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Q694C1 (ABC3G_GORGO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA dC->dU-editing enzyme APOBEC-3G

EC=3.5.4.-
Alternative name(s):
Deoxycytidine deaminase
Gene names
Name:APOBEC3G
OrganismGorilla gorilla gorilla (Lowland gorilla) [Reference proteome]
Taxonomic identifier9595 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeGorilla

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. 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 By similarity.

Catalytic activity

Deoxycytidine + H2O = deoxyuridine + NH3.

Cofactor

Zinc By similarity.

Enzyme regulation

Assembly into ribonucleoprotein complexes of high-molecular-mass (HMM) inhibits its enzymatic activity By similarity.

Subunit structure

Homodimer. Homooligomer. Can bind RNA to form ribonucleoprotein complexes of high-molecular-mass (HMM) or low-molecular-mass (LMM). HMM is inactive and heterogeneous in protein composition because of binding nonselectively to cellular RNAs, which in turn are associated with variety of cellular proteins. The LMM form which is enzymatically active has few or no RNAs associated. Its ability to form homooligomer is distinct from its ability to assemble into HMM. Interacts with APOBEC3B, APOBEC3F, MOV10, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with AGO1, AGO3 and PKA/PRKACA By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. CytoplasmP-body By similarity. Note: Mainly cytoplasmic, small amount are found in the nucleus By similarity.

Domain

The CMP/dCMP deaminase zinc-binding 1 domain mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase zinc-binding 2 domain confers deoxycytidine deaminase activity and substrate sequence specificity By similarity.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Contains 2 CMP/dCMP deaminase zinc-binding domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384DNA dC->dU-editing enzyme APOBEC-3G
PRO_0000171760

Regions

Domain65 – 10036CMP/dCMP deaminase zinc-binding 1
Domain257 – 29135CMP/dCMP deaminase zinc-binding 2
Region1 – 6060Essential for cytoplasmic localization By similarity
Region209 – 336128Necessary for homooligomerization By similarity
Region213 – 2153Interaction with DNA By similarity
Region313 – 3208Interaction with DNA By similarity

Sites

Active site2591Proton donor By similarity
Metal binding651Zinc By similarity
Metal binding971Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding2571Zinc; catalytic By similarity
Metal binding2881Zinc; catalytic By similarity
Metal binding2911Zinc; catalytic By similarity
Site2441Interaction with DNA By similarity

Amino acid modifications

Modified residue321Phosphothreonine; by PKA By similarity
Modified residue2181Phosphothreonine; by PKA and CAMK2 By similarity

Experimental info

Sequence conflict31P → S in AAT72157. Ref.1
Sequence conflict621L → F in AAT72157. Ref.1
Sequence conflict3521Y → D in AAT72157. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q694C1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 7BA709E91D3C68DA

FASTA38446,269
        10         20         30         40         50         60 
MTPQFRNTVE RMYRDTFSYN FNNRPILSRR NTVWLCYEVK TKDPSRPPLD AKIFRGQVYS 

        70         80         90        100        110        120 
ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRNVATFLAE DPKVTLTIFV 

       130        140        150        160        170        180 
ARLYYFWDQD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK 

       190        200        210        220        230        240 
YYMLLHIMLG EILRHSMDPP TFTSNFNNEH WVRGRHETYL CYEVERLHND TWVLLNQRRG 

       250        260        270        280        290        300 
FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLHQDYRVT CFTSWSPCFS CAQEMAKFIS 

       310        320        330        340        350        360 
NKKHVSLCIF AARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VYHQGCPFQP 

       370        380 
WDGLEEHSQA LSGRLQAILQ NQGN 

« Hide

References

[1]"Rapid evolution of primate antiviral enzyme APOBEC3G."
Zhang J., Webb D.M.
Hum. Mol. Genet. 13:1785-1791(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G."
Sawyer S.L., Emerman M., Malik H.S.
PLoS Biol. 2:1278-1285(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY639868 mRNA. Translation: AAT72157.1.
AY622553 expand/collapse EMBL AC list , AY622546, AY622547, AY622548, AY622549, AY622550, AY622551, AY622552 Genomic DNA. Translation: AAT44394.1.

3D structure databases

ProteinModelPortalQ694C1.
SMRQ694C1. Positions 198-384.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG050434.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamPF08210. APOBEC_N. 2 hits.
[Graphical view]
SUPFAMSSF53927. SSF53927. 2 hits.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameABC3G_GORGO
AccessionPrimary (citable) accession number: Q694C1
Secondary accession number(s): Q6DVQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: September 13, 2004
Last modified: April 16, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families