SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q694C1

- ABC3G_GORGO

UniProt

Q694C1 - ABC3G_GORGO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene
APOBEC3G
Organism
Gorilla gorilla gorilla (Lowland gorilla)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

Deoxycytidine + H2O = deoxyuridine + NH3.

Cofactori

Zinc By similarity.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651Zinc By similarity
Metal bindingi97 – 971Zinc By similarity
Metal bindingi100 – 1001Zinc By similarity
Sitei244 – 2441Interaction with DNA By similarity
Metal bindingi257 – 2571Zinc; catalytic By similarity
Active sitei259 – 2591Proton donor By similarity
Metal bindingi288 – 2881Zinc; catalytic By similarity
Metal bindingi291 – 2911Zinc; catalytic By similarity

GO - Molecular functioni

  1. deoxycytidine deaminase activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. cytidine deamination Source: UniProtKB
  2. defense response to virus Source: UniProtKB
  3. DNA cytosine deamination Source: UniProtKB
  4. innate immune response Source: UniProtKB-KW
  5. negative regulation of transposition Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA dC->dU-editing enzyme APOBEC-3G (EC:3.5.4.-)
Alternative name(s):
Deoxycytidine deaminase
Gene namesi
Name:APOBEC3G
OrganismiGorilla gorilla gorilla (Lowland gorilla)
Taxonomic identifieri9595 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeGorilla
ProteomesiUP000001519: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic mRNA processing body Source: UniProtKB
  3. nucleus Source: UniProtKB-SubCell
  4. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384DNA dC->dU-editing enzyme APOBEC-3GPRO_0000171760Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphothreonine; by PKA By similarity
Modified residuei218 – 2181Phosphothreonine; by PKA and CAMK2 By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ694C1.
SMRiQ694C1. Positions 198-384.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 10036CMP/dCMP deaminase zinc-binding 1Add
BLAST
Domaini257 – 29135CMP/dCMP deaminase zinc-binding 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060Essential for cytoplasmic localization By similarityAdd
BLAST
Regioni209 – 336128Necessary for homooligomerization By similarityAdd
BLAST
Regioni213 – 2153Interaction with DNA By similarity
Regioni313 – 3208Interaction with DNA By similarity

Domaini

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 similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG050434.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF08210. APOBEC_N. 2 hits.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 2 hits.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q694C1-1 [UniParc]FASTAAdd to Basket

« Hide

MTPQFRNTVE RMYRDTFSYN FNNRPILSRR NTVWLCYEVK TKDPSRPPLD    50
AKIFRGQVYS ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC 100
TRNVATFLAE DPKVTLTIFV ARLYYFWDQD YQEALRSLCQ KRDGPRATMK 150
IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK YYMLLHIMLG EILRHSMDPP 200
TFTSNFNNEH WVRGRHETYL CYEVERLHND TWVLLNQRRG FLCNQAPHKH 250
GFLEGRHAEL CFLDVIPFWK LDLHQDYRVT CFTSWSPCFS CAQEMAKFIS 300
NKKHVSLCIF AARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF 350
VYHQGCPFQP WDGLEEHSQA LSGRLQAILQ NQGN 384
Length:384
Mass (Da):46,269
Last modified:September 13, 2004 - v1
Checksum:i7BA709E91D3C68DA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31P → S in AAT72157. 1 Publication
Sequence conflicti62 – 621L → F in AAT72157. 1 Publication
Sequence conflicti352 – 3521Y → D in AAT72157. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY639868 mRNA. Translation: AAT72157.1.
AY622553
, AY622546, AY622547, AY622548, AY622549, AY622550, AY622551, AY622552 Genomic DNA. Translation: AAT44394.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY639868 mRNA. Translation: AAT72157.1 .
AY622553
, AY622546 , AY622547 , AY622548 , AY622549 , AY622550 , AY622551 , AY622552 Genomic DNA. Translation: AAT44394.1 .

3D structure databases

ProteinModelPortali Q694C1.
SMRi Q694C1. Positions 198-384.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG050434.

Family and domain databases

InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view ]
Pfami PF08210. APOBEC_N. 2 hits.
[Graphical view ]
SUPFAMi SSF53927. SSF53927. 2 hits.
PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiABC3G_GORGO
AccessioniPrimary (citable) accession number: Q694C1
Secondary accession number(s): Q6DVQ0
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi