ID A0A1U7UC77_CARSF Unreviewed; 1384 AA.
AC A0A1U7UC77;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 28-JAN-2026, entry version 41.
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_008066338.1};
OS Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC Carlito.
OX NCBI_TaxID=1868482 {ECO:0000313|Proteomes:UP000189704, ECO:0000313|RefSeq:XP_008066338.1};
RN [1] {ECO:0000313|RefSeq:XP_008066338.1}
RP IDENTIFICATION.
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_008066338.1; XM_008068147.2.
DR GeneID; 103270614; -.
DR CTD; 10869; -.
DR OrthoDB; 265776at2759; -.
DR Proteomes; UP000189704; Unplaced.
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; -; 2.
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 PRINTS; PR02045; F138DOMAIN.
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_008066338.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000189704};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
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 DOMAIN 113..202
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 383..485
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 600..1317
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 894..936
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..262
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..502
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1384 AA; 152196 MW; FC9C694F4CE19C30 CRC64;
MSGGASATGP RKGPPGLEEA TSKKKQKDRA NQESKDGDPR KETGSLYVAQ PGLELLASSD
PSASASQVAG ITGSHHHTHL FFSLSSGSVS TPQEEQIKEG SCADLCDLFA TSPTELLLDW
RQSAEEVIVK LHVGVGSLQL EEVDAAFTDT NCVLRFSGGR QWGGIFYAEI ESSCTKVQAR
KGGLLQLTLP KKVPMLTWPS LLKKPLGTQE LVPGLRCQEN GQELSPIALE PGPEPHRAKQ
EARNQKRAQG RGEVGSGAGP GAQAGPSAKR AVHLRRGPEG EGSRDGPGPR GDAPPFLADP
ATQVEAEEQL HIPQLNPQTC LLGSEENLAL LTGEKAVSPR NDLVSPGMAQ STDPGKDDHI
KEGMAVAADA ATLVDDPESM VNLAFVKNDS YEKGPDSVVV HVYVKEIRRD TSRVLFREQD
FTLIFQTRDG NFLRLHPGCG PHTIFRWQVK LRNLIEPEQC TFCFTASRID ICLRKRQSQR
WGGLEAPAAR GAVGGAKVAV PTGPTPLDPT PSGSASHPLT GQEEARAVEK DKPKARSEDT
GLDSVATRTS MEHVTAKPET HLASPKPTCM VPPMPHSPVS GDSVEEEEEE EKKVCLPGFT
GLVNLGNTCF MNSVIQSLSN TRELRDFFHD RSFEAEINYN NPLGTGGRLA IGFAVLLRAL
WKGTHHAFQP SKLKAIVASK ASQFTGYAQH DAQEFMAFLL DGLHEDLNRI QNKPYTETVD
SDGRPDEVVA EEAWQRHKMR NDSFIVDLFQ GQYKSKLVCP VCAKVSITFD PFLYLPVPLP
QKQKVLPVFY FAREPHSKPI KFLVSISKEN SSASEVLDSL SQSVHVKPEN LRLAEVIKNR
FHRVFLPSHS LDTVSASDTL LCFELLSPEL AKERVVVLEV QQRPQVPSVP ISKCAACQRK
QQSEEEKLKR CTRCYRVGYC NQLCQKTHWP DHKGLCRPEN IGYPFLVSVP ASRLTYARLA
QLLEGYARYS VSVFQPPFQP GRMALESQGP GCTMLLSSTS LEAGDSERDP VQPPELQLVT
PVAEGDTGIS RVWATPDRGT VPSTSGISSE MLASEPIEIG SLSAGERVSR PEAAVPGYQH
PSEVMNAHTP QFFIYKIDAS SREQRIEDKG ETPLELGDDC SLALVWRNNE RLQEFVLVAS
KELECAEDPG SAGEAARAGH FTLDQCLNLF TRPEVLAPEE AWYCPQCKQH REASKQLLLW
RLPNVLIVQL KRFSFRSFIW RDKINDLVEF PVRNLDLSKF CIGQKEEQLP SYDLYAVINH
YGGMIGGHYT ACARLPNDRS SQRSDVGWRL FDDSTVTTVD ESQVVTRYAY VLFYRRRNSP
VERPPRAGHS EHHPDLGPAA EAAASQGLGP GQAPEVAPTR TAPERFAPPV DRPAPTYSNM
EEVD
//
