ID A0A2I3ST01_PANTR Unreviewed; 435 AA.
AC A0A2I3ST01;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP3 {ECO:0000313|Ensembl:ENSPTRP00000080168.1,
GN ECO:0000313|VGNC:VGNC:13454};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000080168.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000080168.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000080168.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; AACZ04064614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3ST01; -.
DR Ensembl; ENSPTRT00000089844.1; ENSPTRP00000080168.1; ENSPTRG00000007149.6.
DR VGNC; VGNC:13454; USP3.
DR GeneTree; ENSGT00940000157850; -.
DR Proteomes; UP000002277; Chromosome 15.
DR Bgee; ENSPTRG00000007149; Expressed in bone marrow and 20 other cell types or tissues.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF19; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 3; 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 Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 74..426
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 435 AA; 49553 MW; 71BCA018732527D6 CRC64;
IENGPGYKRL YRCDDFVVND TKLGLVQKVR EHLQNLENSA FTADRHRKRK LLENSTLNSK
LLKVNGSTTA ICATGLRNLG NTCFMNAILQ SLSNIEQFCC YFKELPAVEL RNGKTAGRRT
YHTRSQGDNN VSLVEEFRKT LCALWQGSQT AFSPESLFYV VWKIMPNFRG YQQQDAHEFM
RYLLDHLHLE LQGGFNGVSR SAILQENSTL SASNKCCING ASTVVTAIFG GILQNEVNCL
ICGTESRKFD PFLDLSLDIP SQFRSKRSKN QENGPVCSLR DCLRSFTDLE ELDETELYMC
HKCKKKQKST KKFWIQKLPK VLCLHLKRFH WTAYLRNKVD TYVEFPLRGL DMKCYLLEPE
NSGPESCLYD LAAVVVHHGS GVGSGHYTAY ATHEGRWFHF NDSTVTLTDE ETVVKAKAYI
LFYVEHQAKA GSDKL
//
