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Protein

C->U-editing enzyme APOBEC-1

Gene

Apobec1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi61Zinc; catalyticBy similarity1
Active sitei63Proton donorBy similarity1
Metal bindingi93Zinc; catalyticBy similarity1
Metal bindingi96Zinc; catalyticBy similarity1

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
  • negative regulation of triglyceride metabolic process Source: MGI
  • positive regulation of mRNA modification Source: Ensembl
  • regulation of cell proliferation Source: MGI
  • response to calcium ion 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
  • triglyceride metabolic process Source: MGI

Keywordsi

Molecular functionHydrolase
Biological processmRNA processing
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:103298 Apobec1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001717451 – 229C->U-editing enzyme APOBEC-1Add BLAST229

Proteomic databases

PaxDbiP51908
PeptideAtlasiP51908
PRIDEiP51908

PTM databases

iPTMnetiP51908
PhosphoSitePlusiP51908

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000040613
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 interactors
STRINGi10090.ENSMUSP00000108204

Structurei

3D structure databases

ProteinModelPortaliP51908
SMRiP51908
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 134CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST125

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi180 – 193Leu-richAdd BLAST14

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IKDF Eukaryota
ENOG4111BJA LUCA
GeneTreeiENSGT00530000062933
HOGENOMiHOG000033766
HOVERGENiHBG050445
InParanoidiP51908
KOiK16932
OMAiNFVNYPP
OrthoDBiEOG091G0PT8
PhylomeDBiP51908
TreeFamiTF331356

Family and domain databases

InterProiView protein in InterPro
IPR016192 APOBEC/CMP_deaminase_Zn-bd
IPR013158 APOBEC_N
IPR002125 CMP_dCMP_dom
IPR016193 Cytidine_deaminase-like
PfamiView protein in Pfam
PF08210 APOBEC_N, 1 hit
SUPFAMiSSF53927 SSF53927, 1 hit
PROSITEiView protein in PROSITE
PS00903 CYT_DCMP_DEAMINASES_1, 1 hit
PS51747 CYT_DCMP_DEAMINASES_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti106R → Q in AAH03792 (PubMed:15489334).Curated1

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_011241159.2
UniGeneiMm.3333

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiABEC1_MOUSE
AccessioniPrimary (citable) accession number: P51908
Secondary accession number(s): Q99L67
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 148 of the entry and version 1 of the sequence. See 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

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