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Protein

C->U-editing enzyme APOBEC-1

Gene

Apobec1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the APOB mRNA. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.1 Publication

Catalytic activityi

Cytosine(6666) in apolipoprotein B mRNA + H2O = uracil(6666) in apolipoprotein B mRNA + NH3.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 Zn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Zinc; catalyticBy similarity
Active sitei63 – 631Proton donorBy similarity
Metal bindingi93 – 931Zinc; catalyticBy similarity
Metal bindingi96 – 961Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to insulin stimulus Source: Ensembl
  • cytidine to uridine editing Source: MGI
  • defense response to virus Source: Ensembl
  • DNA cytosine deamination Source: Ensembl
  • DNA demethylation Source: UniProtKB
  • lipoprotein biosynthetic process Source: MGI
  • lipoprotein metabolic process Source: MGI
  • lipoprotein transport Source: MGI
  • mRNA modification Source: MGI
  • mRNA processing Source: UniProtKB-KW
  • mRNA stabilization Source: MGI
  • negative regulation of methylation-dependent chromatin silencing Source: UniProtKB
  • positive regulation of mRNA modification Source: Ensembl
  • regulation of cell proliferation Source: MGI
  • response to calcium ion Source: Ensembl
  • response to drug Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to gamma radiation Source: MGI
  • response to osmotic stress Source: Ensembl
  • response to zinc ion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.1. 3474.
3.5.4.36. 3474.
ReactomeiR-MMU-72200. mRNA Editing: C to U Conversion.
R-MMU-75094. Formation of the Editosome.

Names & Taxonomyi

Protein namesi
Recommended name:
C->U-editing enzyme APOBEC-1 (EC:3.5.4.36)
Alternative name(s):
Apolipoprotein B mRNA-editing enzyme 1
mRNA(cytosine(6666)) deaminase 1
Gene namesi
Name:Apobec1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:103298. Apobec1.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229C->U-editing enzyme APOBEC-1PRO_0000171745Add
BLAST

Proteomic databases

PaxDbiP51908.
PRIDEiP51908.

PTM databases

PhosphoSiteiP51908.

Expressioni

Tissue specificityi

Expressed in the spleen. Expressed at lower level in the kidney, testis, lung, brain and liver.1 Publication

Gene expression databases

BgeeiP51908.
CleanExiMM_APOBEC1.
ExpressionAtlasiP51908. baseline and differential.
GenevisibleiP51908. MM.

Interactioni

Subunit structurei

Homodimer. Part of the apolipoprotein B mRNA editing complex with APC. Interacts with HNRPAB and SYNCRIP.By similarity

Protein-protein interaction databases

BioGridi198158. 2 interactions.
STRINGi10090.ENSMUSP00000108204.

Structurei

3D structure databases

ProteinModelPortaliP51908.
SMRiP51908. Positions 18-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 134125CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi180 – 19314Leu-richAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IKDF. Eukaryota.
ENOG4111BJA. LUCA.
HOGENOMiHOG000033766.
HOVERGENiHBG050445.
InParanoidiP51908.
KOiK16932.
OMAiNFVNYPP.
OrthoDBiEOG7NGQCB.
PhylomeDBiP51908.
TreeFamiTF331356.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF08210. APOBEC_N. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSETGPVAV DPTLRRRIEP HEFEVFFDPR ELRKETCLLY EINWGGRHSV
60 70 80 90 100
WRHTSQNTSN HVEVNFLEKF TTERYFRPNT RCSITWFLSW SPCGECSRAI
110 120 130 140 150
TEFLSRHPYV TLFIYIARLY HHTDQRNRQG LRDLISSGVT IQIMTEQEYC
160 170 180 190 200
YCWRNFVNYP PSNEAYWPRY PHLWVKLYVL ELYCIILGLP PCLKILRRKQ
210 220
PQLTFFTITL QTCHYQRIPP HLLWATGLK
Length:229
Mass (Da):27,522
Last modified:October 1, 1996 - v1
Checksum:i1CBCF9929066ABAD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061R → Q in AAH03792 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21951
, U21947, U21948, U21949, U21950 Genomic DNA. Translation: AAC52211.1.
U22262 mRNA. Translation: AAC52212.1.
U22263 mRNA. Translation: AAC52213.1.
U22264 mRNA. Translation: AAC52214.1.
BC003792 mRNA. Translation: AAH03792.1.
CCDSiCCDS20498.1.
PIRiI48249.
RefSeqiNP_001127863.1. NM_001134391.1.
NP_112436.1. NM_031159.3.
XP_006505464.1. XM_006505401.2.
XP_011239461.1. XM_011241159.1.
XP_011239462.1. XM_011241160.1.
UniGeneiMm.3333.

Genome annotation databases

EnsembliENSMUST00000112585; ENSMUSP00000108204; ENSMUSG00000040613.
ENSMUST00000112586; ENSMUSP00000108205; ENSMUSG00000040613.
ENSMUST00000112587; ENSMUSP00000108206; ENSMUSG00000040613.
GeneIDi11810.
KEGGimmu:11810.
UCSCiuc009dpk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21951
, U21947, U21948, U21949, U21950 Genomic DNA. Translation: AAC52211.1.
U22262 mRNA. Translation: AAC52212.1.
U22263 mRNA. Translation: AAC52213.1.
U22264 mRNA. Translation: AAC52214.1.
BC003792 mRNA. Translation: AAH03792.1.
CCDSiCCDS20498.1.
PIRiI48249.
RefSeqiNP_001127863.1. NM_001134391.1.
NP_112436.1. NM_031159.3.
XP_006505464.1. XM_006505401.2.
XP_011239461.1. XM_011241159.1.
XP_011239462.1. XM_011241160.1.
UniGeneiMm.3333.

3D structure databases

ProteinModelPortaliP51908.
SMRiP51908. Positions 18-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198158. 2 interactions.
STRINGi10090.ENSMUSP00000108204.

PTM databases

PhosphoSiteiP51908.

Proteomic databases

PaxDbiP51908.
PRIDEiP51908.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112585; ENSMUSP00000108204; ENSMUSG00000040613.
ENSMUST00000112586; ENSMUSP00000108205; ENSMUSG00000040613.
ENSMUST00000112587; ENSMUSP00000108206; ENSMUSG00000040613.
GeneIDi11810.
KEGGimmu:11810.
UCSCiuc009dpk.1. mouse.

Organism-specific databases

CTDi339.
MGIiMGI:103298. Apobec1.

Phylogenomic databases

eggNOGiENOG410IKDF. Eukaryota.
ENOG4111BJA. LUCA.
HOGENOMiHOG000033766.
HOVERGENiHBG050445.
InParanoidiP51908.
KOiK16932.
OMAiNFVNYPP.
OrthoDBiEOG7NGQCB.
PhylomeDBiP51908.
TreeFamiTF331356.

Enzyme and pathway databases

BRENDAi3.5.4.1. 3474.
3.5.4.36. 3474.
ReactomeiR-MMU-72200. mRNA Editing: C to U Conversion.
R-MMU-75094. Formation of the Editosome.

Miscellaneous databases

NextBioi279679.
PROiP51908.
SOURCEiSearch...

Gene expression databases

BgeeiP51908.
CleanExiMM_APOBEC1.
ExpressionAtlasiP51908. baseline and differential.
GenevisibleiP51908. MM.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF08210. APOBEC_N. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Alternative mRNA splicing and differential promoter utilization determine tissue-specific expression of the apolipoprotein B mRNA-editing protein (Apobec1) gene in mice. Structure and evolution of Apobec1 and related nucleoside/nucleotide deaminases."
    Nakamuta M., Oka K., Krushkal J., Kobayashi K., Yamamoto M., Li W.H., Chan L.
    J. Biol. Chem. 270:13042-13056(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Small intestine.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: TISSUE SPECIFICITY.
  4. "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain."
    Guo J.U., Su Y., Zhong C., Ming G.L., Song H.
    Cell 145:423-434(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA DEMETHYLATION.

Entry informationi

Entry nameiABEC1_MOUSE
AccessioniPrimary (citable) accession number: P51908
Secondary accession number(s): Q99L67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 134 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.