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Q694C1

- ABC3G_GORGO

UniProt

Q694C1 - ABC3G_GORGO

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
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      Previous versions | rss
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    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

    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

    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.

    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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    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

    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.

    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 1, 2014
    This is version 50 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