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Protein

DNA dC->dU-editing enzyme APOBEC-3A

Gene

APOBEC3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA deaminase (cytidine deaminase) with restriction activity against viruses, foreign DNA and mobility of retrotransposons. Exhibits antiviral activity against adeno-associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. Selectively targets single-stranded DNA and can deaminate both methylcytosine and cytosine in foreign DNA. Can induce somatic hypermutation in the nuclear and mitochondrial DNA. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.12 Publications

Catalytic activityi

Cytidine + H2O = uridine + NH3.4 Publications

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi70Zinc; catalyticBy similarity1
Active sitei72Proton donorBy similarity1
Metal bindingi101Zinc; catalyticBy similarity1
Metal bindingi106Zinc; catalyticBy similarity1

GO - Molecular functioni

  • cytidine deaminase activity Source: UniProtKB
  • deoxycytidine deaminase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to xenobiotic stimulus Source: UniProtKB
  • clearance of foreign intracellular DNA by conversion of DNA cytidine to uridine Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • DNA cytosine deamination Source: UniProtKB
  • DNA demethylation Source: UniProtKB
  • innate immune response Source: UniProtKB
  • negative regulation of transposition Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128383-MONOMER.
ReactomeiR-HSA-72200. mRNA Editing: C to U Conversion.
R-HSA-75094. Formation of the Editosome.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA dC->dU-editing enzyme APOBEC-3A (EC:3.5.4.-)
Short name:
A3A
Alternative name(s):
Phorbolin-1
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:17343. APOBEC3A.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi28R → E: No effect on deaminase activity despite an altered restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi29H → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi30K → F: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi57N → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi60K → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi69R → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi70H → R: Altered deaminase activity. 1 Publication1
Mutagenesisi72E → Q: Altered deaminase activity and restriction activity towards genetic invaders. 2 Publications1
Mutagenesisi98W → L: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi106C → S: Altered deaminase activity. 1 Publication1
Mutagenesisi128R → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi130Y → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi131D → N: No effect on deaminase activity despite an altered restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi133D → N: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1
Mutagenesisi136Y → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication1

Organism-specific databases

DisGeNETi100913187.
200315.
OpenTargetsiENSG00000128383.
ENSG00000262156.
PharmGKBiPA24891.

Chemistry databases

ChEMBLiCHEMBL1741179.

Polymorphism and mutation databases

BioMutaiAPOBEC3A.
DMDMi12644206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001717521 – 199DNA dC->dU-editing enzyme APOBEC-3AAdd BLAST199

Proteomic databases

MaxQBiP31941.
PaxDbiP31941.
PeptideAtlasiP31941.
PRIDEiP31941.

PTM databases

iPTMnetiP31941.
PhosphoSitePlusiP31941.

Expressioni

Tissue specificityi

Expressed in peripheral leukocytes with higher expression in CD14-positive phagocytic cells. Highly expressed in keratinocytes and in periphery blood monocytes. Also detected in non-lymphoid tissues including lung and adipose tissues. Found at high levels in colorectal adenocarcinoma, Burkitt's lymphoma and chronic myelogenous leukemia.4 Publications

Inductioni

Up-regulated by interferon and CpG single-stranded DNA (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000128383.
CleanExiHS_APOBEC3A.
ExpressionAtlasiP31941. baseline and differential.
GenevisibleiP31941. HS.

Organism-specific databases

HPAiHPA043237.

Interactioni

Subunit structurei

Interacts with AGO2. Interacts with TRIB3 (via N-terminus).2 Publications

Protein-protein interaction databases

BioGridi128318. 2 interactors.
DIPiDIP-61365N.
STRINGi9606.ENSP00000249116.

Chemistry databases

BindingDBiP31941.

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 21Combined sources7
Beta strandi24 – 26Combined sources3
Beta strandi27 – 29Combined sources3
Beta strandi32 – 39Combined sources8
Beta strandi44 – 47Combined sources4
Beta strandi53 – 56Combined sources4
Turni62 – 65Combined sources4
Helixi71 – 82Combined sources12
Beta strandi90 – 98Combined sources9
Turni103 – 105Combined sources3
Helixi106 – 116Combined sources11
Beta strandi120 – 128Combined sources9
Helixi136 – 144Combined sources9
Turni145 – 147Combined sources3
Beta strandi148 – 152Combined sources5
Helixi155 – 164Combined sources10
Helixi179 – 195Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M65NMR-A1-199[»]
4XXOX-ray2.84A/B1-199[»]
ProteinModelPortaliP31941.
SMRiP31941.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 143CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST117

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410JNPI. Eukaryota.
ENOG4111DZ4. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033754.
HOVERGENiHBG050434.
KOiK18750.
OMAiSGPRHLM.
OrthoDBiEOG091G07EI.
PhylomeDBiP31941.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P31941-1) [UniParc]FASTAAdd to basket
Also known as: Phorbolin-1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEASPASGPR HLMDPHIFTS NFNNGIGRHK TYLCYEVERL DNGTSVKMDQ
60 70 80 90 100
HRGFLHNQAK NLLCGFYGRH AELRFLDLVP SLQLDPAQIY RVTWFISWSP
110 120 130 140 150
CFSWGCAGEV RAFLQENTHV RLRIFAARIY DYDPLYKEAL QMLRDAGAQV
160 170 180 190
SIMTYDEFKH CWDTFVDHQG CPFQPWDGLD EHSQALSGRL RAILQNQGN
Note: Enzymatically active.
Length:199
Mass (Da):23,012
Last modified:January 11, 2001 - v3
Checksum:i42E99E0D7DF7AA14
GO
Isoform 2 (identifier: P31941-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.

Note: Enzymatically active.
Show »
Length:187
Mass (Da):21,778
Checksum:iC7901DFD6A693D9D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04872119T → A.Corresponds to variant rs17000556dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0417231 – 12Missing in isoform 2. CuratedAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03891 mRNA. Translation: AAA03706.2.
CR456393 mRNA. Translation: CAG30279.1.
AL022318 Genomic DNA. Translation: CAI17897.1.
BC126416 mRNA. Translation: AAI26417.1.
CCDSiCCDS13981.1. [P31941-1]
PIRiG01233.
RefSeqiNP_001180218.1. NM_001193289.1. [P31941-1]
NP_663745.1. NM_145699.3. [P31941-1]
UniGeneiHs.226307.

Genome annotation databases

EnsembliENST00000249116; ENSP00000249116; ENSG00000128383. [P31941-1]
ENST00000402255; ENSP00000384359; ENSG00000128383. [P31941-1]
ENST00000570508; ENSP00000461288; ENSG00000262156. [P31941-1]
ENST00000618553; ENSP00000481904; ENSG00000128383. [P31941-1]
ENST00000623492; ENSP00000485234; ENSG00000262156. [P31941-1]
GeneIDi100913187.
200315.
KEGGihsa:100913187.
hsa:200315.
UCSCiuc003awn.2. human. [P31941-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03891 mRNA. Translation: AAA03706.2.
CR456393 mRNA. Translation: CAG30279.1.
AL022318 Genomic DNA. Translation: CAI17897.1.
BC126416 mRNA. Translation: AAI26417.1.
CCDSiCCDS13981.1. [P31941-1]
PIRiG01233.
RefSeqiNP_001180218.1. NM_001193289.1. [P31941-1]
NP_663745.1. NM_145699.3. [P31941-1]
UniGeneiHs.226307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M65NMR-A1-199[»]
4XXOX-ray2.84A/B1-199[»]
ProteinModelPortaliP31941.
SMRiP31941.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128318. 2 interactors.
DIPiDIP-61365N.
STRINGi9606.ENSP00000249116.

Chemistry databases

BindingDBiP31941.
ChEMBLiCHEMBL1741179.

PTM databases

iPTMnetiP31941.
PhosphoSitePlusiP31941.

Polymorphism and mutation databases

BioMutaiAPOBEC3A.
DMDMi12644206.

Proteomic databases

MaxQBiP31941.
PaxDbiP31941.
PeptideAtlasiP31941.
PRIDEiP31941.

Protocols and materials databases

DNASUi200315.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249116; ENSP00000249116; ENSG00000128383. [P31941-1]
ENST00000402255; ENSP00000384359; ENSG00000128383. [P31941-1]
ENST00000570508; ENSP00000461288; ENSG00000262156. [P31941-1]
ENST00000618553; ENSP00000481904; ENSG00000128383. [P31941-1]
ENST00000623492; ENSP00000485234; ENSG00000262156. [P31941-1]
GeneIDi100913187.
200315.
KEGGihsa:100913187.
hsa:200315.
UCSCiuc003awn.2. human. [P31941-1]

Organism-specific databases

CTDi100913187.
200315.
DisGeNETi100913187.
200315.
GeneCardsiAPOBEC3A.
HGNCiHGNC:17343. APOBEC3A.
HPAiHPA043237.
MIMi607109. gene.
neXtProtiNX_P31941.
OpenTargetsiENSG00000128383.
ENSG00000262156.
PharmGKBiPA24891.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JNPI. Eukaryota.
ENOG4111DZ4. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033754.
HOVERGENiHBG050434.
KOiK18750.
OMAiSGPRHLM.
OrthoDBiEOG091G07EI.
PhylomeDBiP31941.
TreeFamiTF331356.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128383-MONOMER.
ReactomeiR-HSA-72200. mRNA Editing: C to U Conversion.
R-HSA-75094. Formation of the Editosome.

Miscellaneous databases

PROiP31941.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128383.
CleanExiHS_APOBEC3A.
ExpressionAtlasiP31941. baseline and differential.
GenevisibleiP31941. HS.

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...

Entry informationi

Entry nameiABC3A_HUMAN
AccessioniPrimary (citable) accession number: P31941
Secondary accession number(s): A0AVM1
, Q12807, Q5JZ93, Q9UH18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.