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Q694C1

- ABC3G_GORGO

UniProt

Q694C1 - ABC3G_GORGO

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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.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 – 651ZincBy similarity
Metal bindingi97 – 971ZincBy similarity
Metal bindingi100 – 1001ZincBy similarity
Sitei244 – 2441Interaction with DNABy similarity
Metal bindingi257 – 2571Zinc; catalyticBy similarity
Active sitei259 – 2591Proton donorBy similarity
Metal bindingi288 – 2881Zinc; catalyticBy similarity
Metal bindingi291 – 2911Zinc; catalyticBy 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-KW
  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 PKABy similarity
Modified residuei218 – 2181Phosphothreonine; by PKA and CAMK2By 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.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ694C1.
SMRiQ694C1. Positions 198-384.
ModBaseiSearch...
MobiDBiSearch...

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 localizationBy similarityAdd
BLAST
Regioni209 – 336128Necessary for homooligomerizationBy similarityAdd
BLAST
Regioni213 – 2153Interaction with DNABy similarity
Regioni313 – 3208Interaction with DNABy 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.
InParanoidiQ694C1.

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

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        10         20         30         40         50
MTPQFRNTVE RMYRDTFSYN FNNRPILSRR NTVWLCYEVK TKDPSRPPLD
60 70 80 90 100
AKIFRGQVYS ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC
110 120 130 140 150
TRNVATFLAE DPKVTLTIFV ARLYYFWDQD YQEALRSLCQ KRDGPRATMK
160 170 180 190 200
IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK YYMLLHIMLG EILRHSMDPP
210 220 230 240 250
TFTSNFNNEH WVRGRHETYL CYEVERLHND TWVLLNQRRG FLCNQAPHKH
260 270 280 290 300
GFLEGRHAEL CFLDVIPFWK LDLHQDYRVT CFTSWSPCFS CAQEMAKFIS
310 320 330 340 350
NKKHVSLCIF AARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF
360 370 380
VYHQGCPFQP WDGLEEHSQA LSGRLQAILQ NQGN
Length:384
Mass (Da):46,269
Last modified:September 13, 2004 - v1
Checksum:i7BA709E91D3C68DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31P → S in AAT72157. (PubMed:15198990)Curated
Sequence conflicti62 – 621L → F in AAT72157. (PubMed:15198990)Curated
Sequence conflicti352 – 3521Y → D in AAT72157. (PubMed:15198990)Curated

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.
InParanoidi Q694C1.

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: October 29, 2014
This is version 51 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