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Protein

C->U-editing enzyme APOBEC-1

Gene

Apobec1

Organism
Rattus norvegicus (Rat)
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.By similarity

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

  • AU-rich element binding Source: Ensembl
  • cytidine deaminase activity Source: UniProtKB
  • cytosine deaminase activity Source: RGD
  • enzyme activator activity Source: RGD
  • mRNA binding Source: RGD
  • protein domain specific binding Source: RGD
  • ribonucleoprotein complex binding Source: RGD
  • RNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.36. 5301.
ReactomeiR-RNO-72200. mRNA Editing: C to U Conversion.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2133. Apobec1.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229C->U-editing enzyme APOBEC-1PRO_0000171748Add
BLAST

Proteomic databases

PaxDbiP38483.
PRIDEiP38483.

PTM databases

PhosphoSiteiP38483.

Expressioni

Tissue specificityi

Expressed in the liver as well as small intestine.

Gene expression databases

GenevisibleiP38483. RN.

Interactioni

Subunit structurei

Homodimer. Part of the apolipoprotein B mRNA editing complex with A1CF. Interacts with SYNCRIP. Interacts with HNRPAB.By similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020735.

Structurei

3D structure databases

ProteinModelPortaliP38483.
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.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033766.
HOVERGENiHBG050445.
InParanoidiP38483.
KOiK16932.
OMAiNFVNYPP.
OrthoDBiEOG7NGQCB.
PhylomeDBiP38483.
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.

P38483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSETGPVAV DPTLRRRIEP HEFEVFFDPR ELRKETCLLY EINWGGRHSI
60 70 80 90 100
WRHTSQNTNK HVEVNFIEKF TTERYFCPNT RCSITWFLSW SPCGECSRAI
110 120 130 140 150
TEFLSRYPHV TLFIYIARLY HHADPRNRQG LRDLISSGVT IQIMTEQESG
160 170 180 190 200
YCWRNFVNYS PSNEAHWPRY PHLWVRLYVL ELYCIILGLP PCLNILRRKQ
210 220
PQLTFFTIAL QSCHYQRLPP HILWATGLK
Length:229
Mass (Da):27,274
Last modified:October 1, 1994 - v1
Checksum:i08766441882789B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07114 mRNA. Translation: AAA17394.1.
BC085335 mRNA. Translation: AAH85335.1.
PIRiI59577.
RefSeqiNP_037039.1. NM_012907.2.
XP_006237352.1. XM_006237290.2.
XP_006237353.1. XM_006237291.2.
XP_006237354.1. XM_006237292.2.
XP_006237355.1. XM_006237293.2.
XP_008761442.1. XM_008763220.1.
UniGeneiRn.10002.

Genome annotation databases

EnsembliENSRNOT00000020735; ENSRNOP00000020735; ENSRNOG00000015411.
GeneIDi25383.
KEGGirno:25383.
UCSCiRGD:2133. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07114 mRNA. Translation: AAA17394.1.
BC085335 mRNA. Translation: AAH85335.1.
PIRiI59577.
RefSeqiNP_037039.1. NM_012907.2.
XP_006237352.1. XM_006237290.2.
XP_006237353.1. XM_006237291.2.
XP_006237354.1. XM_006237292.2.
XP_006237355.1. XM_006237293.2.
XP_008761442.1. XM_008763220.1.
UniGeneiRn.10002.

3D structure databases

ProteinModelPortaliP38483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020735.

PTM databases

PhosphoSiteiP38483.

Proteomic databases

PaxDbiP38483.
PRIDEiP38483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020735; ENSRNOP00000020735; ENSRNOG00000015411.
GeneIDi25383.
KEGGirno:25383.
UCSCiRGD:2133. rat.

Organism-specific databases

CTDi339.
RGDi2133. Apobec1.

Phylogenomic databases

eggNOGiENOG410IKDF. Eukaryota.
ENOG4111BJA. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033766.
HOVERGENiHBG050445.
InParanoidiP38483.
KOiK16932.
OMAiNFVNYPP.
OrthoDBiEOG7NGQCB.
PhylomeDBiP38483.
TreeFamiTF331356.

Enzyme and pathway databases

BRENDAi3.5.4.36. 5301.
ReactomeiR-RNO-72200. mRNA Editing: C to U Conversion.
R-RNO-75094. Formation of the Editosome.

Miscellaneous databases

NextBioi606431.
PROiP38483.

Gene expression databases

GenevisibleiP38483. RN.

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. "Molecular cloning of an apolipoprotein B messenger RNA editing protein."
    Teng B., Burant C.F., Davidson N.O.
    Science 260:1816-1819(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    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].
    Tissue: Ovary.
  3. "Molecular cloning of APOBEC-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA."
    Mehta A., Kinter M.T., Sherman N.E., Driscoll D.M.
    Mol. Cell. Biol. 20:1846-1854(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH A1CF.
  4. "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing."
    Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A., Scott J., Davidson N.O.
    J. Biol. Chem. 276:10272-10283(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNCRIP.

Entry informationi

Entry nameiABEC1_RAT
AccessioniPrimary (citable) accession number: P38483
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: December 9, 2015
This is version 122 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. 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.