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Protein

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

Gene

APOBEC3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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

Keywordsi

Molecular functionHydrolase
Biological processAntiviral defense, Immunity, Innate immunity
LigandMetal-binding, Zinc

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000128383.12
HGNCiHGNC:17343 APOBEC3A
MIMi607109 gene
neXtProtiNX_P31941

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, 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
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
ProteomicsDBi54806
54807 [P31941-2]

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
HPA056980
HPA066719

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi128318, 2 interactors
DIPiDIP-61365N
IntActiP31941, 2 interactors
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 – 41Combined sources10
Beta strandi44 – 47Combined sources4
Helixi49 – 51Combined sources3
Beta strandi53 – 56Combined sources4
Turni62 – 65Combined sources4
Helixi71 – 82Combined sources12
Beta strandi88 – 98Combined sources11
Turni103 – 105Combined sources3
Helixi106 – 116Combined sources11
Beta strandi120 – 128Combined sources9
Helixi136 – 145Combined sources10
Beta strandi149 – 152Combined sources4
Helixi155 – 165Combined sources11
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[»]
5KEGX-ray2.20A1-199[»]
5SWWX-ray3.15A/B/C/D1-196[»]
ProteinModelPortaliP31941
SMRiP31941
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410JNPI Eukaryota
ENOG4111DZ4 LUCA
GeneTreeiENSGT00530000062933
HOGENOMiHOG000033754
HOVERGENiHBG050434
KOiK18750
OMAiSGPRHLM
OrthoDBiEOG091G07EI
PhylomeDBiP31941
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

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 dbSNP:rs17000556Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiABC3A_HUMAN
AccessioniPrimary (citable) accession number: P31941
Secondary accession number(s): A0AVM1
, Q12807, Q5JZ93, Q9UH18
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 11, 2001
Last modified: June 20, 2018
This is version 158 of the entry and version 3 of the sequence. See 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

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

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