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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)DescriptionActionsGraphical viewLength
Binding sitei239SubstrateBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_0000084487‹1 – 258O-acetyl-ADP-ribose deacetylase MACROD1Add BLAST›258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei29N6-succinyllysineBy similarity1
Modified residuei36N6-succinyllysineBy similarity1
Modified residuei62N6-succinyllysineBy similarity1
Modified residuei96N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ8K4G6.

PTM databases

iPTMnetiQ8K4G6.
PhosphoSitePlusiQ8K4G6.

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)DescriptionActionsGraphical viewLength
Domaini74 – 255MacroPROSITE-ProRule annotationAdd BLAST182

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni92 – 94Substrate bindingBy similarity3
Regioni105 – 107Substrate bindingBy similarity3
Regioni112 – 117Substrate bindingBy similarity6
Regioni200 – 206Substrate bindingBy similarity7

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

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.
PhosphoSitePlusiQ8K4G6.

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...

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: November 2, 2016
This is version 81 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.