Q694C1 (ABC3G_GORGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA dC->dU-editing enzyme APOBEC-3G
EC=3.5.4.14

Alternative name(s):
Deoxycytidine deaminase

Gene names

Name:

APOBEC3G

Organism

Gorilla gorilla gorilla (Lowland gorilla) [Reference proteome]

Taxonomic identifier

9595 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Gorilla › Gorilla gorilla

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Evidence 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, EIF2C2/AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with EIF2C1/AGO1, EIF2C3/AGO3 and PKA/PRKACA By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cytoplasm › P-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.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA cytosine deamination Inferred from sequence or structural similarity. Source: UniProtKB cytidine deamination Inferred from sequence or structural similarity. Source: UniProtKB defense response to virus Inferred from sequence or structural similarity. Source: UniProtKB innate immune response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transposition Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasmic mRNA processing body Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	deoxycytidine deaminase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 384	384	DNA dC->dU-editing enzyme APOBEC-3G		PRO_0000171760
Regions
	Domain	65 – 100	36	CMP/dCMP deaminase zinc-binding 1
	Domain	257 – 291	35	CMP/dCMP deaminase zinc-binding 2
	Region	1 – 60	60	Essential for cytoplasmic localization By similarity
	Region	209 – 336	128	Necessary for homooligomerization By similarity
	Region	213 – 215	3	Interaction with DNA By similarity
	Region	313 – 320	8	Interaction with DNA By similarity
Sites
	Active site	259	1	Proton donor By similarity
	Metal binding	65	1	Zinc By similarity
	Metal binding	97	1	Zinc By similarity
	Metal binding	100	1	Zinc By similarity
	Metal binding	257	1	Zinc; catalytic By similarity
	Metal binding	288	1	Zinc; catalytic By similarity
	Metal binding	291	1	Zinc; catalytic By similarity
	Site	244	1	Interaction with DNA By similarity
Amino acid modifications
	Modified residue	32	1	Phosphothreonine; by PKA By similarity
	Modified residue	218	1	Phosphothreonine; by PKA and CAMK2 By similarity
Experimental info
	Sequence conflict	3	1	P → S in AAT72157. Ref.1
	Sequence conflict	62	1	L → F in AAT72157. Ref.1
	Sequence conflict	352	1	Y → D in AAT72157. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q694C1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 7BA709E91D3C68DA	FASTA	384	46,269
	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

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 , AY622546, AY622547, AY622548, AY622549, AY622550, AY622551, AY622552 Genomic DNA. Translation: AAT44394.1.
3D structure databases
ProteinModelPortal	Q694C1.
SMR	Q694C1. Positions 198-384.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG050434.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR013158. APOBEC_N. IPR016193. Cytidine_deaminase-like. [Graphical view]
Pfam	PF08210. APOBEC_N. 2 hits. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ABC3G_GORGO

Accession

Primary (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:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program