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Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase (EC 3.6.1.13) (EC 3.6.1.16) (EC 3.6.1.53) (ADPRibase-Mn) (CDP-choline phosphohydrolase)

 ADPRM_HUMAN             Reviewed;         342 AA.
Q3LIE5; A8K9B4; D3DTS4; Q9BVD4; Q9NRU8;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 1.
12-SEP-2018, entry version 106.
RecName: Full=Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase;
EC=3.6.1.13;
EC=3.6.1.16;
EC=3.6.1.53;
AltName: Full=ADPRibase-Mn;
AltName: Full=CDP-choline phosphohydrolase;
Name=ADPRM; Synonyms=C17orf48; ORFNames=MDS006, Nbla03831;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Neuroblastoma;
PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
Hirato J., Nakagawara A.;
"Neuroblastoma oligo-capping cDNA project: toward the understanding of
the genesis and biology of neuroblastoma.";
Cancer Lett. 197:63-68(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 (ISOFORM 1).
TISSUE=Hematopoietic stem cell;
Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J.,
Gu J., Huang Q., Yu Y., Xu S., Ren S., Fu G.;
"Novel genes expressed in hematopoietic stem/progenitor cells from
myelodysplastic syndrome patients.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-
choline and CDP-ethanolamine, but not other non-reducing ADP-
sugars or CDP-glucose. May be involved in immune cell signaling as
suggested by the second-messenger role of ADP-ribose, which
activates TRPM2 as a mediator of oxidative/nitrosative stress (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: CDP-choline + H(2)O = CMP + phosphocholine.
-!- CATALYTIC ACTIVITY: ADP-D-ribose + H(2)O = AMP + D-ribose 5-
phosphate.
-!- CATALYTIC ACTIVITY: CDP-glycerol + H(2)O = CMP + sn-glycerol 3-
phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3LIE5-1; Sequence=Displayed;
Name=2;
IsoId=Q3LIE5-3; Sequence=VSP_025092, VSP_025093;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- SIMILARITY: Belongs to the ADPRibase-Mn family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF87317.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB073393; BAE45723.1; -; mRNA.
EMBL; AK292629; BAF85318.1; -; mRNA.
EMBL; CH471108; EAW89995.1; -; Genomic_DNA.
EMBL; CH471108; EAW89996.1; -; Genomic_DNA.
EMBL; BC001294; AAH01294.1; -; mRNA.
EMBL; BC070155; AAH70155.1; -; mRNA.
EMBL; AF168715; AAF87317.1; ALT_FRAME; mRNA.
CCDS; CCDS11159.2; -. [Q3LIE5-1]
RefSeq; NP_064618.3; NM_020233.4. [Q3LIE5-1]
UniGene; Hs.47668; -.
UniGene; Hs.708369; -.
ProteinModelPortal; Q3LIE5; -.
SMR; Q3LIE5; -.
STRING; 9606.ENSP00000369099; -.
iPTMnet; Q3LIE5; -.
BioMuta; ADPRM; -.
DMDM; 121942723; -.
PaxDb; Q3LIE5; -.
PeptideAtlas; Q3LIE5; -.
PRIDE; Q3LIE5; -.
ProteomicsDB; 61776; -.
ProteomicsDB; 61777; -. [Q3LIE5-3]
DNASU; 56985; -.
Ensembl; ENST00000379774; ENSP00000369099; ENSG00000170222. [Q3LIE5-1]
Ensembl; ENST00000468843; ENSP00000431622; ENSG00000170222. [Q3LIE5-3]
GeneID; 56985; -.
KEGG; hsa:56985; -.
UCSC; uc060bgm.1; human. [Q3LIE5-1]
CTD; 56985; -.
EuPathDB; HostDB:ENSG00000170222.11; -.
GeneCards; ADPRM; -.
HGNC; HGNC:30925; ADPRM.
HPA; HPA023265; -.
HPA; HPA023820; -.
neXtProt; NX_Q3LIE5; -.
OpenTargets; ENSG00000170222; -.
PharmGKB; PA142672231; -.
eggNOG; ENOG410IJ2N; Eukaryota.
eggNOG; COG1409; LUCA.
GeneTree; ENSGT00390000014667; -.
HOGENOM; HOG000154875; -.
HOVERGEN; HBG100432; -.
InParanoid; Q3LIE5; -.
KO; K01517; -.
OMA; LAWNYRD; -.
OrthoDB; EOG091G0CMY; -.
PhylomeDB; Q3LIE5; -.
TreeFam; TF331229; -.
Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins.
GenomeRNAi; 56985; -.
PRO; PR:Q3LIE5; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000170222; Expressed in 186 organ(s), highest expression level in prostate gland.
CleanEx; HS_C17orf48; -.
ExpressionAtlas; Q3LIE5; baseline and differential.
Genevisible; Q3LIE5; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0047631; F:ADP-ribose diphosphatase activity; TAS:Reactome.
GO; GO:0047734; F:CDP-glycerol diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
Pfam; PF00149; Metallophos; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Hydrolase;
Metal-binding; Polymorphism; Reference proteome; Zinc.
CHAIN 1 342 Manganese-dependent ADP-ribose/CDP-
alcohol diphosphatase.
/FTId=PRO_0000286567.
METAL 25 25 Zinc 1. {ECO:0000250}.
METAL 27 27 Zinc 1. {ECO:0000250}.
METAL 74 74 Zinc 1. {ECO:0000250}.
METAL 74 74 Zinc 2. {ECO:0000250}.
METAL 110 110 Zinc 2. {ECO:0000250}.
METAL 241 241 Zinc 2. {ECO:0000250}.
METAL 278 278 Zinc 2. {ECO:0000250}.
METAL 280 280 Zinc 1. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
VAR_SEQ 202 205 LSEP -> ELFL (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_025092.
VAR_SEQ 206 342 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_025093.
VARIANT 92 92 L -> R (in dbSNP:rs34940296).
/FTId=VAR_032125.
VARIANT 337 337 E -> G (in dbSNP:rs406446).
/FTId=VAR_032126.
CONFLICT 113 113 F -> S (in Ref. 4; BAF85318).
{ECO:0000305}.
CONFLICT 202 202 L -> F (in Ref. 1; AAF87317).
{ECO:0000305}.
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


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