ID A0A8C6VD41_NAJNA Unreviewed; 1332 AA.
AC A0A8C6VD41;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=USP19 {ECO:0000313|Ensembl:ENSNNAP00000004043.1};
OS Naja naja (Indian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=35670 {ECO:0000313|Ensembl:ENSNNAP00000004043.1, ECO:0000313|Proteomes:UP000694559};
RN [1] {ECO:0000313|Ensembl:ENSNNAP00000004043.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSNNAP00000004043.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSNNAT00000004230.1; ENSNNAP00000004043.1; ENSNNAG00000001936.1.
DR GeneTree; ENSGT00940000159085; -.
DR OrthoDB; 265776at2759; -.
DR Proteomes; UP000694559; Unplaced.
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 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; 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; 2.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000694559};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT TRANSMEM 1305..1326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..135
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 265..367
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 481..1229
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 775..817
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 163..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 149479 MW; 8EC4DCC5C376CB0A CRC64;
MSSSASVPGQ RRTARGVDDA TNKKKQKDRA NQESKEGEKP AGSDLKKDLQ LEWKQNADEV
IVKLNLGSRN PKVEEVDSSF TDTNCVIKLP DGRQWSCEFY EEIESSCTKV QFKKGNILQL
VLPKKIPLHS WASLSKGLSA GGTSEEPPLD STVELIRSKR EPSNPKRILG KNDTVGGRNL
INPRLPTGPG TKAACIKASL SEEERNSRSM GSPGLSGITD RQRTDQVAEG ASQLDLKVRN
KGVSYSHCRY CFIFFLLEPE PIVNLTFVKN DSYEKGNDSM VVHVYVKEIH KEMSSVHFRE
QDFTLMFQTS DANFLRLHQG CSAHSVFRWQ VKLRNLIEPD QCTYNFTTAR INICLKKRHS
QRWGGLEAPA TRGAVGGAKV AMPTGPTPLD KSQPGSNQHP LSTKEEARAV EKEKPRAEDS
GLDSVAARTV SDHLPVKQEP LVPSPKPTCM VPPMTHSPVS NESVEEEEEE EDKKVCLPGF
TGLVNLGNTC FMNSVIQSLS NTRELRDYFH DRSFESEINY SNPLGTGGRL AIGFAVLLRA
LWKGTHHAFQ PSKLKAIVAS KASQFTGYAQ HDAQEFMAFL LDGLHEDLNR IQNKPYTETV
DSDGRPDEVV AEEAWQRHKM RNDSFIVDLF QGQFKSKLVC PVCSKVSITF DPFLYLPVPL
PQKQKVLTVY YFAKEPHNKP VKFLVSISKE NSTAMEVLDS VSHSVRVNSE NLRLAEVIKN
HFHRMFLPSQ SLDAVSPTDL LLCFEVLSPE LAKERVVELQ VQQRPQVPSI PITKCAACQK
KQQSDEEKLK RCTRCYRVGY CNVVCQRTHW SNHKTLCRPE NIGFPFLISI PESRLTYARL
AQLLEGYARY SVSVFQPPFQ VGRMPSEQGL PLLSSEKQEP PVRSSCATVG SAAAAAAAVE
TSAMESGDGA RAPHLLQEPQ PSLSAPELQP ELGDASTFRS KVPTGRSSGL SLDSGYSESS
AESQLESCLE RELPYERVPR PEAAIPGYQH PAEGLSSQVT QFYINKIDAT SKEQKLEDKG
ENAPLDLTDD CSLALVWKNN ERMKEFVLVE SKELECVEDP GSASEAARAG HFTLEQCLNL
FTKPEVLAPE EAWYCPKCKQ HREASKQLML WRLPNILIIQ LKRFSFRSFI WRDKINDMVD
FPVRSLDLSK FCIGQKDEQQ LPMYDLYAVI NHYGGMIGGH YTAYARLPSD KNSQRSDVGW
RLFDDSTVTT VDESQVVTRY AYVLFYRRRN SPVDRPPRGP PRPSDPRGDL APSAEAAASQ
ASLLWQELEA EEDAARRLMR NPWRSCSQRT RKLSSECPDE GHVRYFVLGT MAAIVALFLN
VFYPLIYQTR WR
//
