ADPRM_HUMAN
ID ADPRM_HUMAN Reviewed; 342 AA.
AC Q3LIE5; A8K9B4; D3DTS4; Q9BVD4; Q9NRU8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
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; Synonyms=C17orf48; ORFNames=MDS006, Nbla03831;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J., Gu J.,
RA Huang Q., Yu Y., Xu S., Ren S., Fu G.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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=Q3LIE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3LIE5-3; Sequence=VSP_025092, VSP_025093;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ADPRibase-Mn family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87317.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB073393; BAE45723.1; -; mRNA.
DR EMBL; AK292629; BAF85318.1; -; mRNA.
DR EMBL; CH471108; EAW89995.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW89996.1; -; Genomic_DNA.
DR EMBL; BC001294; AAH01294.1; -; mRNA.
DR EMBL; BC070155; AAH70155.1; -; mRNA.
DR EMBL; AF168715; AAF87317.1; ALT_FRAME; mRNA.
DR CCDS; CCDS11159.2; -. [Q3LIE5-1]
DR RefSeq; NP_064618.3; NM_020233.4. [Q3LIE5-1]
DR AlphaFoldDB; Q3LIE5; -.
DR SMR; Q3LIE5; -.
DR BioGRID; 121302; 5.
DR IntAct; Q3LIE5; 1.
DR STRING; 9606.ENSP00000369099; -.
DR iPTMnet; Q3LIE5; -.
DR PhosphoSitePlus; Q3LIE5; -.
DR BioMuta; ADPRM; -.
DR DMDM; 121942723; -.
DR EPD; Q3LIE5; -.
DR MassIVE; Q3LIE5; -.
DR MaxQB; Q3LIE5; -.
DR PaxDb; Q3LIE5; -.
DR PeptideAtlas; Q3LIE5; -.
DR PRIDE; Q3LIE5; -.
DR ProteomicsDB; 61776; -. [Q3LIE5-1]
DR ProteomicsDB; 61777; -. [Q3LIE5-3]
DR Antibodypedia; 12941; 65 antibodies from 17 providers.
DR DNASU; 56985; -.
DR Ensembl; ENST00000379774.5; ENSP00000369099.4; ENSG00000170222.12. [Q3LIE5-1]
DR Ensembl; ENST00000468843.1; ENSP00000431622.1; ENSG00000170222.12. [Q3LIE5-3]
DR GeneID; 56985; -.
DR KEGG; hsa:56985; -.
DR MANE-Select; ENST00000379774.5; ENSP00000369099.4; NM_020233.5; NP_064618.3.
DR UCSC; uc060bgm.1; human. [Q3LIE5-1]
DR CTD; 56985; -.
DR DisGeNET; 56985; -.
DR GeneCards; ADPRM; -.
DR HGNC; HGNC:30925; ADPRM.
DR HPA; ENSG00000170222; Low tissue specificity.
DR neXtProt; NX_Q3LIE5; -.
DR OpenTargets; ENSG00000170222; -.
DR PharmGKB; PA142672231; -.
DR VEuPathDB; HostDB:ENSG00000170222; -.
DR eggNOG; ENOG502QUQW; Eukaryota.
DR GeneTree; ENSGT00390000014667; -.
DR HOGENOM; CLU_039893_0_0_1; -.
DR InParanoid; Q3LIE5; -.
DR OMA; GHNHAGN; -.
DR PhylomeDB; Q3LIE5; -.
DR TreeFam; TF331229; -.
DR BRENDA; 3.6.1.13; 2681.
DR BRENDA; 3.6.1.53; 2681.
DR PathwayCommons; Q3LIE5; -.
DR Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR BioGRID-ORCS; 56985; 22 hits in 1085 CRISPR screens.
DR ChiTaRS; ADPRM; human.
DR GenomeRNAi; 56985; -.
DR Pharos; Q3LIE5; Tdark.
DR PRO; PR:Q3LIE5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q3LIE5; protein.
DR Bgee; ENSG00000170222; Expressed in calcaneal tendon and 158 other tissues.
DR ExpressionAtlas; Q3LIE5; baseline and differential.
DR Genevisible; Q3LIE5; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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..342
FT /note="Manganese-dependent ADP-ribose/CDP-alcohol
FT diphosphatase"
FT /id="PRO_0000286567"
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:0007744|PubMed:22814378"
FT VAR_SEQ 202..205
FT /note="LSEP -> ELFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025092"
FT VAR_SEQ 206..342
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025093"
FT VARIANT 92
FT /note="L -> R (in dbSNP:rs34940296)"
FT /id="VAR_032125"
FT VARIANT 337
FT /note="E -> G (in dbSNP:rs406446)"
FT /id="VAR_032126"
FT CONFLICT 113
FT /note="F -> S (in Ref. 4; BAF85318)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="L -> F (in Ref. 1; AAF87317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 39529 MW; 2DBD4499D9DA2AC2 CRC64;
MDDKPNPEAL SDSSERLFSF GVIADVQFAD LEDGFNFQGT RRRYYRHSLL HLQGAIEDWN
NESSMPCCVL QLGDIIDGYN AQYNASKKSL ELVMDMFKRL KVPVHHTWGN HEFYNFSREY
LTHSKLNTKF LEDQIVHHPE TMPSEDYYAY HFVPFPKFRF ILLDAYDLSV LGVDQSSPKY
EQCMKILREH NPNTELNSPQ GLSEPQFVQF NGGFSQEQLN WLNEVLTFSD TNQEKVVIVS
HLPIYPDASD NVCLAWNYRD ALAVIWSHEC VVCFFAGHTH DGGYSEDPFG VYHVNLEGVI
ETAPDSQAFG TVHVYPDKMM LKGRGRVPDR IMNYKKERAF HC
