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ADPRS_BOVIN
ID   ADPRS_BOVIN             Reviewed;         365 AA.
AC   Q3SYV9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=ADP-ribosylhydrolase ARH3 {ECO:0000305};
DE   AltName: Full=ADP-ribose glycohydrolase ARH3 {ECO:0000305};
DE   AltName: Full=ADP-ribosylhydrolase 3 {ECO:0000250|UniProtKB:Q9NX46};
DE   AltName: Full=O-acetyl-ADP-ribose deacetylase ARH3 {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q9NX46};
DE   AltName: Full=Poly(ADP-ribose) glycohydrolase ARH3 {ECO:0000305};
DE            EC=3.2.1.143 {ECO:0000250|UniProtKB:Q9NX46};
DE   AltName: Full=[Protein ADP-ribosylarginine] hydrolase-like protein 2 {ECO:0000305};
DE   AltName: Full=[Protein ADP-ribosylserine] hydrolase;
DE            EC=3.2.2.-;
GN   Name=ADPRS;
GN   Synonyms=ADPRHL2 {ECO:0000250|UniProtKB:Q9NX46},
GN   ARH3 {ECO:0000250|UniProtKB:Q9NX46};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ADP-ribosylhydrolase that preferentially hydrolyzes the
CC       scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-
CC       ribose and acts on different substrates, such as proteins ADP-
CC       ribosylated on serine and threonine, free poly(ADP-ribose) and O-
CC       acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-
CC       ribosylhydrolase by mediating the removal of mono-ADP-ribose attached
CC       to serine residues on proteins, thereby playing a key role in DNA
CC       damage response. Serine ADP-ribosylation of proteins constitutes the
CC       primary form of ADP-ribosylation of proteins in response to DNA damage.
CC       Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or
CC       -asparagine bonds. Also able to degrade protein free poly(ADP-ribose),
CC       which is synthesized in response to DNA damage: free poly(ADP-ribose)
CC       acts as a potent cell death signal and its degradation by ADPRHL2
CC       protects cells from poly(ADP-ribose)-dependent cell death, a process
CC       named parthanatos (By similarity). Also hydrolyzes free poly(ADP-
CC       ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a
CC       product of deacetylation reactions catalyzed by sirtuins. Specifically
CC       degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-
CC       ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
CC       {ECO:0000250|UniProtKB:Q9NX46}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-
CC         alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-
CC         COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143;
CC         Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1''-O-acetyl-ADP-alpha-D-ribose + H2O = acetate + ADP-D-ribose
CC         + H(+); Xref=Rhea:RHEA:58112, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:142511;
CC         Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-(ADP-D-ribosyl)-L-seryl-[protein] = ADP-D-ribose + L-
CC         seryl-[protein]; Xref=Rhea:RHEA:58256, Rhea:RHEA-COMP:9863,
CC         Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:142556;
CC         Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017;
CC         Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC       Note=Binds 2 magnesium ions per subunit.
CC       {ECO:0000250|UniProtKB:Q9NX46};
CC   -!- ACTIVITY REGULATION: The protein undergoes a dramatic conformational
CC       switch from closed to open states upon substrate-binding, which enables
CC       specific substrate recognition for the 1''-O-linkage. The glutamate
CC       flap (Glu-42) blocks substrate entrance to Mg(2+) in the unliganded
CC       closed state. In presence of substrate, Glu-42 is ejected from the
CC       active site: this closed-to-open transition significantly widens the
CC       substrate-binding channel and precisely positions the scissile 1''-O-
CC       linkage for cleavage while securing tightly 2'- and 3'-hydroxyls of
CC       ADP-ribose. {ECO:0000250|UniProtKB:Q9NX46}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NX46}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NX46}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9NX46}. Chromosome
CC       {ECO:0000250|UniProtKB:Q9NX46}. Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9NX46}. Note=Recruited to DNA lesion regions
CC       following DNA damage; ADP-D-ribose-recognition is required for
CC       recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q9NX46}.
CC   -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; BC103360; AAI03361.1; -; mRNA.
DR   RefSeq; NP_001030417.1; NM_001035340.2.
DR   AlphaFoldDB; Q3SYV9; -.
DR   SMR; Q3SYV9; -.
DR   STRING; 9913.ENSBTAP00000028950; -.
DR   PaxDb; Q3SYV9; -.
DR   PRIDE; Q3SYV9; -.
DR   GeneID; 521650; -.
DR   KEGG; bta:521650; -.
DR   CTD; 54936; -.
DR   eggNOG; ENOG502QUER; Eukaryota.
DR   InParanoid; Q3SYV9; -.
DR   OrthoDB; 988788at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0140292; F:ADP-ribosylserine hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0061463; F:O-acetyl-ADP-ribose deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0060546; P:negative regulation of necroptotic process; ISS:UniProtKB.
DR   GO; GO:0140290; P:peptidyl-serine ADP-deribosylation; ISS:UniProtKB.
DR   Gene3D; 1.10.4080.10; -; 1.
DR   InterPro; IPR005502; Ribosyl_crysJ1.
DR   InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR   Pfam; PF03747; ADP_ribosyl_GH; 1.
DR   SUPFAM; SSF101478; SSF101478; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Cytoplasm; DNA damage; DNA repair; Hydrolase; Magnesium;
KW   Metal-binding; Mitochondrion; Nucleus; Reference proteome.
FT   CHAIN           1..365
FT                   /note="ADP-ribosylhydrolase ARH3"
FT                   /id="PRO_0000277612"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         77
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         147..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   BINDING         318
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT   SITE            42
FT                   /note="Glutamate flap"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX46"
SQ   SEQUENCE   365 AA;  39221 MW;  59F65453AABF2802 CRC64;
     MAAAAAMTAA GCGGAGAARS LSRFRGCLAG ALLGDCVGAV YEARDTVDLT SVLRQVQDLE
     PDPGSPGSAR TEALCYTDDT AMARALVQSL LAKEAFDEVD MAHRFAQEYK KDPDRGYGAG
     VITVFRKHLS PRCRDVFEPA RAQFNGKGSY GNGGAMRVAG ISLAYSSVQD VQKFARLSAQ
     LTHASSLGYN GAILQALAVH LALQGESSSE HFLEQLLGHM EELESDAQSV LDARELGMEE
     RPYSSRLKKI GELLEQDSVT REEVVSELGN GIAAFESVPT AIYCFLRCME PDPEIPSTFN
     SLQRTLVYSI SLGGDTDTIA TMAGAIAGAY YGMEQVPESW QQSCEGYEET DVLAQSLHRV
     FQKSL
 
 
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