ADPRM_MOUSE
ID ADPRM_MOUSE Reviewed; 340 AA.
AC Q99KS6; Q5SUD1; Q9D7K9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99KS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KS6-2; Sequence=VSP_025094, VSP_025095;
CC -!- SIMILARITY: Belongs to the ADPRibase-Mn family. {ECO:0000305}.
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DR EMBL; AK009142; BAB26101.1; -; mRNA.
DR EMBL; AK145941; BAE26771.1; -; mRNA.
DR EMBL; AL645988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004029; AAH04029.1; -; mRNA.
DR CCDS; CCDS48820.1; -. [Q99KS6-1]
DR RefSeq; NP_079786.2; NM_025510.3. [Q99KS6-1]
DR RefSeq; XP_006534003.1; XM_006533940.3. [Q99KS6-1]
DR AlphaFoldDB; Q99KS6; -.
DR SMR; Q99KS6; -.
DR STRING; 10090.ENSMUSP00000112064; -.
DR PhosphoSitePlus; Q99KS6; -.
DR EPD; Q99KS6; -.
DR MaxQB; Q99KS6; -.
DR PaxDb; Q99KS6; -.
DR PRIDE; Q99KS6; -.
DR ProteomicsDB; 285619; -. [Q99KS6-1]
DR ProteomicsDB; 285620; -. [Q99KS6-2]
DR Antibodypedia; 12941; 65 antibodies from 17 providers.
DR DNASU; 66358; -.
DR Ensembl; ENSMUST00000116363; ENSMUSP00000112064; ENSMUSG00000020910. [Q99KS6-1]
DR Ensembl; ENSMUST00000146338; ENSMUSP00000137768; ENSMUSG00000020910. [Q99KS6-2]
DR GeneID; 66358; -.
DR KEGG; mmu:66358; -.
DR UCSC; uc007jlt.2; mouse. [Q99KS6-1]
DR CTD; 56985; -.
DR MGI; MGI:1913608; Adprm.
DR VEuPathDB; HostDB:ENSMUSG00000020910; -.
DR eggNOG; ENOG502QUQW; Eukaryota.
DR GeneTree; ENSGT00390000014667; -.
DR HOGENOM; CLU_039893_0_1_1; -.
DR InParanoid; Q99KS6; -.
DR OMA; GHNHAGN; -.
DR OrthoDB; 1263522at2759; -.
DR PhylomeDB; Q99KS6; -.
DR TreeFam; TF331229; -.
DR BRENDA; 3.6.1.53; 3474.
DR Reactome; R-MMU-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR BioGRID-ORCS; 66358; 5 hits in 73 CRISPR screens.
DR PRO; PR:Q99KS6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99KS6; protein.
DR Bgee; ENSMUSG00000020910; Expressed in granulocyte and 259 other tissues.
DR Genevisible; Q99KS6; MM.
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; Alternative splicing; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..340
FT /note="Manganese-dependent ADP-ribose/CDP-alcohol
FT diphosphatase"
FT /id="PRO_0000286568"
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 VAR_SEQ 202..205
FT /note="LSEP -> ELLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025094"
FT VAR_SEQ 206..340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025095"
FT CONFLICT 59
FT /note="W -> C (in Ref. 1; BAB26101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 38948 MW; 6DCF6BA02F3CE718 CRC64;
MADKLVPSSP ADASEPLFSF GVIADIQYAD LEDGYNYQRS RRRYYRHSLI HLQGAIEDWN
KESSMPCCVL QLGDIIDGYN AQYKVSEKSL ELVMNTFQML KVPVHHTWGN HEFYNFSRDY
LASSKLNSKF LEDQIAQHPE TTPSENYYAY HFVPFPKFRF ILLDSYDLSV LGIDPSSPKY
EQCMKMLREH NPNVELNSPQ GLSEPQYVQF NGGFSQEQLN WLNEVLTFSD TNQEKVVIVS
HLPIYPEASD SVCLAWNYVD ALSIIWSHKC VVCFLAGHTH DGGYSEDPFG VHHVNLEGVI
ETAPDSQAFG TVHVFPDKML LKGRGRVPDR IMNYKREEAL
