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Protein

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

Gene

APOBEC3C

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

Functioni

DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.6 Publications

Catalytic activityi

Cytidine + H2O = uridine + NH3.

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi66Zinc; catalyticBy similarity1
Active sitei68Proton donorBy similarity1
Metal bindingi97Zinc; catalyticBy similarity1
Metal bindingi100Zinc; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cytidine deamination Source: UniProtKB
  • defense response to virus Source: UniProtKB-KW
  • DNA demethylation Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • 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, Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

Metal-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-3C (EC:3.5.4.-)
Short name:
A3C
Alternative name(s):
APOBEC1-like
Phorbolin I
Gene namesi
Name:APOBEC3C
Synonyms:APOBEC1L, PBI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:17353. APOBEC3C.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi27350.
OpenTargetsiENSG00000244509.
PharmGKBiPA24893.

Polymorphism and mutation databases

BioMutaiAPOBEC3C.
DMDMi48474983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001717551 – 190DNA dC->dU-editing enzyme APOBEC-3CAdd BLAST190

Proteomic databases

EPDiQ9NRW3.
MaxQBiQ9NRW3.
PaxDbiQ9NRW3.
PeptideAtlasiQ9NRW3.
PRIDEiQ9NRW3.

PTM databases

iPTMnetiQ9NRW3.
PhosphoSitePlusiQ9NRW3.

Expressioni

Tissue specificityi

Expressed in spleen, testes, peripherical blood lymphocytes, heart, thymus, prostate and ovary.2 Publications

Inductioni

Up-regulated by IFN-alpha.

Gene expression databases

BgeeiENSG00000244509.
CleanExiHS_APOBEC3C.
ExpressionAtlasiQ9NRW3. baseline and differential.
GenevisibleiQ9NRW3. HS.

Organism-specific databases

HPAiCAB033048.

Interactioni

Subunit structurei

Homodimer. Interacts with human foamy virus protein Bet; this interaction does not induce APOBEC3C degradation, but prevents dimerization and incorporation into virion of the latter. Interacts with TRIB3 and AGO2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RBMXP381595EBI-1044593,EBI-743526
RBMY1A1P0DJD33EBI-1044593,EBI-8638511
RBMY1JQ154155EBI-1044593,EBI-8642021

Protein-protein interaction databases

BioGridi118162. 18 interactors.
DIPiDIP-48919N.
IntActiQ9NRW3. 9 interactors.
MINTiMINT-6631470.
STRINGi9606.ENSP00000355340.

Structurei

Secondary structure

1190
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 20Combined sources7
Turni27 – 29Combined sources3
Beta strandi32 – 43Combined sources12
Beta strandi46 – 58Combined sources13
Helixi63 – 65Combined sources3
Helixi67 – 75Combined sources9
Beta strandi84 – 94Combined sources11
Helixi98 – 110Combined sources13
Beta strandi114 – 122Combined sources9
Turni124 – 127Combined sources4
Helixi129 – 141Combined sources13
Beta strandi144 – 147Combined sources4
Helixi150 – 160Combined sources11
Helixi174 – 189Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VM8X-ray3.00A/B1-190[»]
3VOWX-ray2.15A/B1-190[»]
ProteinModelPortaliQ9NRW3.
SMRiQ9NRW3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 138CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST110

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410KG48. Eukaryota.
ENOG4110SPD. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033754.
HOVERGENiHBG050434.
KOiK18750.
OMAiSETHCHA.
OrthoDBiEOG091G07EI.
PhylomeDBiQ9NRW3.
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.

Q9NRW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPQIRNPMK AMYPGTFYFQ FKNLWEANDR NETWLCFTVE GIKRRSVVSW
60 70 80 90 100
KTGVFRNQVD SETHCHAERC FLSWFCDDIL SPNTKYQVTW YTSWSPCPDC
110 120 130 140 150
AGEVAEFLAR HSNVNLTIFT ARLYYFQYPC YQEGLRSLSQ EGVAVEIMDY
160 170 180 190
EDFKYCWENF VYNDNEPFKP WKGLKTNFRL LKRRLRESLQ
Length:190
Mass (Da):22,826
Last modified:March 29, 2004 - v2
Checksum:iBE49E80F95C71214
GO

Sequence cautioni

The sequence AAF86650 differs from that shown. Reason: Frameshift at position 172.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31N → D in AAH11739 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF165520 mRNA. Translation: AAF86650.1. Frameshift.
CR456394 mRNA. Translation: CAG30280.1.
AK313272 mRNA. Translation: BAG36081.1.
AL022318 Genomic DNA. Translation: CAI17898.1.
CH471095 Genomic DNA. Translation: EAW60284.1.
BC011739 mRNA. Translation: AAH11739.1.
BC021080 mRNA. No translation available.
CCDSiCCDS13983.1.
RefSeqiNP_055323.2. NM_014508.2.
UniGeneiHs.441124.

Genome annotation databases

EnsembliENST00000361441; ENSP00000355340; ENSG00000244509.
GeneIDi27350.
KEGGihsa:27350.
UCSCiuc003awr.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF165520 mRNA. Translation: AAF86650.1. Frameshift.
CR456394 mRNA. Translation: CAG30280.1.
AK313272 mRNA. Translation: BAG36081.1.
AL022318 Genomic DNA. Translation: CAI17898.1.
CH471095 Genomic DNA. Translation: EAW60284.1.
BC011739 mRNA. Translation: AAH11739.1.
BC021080 mRNA. No translation available.
CCDSiCCDS13983.1.
RefSeqiNP_055323.2. NM_014508.2.
UniGeneiHs.441124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VM8X-ray3.00A/B1-190[»]
3VOWX-ray2.15A/B1-190[»]
ProteinModelPortaliQ9NRW3.
SMRiQ9NRW3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118162. 18 interactors.
DIPiDIP-48919N.
IntActiQ9NRW3. 9 interactors.
MINTiMINT-6631470.
STRINGi9606.ENSP00000355340.

PTM databases

iPTMnetiQ9NRW3.
PhosphoSitePlusiQ9NRW3.

Polymorphism and mutation databases

BioMutaiAPOBEC3C.
DMDMi48474983.

Proteomic databases

EPDiQ9NRW3.
MaxQBiQ9NRW3.
PaxDbiQ9NRW3.
PeptideAtlasiQ9NRW3.
PRIDEiQ9NRW3.

Protocols and materials databases

DNASUi27350.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361441; ENSP00000355340; ENSG00000244509.
GeneIDi27350.
KEGGihsa:27350.
UCSCiuc003awr.4. human.

Organism-specific databases

CTDi27350.
DisGeNETi27350.
GeneCardsiAPOBEC3C.
HGNCiHGNC:17353. APOBEC3C.
HPAiCAB033048.
MIMi607750. gene.
neXtProtiNX_Q9NRW3.
OpenTargetsiENSG00000244509.
PharmGKBiPA24893.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KG48. Eukaryota.
ENOG4110SPD. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033754.
HOVERGENiHBG050434.
KOiK18750.
OMAiSETHCHA.
OrthoDBiEOG091G07EI.
PhylomeDBiQ9NRW3.
TreeFamiTF331356.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAPOBEC3C. human.
GeneWikiiAPOBEC3C.
GenomeRNAii27350.
PROiQ9NRW3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000244509.
CleanExiHS_APOBEC3C.
ExpressionAtlasiQ9NRW3. baseline and differential.
GenevisibleiQ9NRW3. 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 nameiABC3C_HUMAN
AccessioniPrimary (citable) accession number: Q9NRW3
Secondary accession number(s): B2R884
, Q5JZ92, Q7Z2N7, Q96F12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: November 30, 2016
This is version 134 of the entry and version 2 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, Reference proteome

Documents

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