ID A0A3Q0TDX5_AMPCI Unreviewed; 342 AA.
AC A0A3Q0TDX5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 46 {ECO:0000256|ARBA:ARBA00039415};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 46 {ECO:0000256|ARBA:ARBA00042431};
DE AltName: Full=Ubiquitin thioesterase 46 {ECO:0000256|ARBA:ARBA00041292};
DE AltName: Full=Ubiquitin-specific-processing protease 46 {ECO:0000256|ARBA:ARBA00042999};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000030342.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000030342.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC {ECO:0000256|ARBA:ARBA00038282}.
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DR AlphaFoldDB; A0A3Q0TDX5; -.
DR STRING; 61819.ENSACIP00000030342; -.
DR Ensembl; ENSACIT00000031134.1; ENSACIP00000030342.1; ENSACIG00000023483.1.
DR GeneTree; ENSGT00940000153284; -.
DR OMA; ANFGNTC; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR CDD; cd02663; Peptidase_C19G; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF714; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 46; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Behavior {ECO:0000256|ARBA:ARBA00022610}.
FT DOMAIN 7..341
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 115..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 39739 MW; 2315334378E8F887 CRC64;
MTVRNIASIC NMFGNTCYCN SVLQALYFCR PFRENVLAYK AQQKKKENLL TCLADLFHSI
ATQKKKVGVI PPKKFISRLR KENDLFDNYM QQDAHEFLNY LLNTVADILQ EEKKQEKQNG
RLKNNGTAVT TEAETENKTE PTWVHDIFQG TLTNETRCLN CETVSSKDED FLDLSVDVEQ
NTSITHCLRD FSNTETLCSE YKYYCETCCS KQEAQKRMRV KKLPMILALH LKRFKYMEQL
HRYTKLSYRV VFPLELRLFN TSGDAVNLDR MYDLVAVVVH CGSGPNRGHY ITIVKSHGFW
LLFDDDIVEK IDAQAIEEFY GLTSDISKNS ESGYILFYQS RE
//
