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O-acetyl-ADP-ribose deacetylase MACROD1 (EC 3.2.2.-) (EC 3.5.1.-) (MACRO domain-containing protein 1) (Protein LRP16) ([Protein ADP-ribosylglutamate] hydrolase)

 MACD1_HUMAN             Reviewed;         325 AA.
Q9BQ69; Q9UH96;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
16-JUN-2003, sequence version 2.
12-SEP-2018, entry version 134.
RecName: Full=O-acetyl-ADP-ribose deacetylase MACROD1;
EC=3.2.2.-;
EC=3.5.1.-;
AltName: Full=MACRO domain-containing protein 1;
AltName: Full=Protein LRP16;
AltName: Full=[Protein ADP-ribosylglutamate] hydrolase;
Name=MACROD1; Synonyms=LRP16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphocyte;
PubMed=12578638;
Han W.-D., Yu L., Lou F.D., Wang Q.S., Zhao Y., Shi Z.J., Jin H.J.;
"The application of RACE technique to clone the full-length cDNA of a
novel leukemia associated gene LRP16.";
Zhongguo Shi Yan Xue Ye Xue Za Zhi 9:18-21(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Eye;
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).
[3]
INDUCTION.
PubMed=12790785; DOI=10.1677/erc.0.0100217;
Han W.-D., Mu Y.-M., Lu X.-C., Xu Z.-M., Li X.-J., Yu L., Song H.-J.,
Li M., Lu J.-M., Zhao Y.-L., Pan C.-Y.;
"Up-regulation of LRP16 mRNA by 17beta-estradiol through activation of
estrogen receptor alpha (ERalpha), but not ERbeta, and promotion of
human breast cancer MCF-7 cell proliferation: a preliminary report.";
Endocr. Relat. Cancer 10:217-224(2003).
[4]
INDUCTION, AND FUNCTION.
PubMed=17893710; DOI=10.1038/cr.2007.79;
Meng Y.G., Han W.-D., Zhao Y.-L., Huang K., Si Y.-L., Wu Z.-Q.,
Mu Y.-M.;
"Induction of the LRP16 gene by estrogen promotes the invasive growth
of Ishikawa human endometrial cancer cells through the downregulation
of E-cadherin.";
Cell Res. 17:869-880(2007).
[5]
INTERACTION WITH ESR1, AND FUNCTION.
PubMed=17914104; DOI=10.1677/ERC-06-0082;
Han W.-D., Zhao Y.-L., Meng Y.G., Zang L., Wu Z.-Q., Li Q., Si Y.-L.,
Huang K., Ba J.-M., Morinaga H., Nomura M., Mu Y.-M.;
"Estrogenically regulated LRP16 interacts with estrogen receptor alpha
and enhances the receptor's transcriptional activity.";
Endocr. Relat. Cancer 14:741-753(2007).
[6]
CHROMOSOMAL TRANSLOCATION WITH RUNX1.
PubMed=17532767; DOI=10.1111/j.1600-0609.2007.00858.x;
Imagama S., Abe A., Suzuki M., Hayakawa F., Katsumi A., Emi N.,
Kiyoi H., Naoe T.;
"LRP16 is fused to RUNX1 in monocytic leukemia cell line with
t(11;21)(q13;q22).";
Eur. J. Haematol. 79:25-31(2007).
[7]
FUNCTION, INTERACTION WITH ANDROGENE RECEPTOR, AND INDUCTION BY
ANDROGEN.
PubMed=19022849; DOI=10.1677/ERC-08-0150;
Yang J., Zhao Y.-L., Wu Z.-Q., Si Y.-L., Meng Y.G., Fu X.B., Mu Y.-M.,
Han W.-D.;
"The single-macro domain protein LRP16 is an essential cofactor of
androgen receptor.";
Endocr. Relat. Cancer 16:139-153(2009).
[8]
INDUCTION, AND FUNCTION.
PubMed=19403568; DOI=10.1677/JOE-09-0054;
Tian L., Wu Z., Zhao Y., Meng Y., Si Y., Fu X., Mu Y., Han W.;
"Differential induction of LRP16 by liganded and unliganded estrogen
receptor alpha in SKOV3 ovarian carcinoma cells.";
J. Endocrinol. 202:167-177(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-174; ASP-184
AND GLY-270.
PubMed=23474712; DOI=10.1038/nsmb.2523;
Jankevicius G., Hassler M., Golia B., Rybin V., Zacharias M.,
Timinszky G., Ladurner A.G.;
"A family of macrodomain proteins reverses cellular mono-ADP-
ribosylation.";
Nat. Struct. Mol. Biol. 20:508-514(2013).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[13]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 91-325, FUNCTION, CATALYTIC
ACTIVITY, MUTAGENESIS OF ASP-160; ASP-167; ASN-171; ASN-174; ASP-184;
HIS-188; SER-268 AND GLY-270, BIOPHYSICOCHEMICAL PROPERTIES, AND
ACTIVITY REGULATION.
PubMed=21257746; DOI=10.1074/jbc.M110.206771;
Chen D., Vollmar M., Rossi M.N., Phillips C., Kraehenbuehl R.,
Slade D., Mehrotra P.V., von Delft F., Crosthwaite S.K., Gileadi O.,
Denu J.M., Ahel I.;
"Identification of macrodomain proteins as novel O-acetyl-ADP-ribose
deacetylases.";
J. Biol. Chem. 286:13261-13271(2011).
-!- FUNCTION: Removes ADP-ribose from glutamate residues in proteins
bearing a single ADP-ribose moiety. Inactive towards proteins
bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a
signaling molecule generated by the deacetylation of acetylated
lysine residues in histones and other proteins. Plays a role in
estrogen signaling. Binds to androgen receptor (AR) and amplifies
the transactivation function of AR in response to androgen. May
play an important role in carcinogenesis and/or progression of
hormone-dependent cancers by feed-forward mechanism that activates
ESR1 transactivation. Could be an ESR1 coactivator, providing a
positive feedback regulatory loop for ESR1 signal transduction.
Could be involved in invasive growth by down-regulating CDH1 in
endometrial cancer cells. Enhances ESR1-mediated transcription
activity. {ECO:0000269|PubMed:17893710,
ECO:0000269|PubMed:17914104, ECO:0000269|PubMed:19022849,
ECO:0000269|PubMed:19403568, ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712}.
-!- ACTIVITY REGULATION: Subject to competitive inhibition by the
product ADP-ribose. {ECO:0000269|PubMed:21257746}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=373 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21257746};
-!- SUBUNIT: Interacts with ESR1; Interacts in a manner that is
estrogen independent but is enhanced by estrogen. Interacts (via
macro domain) with AR. {ECO:0000269|PubMed:17914104,
ECO:0000269|PubMed:19022849}.
-!- INTERACTION:
P03372:ESR1; NbExp=4; IntAct=EBI-5324932, EBI-78473;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23474712}.
Note=Recruited to DNA lesions, probably via mono-APD-ribosylated
proteins.
-!- INDUCTION: Overexpressed by estrogens in breast cancer MCF-7
cells, probably via an activation of nuclear receptors for
steroids (ESR1 but not ESR2). Significantly increased by estrogens
in ESR1-positive Ishikawa endometrial cancer cells. Up-regulated
in 17-beta-estradiol-responsive BG-1 ovarian cancer cells but
down-regulated in estrogen-resistant SKOV3 ovarian cancer cells.
Induced by androgen. {ECO:0000269|PubMed:12790785,
ECO:0000269|PubMed:17893710, ECO:0000269|PubMed:19022849,
ECO:0000269|PubMed:19403568}.
-!- DISEASE: Note=A chromosomal aberration involving MACROD1 is found
in acute leukemia. Translocation t(11;21)(q13;q22) that forms a
RUNX1-MACROD1 fusion protein. {ECO:0000269|PubMed:17532767}.
-!- MISCELLANEOUS: Overexpression may promote MCF-7 cells
proliferation. There is an approximate one-third increase of the
invasive capacity of MACROD1-overexpressing cells. The expression
of CDH1 is repressed by MACROD1. Further analyzes demonstrats that
MACROD1 inhibits CDH1 transactivation in a dose dependent manner.
Inhibition is abolished by estrogen deprivation, indicating that
the down-regulation of CDH1 transcription by MACROD1 requires ESR1
mediation. Binding of ESR1 to the CDH1 promoter is antagonized by
MACROD1, suggesting that MACROD1 could interfere with ESR1-
mediated transcription. Knockdown of MACROD1 leads to impaired AR
function and greatly attenuates the coactivation of AR by other AR
coactivators such as UXT and NCOA1. This interference also
markedly inhibits the androgen-stimulated proliferation of
androgen-sensitive LNCaP prostate cancer cells. MACROD1 knockdown
does not significantly affect the growth rate of AR-negative PC-3
prostate cancer cells.
-!- SEQUENCE CAUTION:
Sequence=AAH03188.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH03188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MACROD1ID50947ch11q13.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF202922; AAF15294.2; -; mRNA.
EMBL; BC000270; AAH00270.2; -; mRNA.
EMBL; BC003188; AAH03188.1; ALT_INIT; mRNA.
EMBL; BC007297; AAH07297.1; -; mRNA.
EMBL; BC008316; AAH08316.1; -; mRNA.
CCDS; CCDS8056.1; -.
RefSeq; NP_054786.2; NM_014067.3.
UniGene; Hs.602898; -.
PDB; 2X47; X-ray; 1.70 A; A=91-325.
PDBsum; 2X47; -.
ProteinModelPortal; Q9BQ69; -.
SMR; Q9BQ69; -.
BioGrid; 118813; 32.
IntAct; Q9BQ69; 4.
STRING; 9606.ENSP00000255681; -.
iPTMnet; Q9BQ69; -.
PhosphoSitePlus; Q9BQ69; -.
BioMuta; MACROD1; -.
DMDM; 32129719; -.
EPD; Q9BQ69; -.
MaxQB; Q9BQ69; -.
PaxDb; Q9BQ69; -.
PeptideAtlas; Q9BQ69; -.
PRIDE; Q9BQ69; -.
ProteomicsDB; 78637; -.
Ensembl; ENST00000255681; ENSP00000255681; ENSG00000133315.
GeneID; 28992; -.
KEGG; hsa:28992; -.
UCSC; uc001nyh.4; human.
CTD; 28992; -.
DisGeNET; 28992; -.
EuPathDB; HostDB:ENSG00000133315.10; -.
GeneCards; MACROD1; -.
HGNC; HGNC:29598; MACROD1.
HPA; HPA041031; -.
HPA; HPA071075; -.
MIM; 610400; gene.
neXtProt; NX_Q9BQ69; -.
OpenTargets; ENSG00000133315; -.
PharmGKB; PA162394816; -.
eggNOG; KOG2633; Eukaryota.
eggNOG; COG2110; LUCA.
GeneTree; ENSGT00520000055566; -.
HOGENOM; HOG000086960; -.
HOVERGEN; HBG052356; -.
InParanoid; Q9BQ69; -.
OMA; KITCGYR; -.
OrthoDB; EOG091G0NNH; -.
PhylomeDB; Q9BQ69; -.
TreeFam; TF341440; -.
ChiTaRS; MACROD1; human.
EvolutionaryTrace; Q9BQ69; -.
GenomeRNAi; 28992; -.
PRO; PR:Q9BQ69; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000133315; Expressed in 189 organ(s), highest expression level in gastrocnemius.
CleanEx; HS_MACROD1; -.
Genevisible; Q9BQ69; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0051725; P:protein de-ADP-ribosylation; IDA:UniProtKB.
GO; GO:0042278; P:purine nucleoside metabolic process; IDA:UniProtKB.
InterPro; IPR002589; Macro_dom.
Pfam; PF01661; Macro; 1.
SMART; SM00506; A1pp; 1.
PROSITE; PS51154; MACRO; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosomal rearrangement;
Complete proteome; DNA damage; Hydrolase; Isopeptide bond; Nucleus;
Reference proteome; Ubl conjugation.
CHAIN 1 325 O-acetyl-ADP-ribose deacetylase MACROD1.
/FTId=PRO_0000084485.
DOMAIN 141 322 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
REGION 159 161 Substrate binding. {ECO:0000250}.
REGION 172 174 Substrate binding. {ECO:0000250}.
REGION 179 184 Substrate binding. {ECO:0000250}.
REGION 267 273 Substrate binding. {ECO:0000305}.
BINDING 306 306 Substrate. {ECO:0000250}.
SITE 100 100 Breakpoint for translocation to form
RUNX1-MACROD1.
{ECO:0000269|PubMed:17532767}.
MOD_RES 96 96 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
MOD_RES 103 103 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
MOD_RES 129 129 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
MOD_RES 163 163 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
CROSSLNK 138 138 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 160 160 D->A: Reduced enzyme activity.
{ECO:0000269|PubMed:21257746}.
MUTAGEN 167 167 D->A: Reduced enzyme activity.
{ECO:0000269|PubMed:21257746}.
MUTAGEN 171 171 N->A: Reduced enzyme activity. No
significant effect on affinity for
substrate. {ECO:0000269|PubMed:21257746}.
MUTAGEN 174 174 N->A: Slightly reduced ADP-ribosyl
hydrolase activity; when associated with
A-184. Reduces O-acetyl-ADP-ribose
deacetylase activity by 93%; when
associated with A-184. No significant
effect on affinity for substrate.
{ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712}.
MUTAGEN 184 184 D->A: Slightly reduced ADP-ribosyl
hydrolase activity; when associated with
A-174. Reduces O-acetyl-ADP-ribose
deacetylase activity by 93%; when
associated with A-174. No significant
effect on affinity for substrate.
{ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712}.
MUTAGEN 188 188 H->A: Reduced enzyme activity.
{ECO:0000269|PubMed:21257746}.
MUTAGEN 268 268 S->A: No significant effect on enzyme
activity. {ECO:0000269|PubMed:21257746}.
MUTAGEN 270 270 G->E: Loss of enzyme activity.
{ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712}.
HELIX 94 103 {ECO:0000244|PDB:2X47}.
HELIX 107 110 {ECO:0000244|PDB:2X47}.
HELIX 111 113 {ECO:0000244|PDB:2X47}.
HELIX 122 124 {ECO:0000244|PDB:2X47}.
HELIX 128 132 {ECO:0000244|PDB:2X47}.
HELIX 148 151 {ECO:0000244|PDB:2X47}.
STRAND 154 159 {ECO:0000244|PDB:2X47}.
HELIX 161 163 {ECO:0000244|PDB:2X47}.
STRAND 164 172 {ECO:0000244|PDB:2X47}.
HELIX 182 191 {ECO:0000244|PDB:2X47}.
HELIX 193 200 {ECO:0000244|PDB:2X47}.
STRAND 210 214 {ECO:0000244|PDB:2X47}.
STRAND 218 227 {ECO:0000244|PDB:2X47}.
HELIX 237 256 {ECO:0000244|PDB:2X47}.
STRAND 261 264 {ECO:0000244|PDB:2X47}.
HELIX 276 294 {ECO:0000244|PDB:2X47}.
HELIX 295 297 {ECO:0000244|PDB:2X47}.
STRAND 299 305 {ECO:0000244|PDB:2X47}.
HELIX 308 321 {ECO:0000244|PDB:2X47}.
SEQUENCE 325 AA; 35505 MW; 82294BFC904FA4D0 CRC64;
MSLQSRLSGR LAQLRAAGQL LVPPRPRPGH LAGATRTRSS TCGPPAFLGV FGRRARTSAG
VGAWGAAAVG RTAGVRTWAP LAMAAKVDLS TSTDWKEAKS FLKGLSDKQR EEHYFCKDFV
RLKKIPTWKE MAKGVAVKVE EPRYKKDKQL NEKISLLRSD ITKLEVDAIV NAANSSLLGG
GGVDGCIHRA AGPLLTDECR TLQSCKTGKA KITGGYRLPA KYVIHTVGPI AYGEPSASQA
AELRSCYLSS LDLLLEHRLR SVAFPCISTG VFGYPCEAAA EIVLATLREW LEQHKDKVDR
LIICVFLEKD EDIYRSRLPH YFPVA


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