UBP46_PONAB
ID UBP46_PONAB Reviewed; 366 AA.
AC Q5RBQ4; Q5RBN2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 46;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P62068};
DE AltName: Full=Deubiquitinating enzyme 46;
DE AltName: Full=Ubiquitin thioesterase 46;
DE AltName: Full=Ubiquitin-specific-processing protease 46;
GN Name=USP46;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that plays a role in behavior,
CC possibly by regulating GABA action. May act by mediating the
CC deubiquitination of GAD1/GAD67 (By similarity). Has almost no
CC deubiquitinating activity by itself and requires the interaction with
CC WDR48 to have a high activity. Not involved in deubiquitination of
CC monoubiquitinated FANCD2 (By similarity).
CC {ECO:0000250|UniProtKB:P62068, ECO:0000250|UniProtKB:P62069}.
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:0000250|UniProtKB:P62068};
CC -!- SUBUNIT: Interacts with WDR48. Interacts with WDR20.
CC {ECO:0000250|UniProtKB:P62068}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RBQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RBQ4-2; Sequence=VSP_037622;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR858584; CAH90806.1; -; mRNA.
DR EMBL; CR858606; CAH90828.1; -; mRNA.
DR RefSeq; NP_001127337.1; NM_001133865.1. [Q5RBQ4-1]
DR RefSeq; NP_001128936.1; NM_001135464.1. [Q5RBQ4-2]
DR AlphaFoldDB; Q5RBQ4; -.
DR SMR; Q5RBQ4; -.
DR STRING; 9601.ENSPPYP00000016505; -.
DR Ensembl; ENSPPYT00000040326; ENSPPYP00000032861; ENSPPYG00000014777. [Q5RBQ4-2]
DR Ensembl; ENSPPYT00000046675; ENSPPYP00000029459; ENSPPYG00000014777. [Q5RBQ4-1]
DR GeneID; 100174399; -.
DR GeneID; 100189895; -.
DR KEGG; pon:100189895; -.
DR CTD; 64854; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000153284; -.
DR HOGENOM; CLU_008279_2_0_1; -.
DR InParanoid; Q5RBQ4; -.
DR OrthoDB; 378361at2759; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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 Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Behavior; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc.
FT CHAIN 1..366
FT /note="Ubiquitin carboxyl-terminal hydrolase 46"
FT /id="PRO_0000304740"
FT DOMAIN 35..365
FT /note="USP"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P62068"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P62068"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P62068"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P62068"
FT VAR_SEQ 13..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037622"
SQ SEQUENCE 366 AA; 42442 MW; 67BB113FC4081C46 CRC64;
MTVRNIASIC NMGTNASALE KDIGPEQFPI NEHYFGLVNF GNTCYCNSVL QALYFCRPFR
ENVLAYKAQQ KKKENLLTCL ADLFHSIATQ KKKVGVIPPK KFISRLRKEN DLFDNYMQQD
AHEFLNYLLN TIADILQEEK KQEKQNGKLK NGNMNEPAEN NKPELTWVHE IFQGTLTNET
RCLNCETVSS KDEDFLDLSV DVEQNTSITH CLRDFSNTET LCSEQKYYCE TCCSKQEAQK
RMRVKKLPMI LALHLKRFKY MEQLHRYTKL SYRVVFPLEL RLFNTSSDAV NLDRMYDLVA
VVVHCGSGPN RGHYITIVKS HGFWLLFDDD IVEKIDAQAI EEFYGLTSDI SKNSESGYIL
FYQSRE
