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Protein

O-acetyl-ADP-ribose deacetylase MACROD1

Gene

Macrod1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage

Names & Taxonomyi

Protein namesi
Recommended name:
O-acetyl-ADP-ribose deacetylase MACROD1 (EC:3.2.2.-, EC:3.5.1.-)
Alternative name(s):
MACRO domain-containing protein 1
Protein LRP16
[Protein ADP-ribosylglutamate] hydrolase
Gene namesi
Name:Macrod1
Synonyms:Lrp16
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628701. Macrod1.

Subcellular locationi

  • Nucleus By similarity

  • Note: Recruited to DNA lesions, probably via mono-APD-ribosylated proteins.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 258›258O-acetyl-ADP-ribose deacetylase MACROD1PRO_0000084487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291N6-succinyllysineBy similarity
Modified residuei36 – 361N6-succinyllysineBy similarity
Modified residuei62 – 621N6-succinyllysineBy similarity
Modified residuei96 – 961N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ8K4G6.

PTM databases

iPTMnetiQ8K4G6.

Interactioni

Subunit structurei

Interacts with ESR1. Interacts with AR (via macro domain).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8K4G6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 255182MacroPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni92 – 943Substrate bindingBy similarity
Regioni105 – 1073Substrate bindingBy similarity
Regioni112 – 1176Substrate bindingBy similarity
Regioni200 – 2067Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 Macro domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000086960.
HOVERGENiHBG105179.
InParanoidiQ8K4G6.
PhylomeDBiQ8K4G6.

Family and domain databases

InterProiIPR002589. Macro_dom.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q8K4G6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AAGRGAWVRT WAPLAMAAKV DLSTSTDWKE AKSFLKGLSD KQREEHYFCK
60 70 80 90 100
DFIKLKKIPM WKETAKGLAG KVENPKYKKD KQLNEKISLF RGDITKLEVD
110 120 130 140 150
AIVNAANNSL LGGGGVDGCI HRAAGSLLTD ECRTLQNCET GKAKITCGYR
160 170 180 190 200
LPAKHVIHTV GPIAVGQPTA SQAAELRSCY LSSLDLLLEH RLRSVAFPCI
210 220 230 240 250
STGVFGYPNE EAAEVVLATL REWLEQHKDK VDRLIICVFL EKDEGIYQER

LPHYFPVA
Length:258
Mass (Da):28,643
Last modified:June 16, 2003 - v2
Checksum:iFB430516A12D6B42
GO

Sequence cautioni

The sequence AAM45760.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF404762 mRNA. Translation: AAM45760.1. Different initiation.
RefSeqiNP_647553.1. NM_139337.1.
UniGeneiRn.98178.

Genome annotation databases

GeneIDi246233.
KEGGirno:246233.
UCSCiRGD:628701. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF404762 mRNA. Translation: AAM45760.1. Different initiation.
RefSeqiNP_647553.1. NM_139337.1.
UniGeneiRn.98178.

3D structure databases

ProteinModelPortaliQ8K4G6.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ8K4G6.

Proteomic databases

PRIDEiQ8K4G6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi246233.
KEGGirno:246233.
UCSCiRGD:628701. rat.

Organism-specific databases

CTDi28992.
RGDi628701. Macrod1.

Phylogenomic databases

HOGENOMiHOG000086960.
HOVERGENiHBG105179.
InParanoidiQ8K4G6.
PhylomeDBiQ8K4G6.

Family and domain databases

InterProiIPR002589. Macro_dom.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Rat mRNA sequence similar to LRP16 protein of humans."
    Zhang X., Ip N.Y.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiMACD1_RAT
AccessioniPrimary (citable) accession number: Q8K4G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: June 8, 2016
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.