPVFY FAREPHSKPI KFLVSISKEN SSASEVLDSL SQSVHVKPEN LRLAEVIKNR
FHRVFLPSHS LDTVSPSDTL LCFELLSPEL AKERVVVLEV QQRPQVPSIP ISKCAACQRK
QQSEDEKLKR CTRCYRVGYC NQLCQKTHWP DHKGLCRPEN IGYPFLVSVP ASRLTYARLA
QLLEGYARYS VSVFQPPFQP GRMALESQGP GCTTLLSTSS LEAGDSERDP IQPPELQLVT
PVAEGDTGVP RAWAAPDRGP VPSTSGVSSE VLASGPVEVG SLPAGERVSR PEAAVPGYQH
PSEAMNAHTP QFFIYKIDAS NREQRLEDKG DTPLELGEDC SLALVWRNNE RLQEFVLVAS
KELECAEDPG SAGEAARAGH FTLDQCLNLF TRPEVLAPEE AWYCPQCKQH REASKQLLLW
RLPNVLIVQL KRFSFRSFIW RDKINDLVEF PVRNLDLSKF CIGQKEEQLP SYDLYAVINH
YGGMIGGHYT ACARLPNDRS SQRSDVGWRL FDDSTVTTVD ESQVVTRYAY VLFYRRRNSP
VERPPRAGHS EHHPDLGPAA EAAASQASRI WQELEAEEEP VPEGPVPLGP WGPQDWVGPP
PRGPTTPDEG CLRYFVLGTV AALVALVLNV FYPLVSQSRW R
//
