ADPRM_RAT
ID ADPRM_RAT Reviewed; 337 AA.
AC Q5M886; A9Y0H8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase;
DE EC=3.6.1.13;
DE EC=3.6.1.16;
DE EC=3.6.1.53;
DE AltName: Full=ADPRibase-Mn;
DE AltName: Full=CDP-choline phosphohydrolase;
GN Name=Adprm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=18352857; DOI=10.1042/bj20071471;
RA Canales J., Fernandez A., Ribeiro J.M., Cabezas A., Rodrigues J.R.,
RA Cameselle J.C., Costas M.J.;
RT "Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel
RT metallophosphoesterase family preferentially expressed in rodent immune
RT cells.";
RL Biochem. J. 413:103-113(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline
CC and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-
CC glucose. May be involved in immune cell signaling as suggested by the
CC second-messenger role of ADP-ribose, which activates TRPM2 as a
CC mediator of oxidative/nitrosative stress.
CC {ECO:0000269|PubMed:18352857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-choline + H2O = CMP + 2 H(+) + phosphocholine;
CC Xref=Rhea:RHEA:32487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:295975;
CC EC=3.6.1.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-glycerol + H2O = CMP + 2 H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:21692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:58311, ChEBI:CHEBI:60377; EC=3.6.1.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18352857};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 uM for ADP-ribose {ECO:0000269|PubMed:18352857};
CC KM=28.5 uM for CDP-choline {ECO:0000269|PubMed:18352857};
CC KM=41.3 uM for CDP-ethanolamine {ECO:0000269|PubMed:18352857};
CC KM=28.1 uM for CDP-glycerol {ECO:0000269|PubMed:18352857};
CC KM=201 uM for ADP {ECO:0000269|PubMed:18352857};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18352857}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in immune cells.
CC {ECO:0000269|PubMed:18352857}.
CC -!- SIMILARITY: Belongs to the ADPRibase-Mn family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU037900; ABW03224.1; -; mRNA.
DR EMBL; BC088174; AAH88174.1; -; mRNA.
DR RefSeq; NP_001009246.1; NM_001009246.1.
DR RefSeq; XP_006246665.1; XM_006246603.3.
DR AlphaFoldDB; Q5M886; -.
DR SMR; Q5M886; -.
DR STRING; 10116.ENSRNOP00000004560; -.
DR PaxDb; Q5M886; -.
DR GeneID; 287406; -.
DR KEGG; rno:287406; -.
DR UCSC; RGD:1309906; rat.
DR CTD; 56985; -.
DR RGD; 1309906; Adprm.
DR VEuPathDB; HostDB:ENSRNOG00000003397; -.
DR eggNOG; ENOG502QUQW; Eukaryota.
DR HOGENOM; CLU_039893_1_0_1; -.
DR InParanoid; Q5M886; -.
DR OMA; GHNHAGN; -.
DR OrthoDB; 1263522at2759; -.
DR PhylomeDB; Q5M886; -.
DR TreeFam; TF331229; -.
DR BRENDA; 3.6.1.53; 5301.
DR Reactome; R-RNO-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR SABIO-RK; Q5M886; -.
DR PRO; PR:Q5M886; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003397; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5M886; RN.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IBA:GO_Central.
DR GO; GO:0047734; F:CDP-glycerol diphosphatase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR CDD; cd07396; MPP_Nbla03831; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041869; MPP_ADPRM.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Magnesium; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..337
FT /note="Manganese-dependent ADP-ribose/CDP-alcohol
FT diphosphatase"
FT /id="PRO_0000286569"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q3LIE5"
FT CONFLICT 44
FT /note="Y -> C (in Ref. 1; ABW03224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 38712 MW; B34FFB3351FD9727 CRC64;
MADKPDPSSP ADGPEPLFSF GVIADIQYAD LEDGYNFQRS RRRYYRHSLV HLQGAIEDWN
KESSMPCCVL QLGDIIDGYN AQYKVSEKSL ELVMNTFQML KVPVHHTWGN HEFYNFSRDY
LANSKLNSKF LEDQIPQHPE TTPSENYYAY HFVPFPKFRF ILLDSYDLSV LGIDQFSPKY
EQCMKILREH NPNVELNSPQ GLSEPQYVQF NGGFSQEQLN WLNEVLTFSD ANQEKVVIVS
HLPIYPEASD SVCLAWNYVD ALSIIWSHQC VVCFLAGHTH DGGYSEDPFG VHHVNLEGVI
ETAPDSQAFG TVHVYPDKML LKGRGRVPDR IMNYKRE
