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Database: UniProt
Entry: H2UMF0_TAKRU
LinkDB: H2UMF0_TAKRU
Original site: H2UMF0_TAKRU 
ID   H2UMF0_TAKRU            Unreviewed;       369 AA.
AC   H2UMF0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 71.
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};
GN   Name=usp46 {ECO:0000313|Ensembl:ENSTRUP00000038121.1};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000038121.1, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000038121.1, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000038121.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_003973892.1; XM_003973843.2.
DR   AlphaFoldDB; H2UMF0; -.
DR   STRING; 31033.ENSTRUP00000084495; -.
DR   MEROPS; C19.052; -.
DR   Ensembl; ENSTRUT00000038258.3; ENSTRUP00000038121.1; ENSTRUG00000014912.3.
DR   GeneID; 101072192; -.
DR   KEGG; tru:101072192; -.
DR   CTD; 64854; -.
DR   eggNOG; KOG1864; Eukaryota.
DR   GeneTree; ENSGT00940000153284; -.
DR   OrthoDB; 227085at2759; -.
DR   TreeFam; TF314144; -.
DR   Proteomes; UP000005226; Chromosome 20.
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; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Behavior {ECO:0000256|ARBA:ARBA00022610};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT   DOMAIN          35..368
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          142..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  42586 MW;  B2E64B38FC4A6441 CRC64;
     MTVRNIASIC NMGTNASALE KDIGPEQFPI NEHYFGLVNF GNTCYCNSVL QALYFCRPFR
     ENVLAYKAQQ KKKENLLTCL ADLFHSIATQ KKKVGVIPPK KFISRLRKEN DLFDNYMQQD
     AHEFLNYLLN TVADILQEEK KQEKQNGRLK NNGTAGATEA ETDNKTESTW VHDIFQGTLT
     NETRCLNCET VSSKDEDFLD LSVDVEQNTS ITHCLRDFSN TETLCSEYKY YCETCCSKQE
     AQKRMRVKKL PMILALHLKR FKYMEQLHRY TKLSYRVVFP LELRLFNTSG DAVNLDRMYD
     LVAVVVHCGS GPNRGHYITI VKSHGFWLLF DDDIVEKIDA QAIEEFYGLT SDISKNSESG
     YILFYQSRE
//
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