APOBEC3G (Kr.22q13.1), A3G, ARCD, ARP9, CEM15,
MDS019,bK150 2.7
- Also known as
- A3G; ARCD; ARP9; ARP-9; CEM15; CEM-15; MDS019; bK150C2.7; dJ494G10.1
-
Summary
- This gene is a member of the cytidine deaminase gene family. It is
one of seven related genes or pseudogenes found in a cluster,
thought to result from gene duplication, on chromosome 22. Members
of the cluster encode proteins that are structurally and
functionally related to the C to U RNA-editing cytidine deaminase
APOBEC1. The protein encoded by this gene catalyzes site-specific
deamination of both RNA and single-stranded DNA. The encoded protein
has been found to be a specific inhibitor of human immunodeficiency
virus-1 (HIV-1) infectivity. [provided by RefSeq, Mar 2017]
-
Expression
- Broad expression in lymph node (RPKM 19.7), spleen (RPKM 13.4) and
22 other tissues See
more
Peptide structure and history
https://www.ncbi.nlm.nih.gov/protein/NP_001336365.1
DNA AUTHORS Shandilya SM, Nalam MN, Nalivaika EA, Gross PJ, Valesano JC, ShindodC->dU-editing enzyme APOBEC-3G isoform 2 [Homo sapiens]
K, Li M, Munson M, Royer WE, Harjes E, Kono T, Matsuo H, Harris RS,
Somasundaran M and Schiffer CA.
TITLE Crystal structure of the APOBEC3G catalytic domain reveals
potential oligomerization interfaces
JOURNAL Structure 18 (1), 28-38 (2010)
PUBMED 20152150
REMARK GeneRIF: crystal structure of the catalytically active C-terminal
domain of APOBEC3G was determined to 2.25 A.
REFERENCE 3 (residues 1 to 373)
AUTHORS Furukawa A, Nagata T, Matsugami A, Habu Y, Sugiyama R, Hayashi F,
Kobayashi N, Yokoyama S, Takaku H and Katahira M.
TITLE Structure, interaction and real-time monitoring of the enzymatic
reaction of wild-type APOBEC3G
JOURNAL EMBO J. 28 (4), 440-451 (2009)
PUBMED 19153609
REMARK GeneRIF: analysis of the enzymatic reaction of wild-type APOBEC3G
REFERENCE 4 (residues 1 to 373)
AUTHORS Stenglein MD, Matsuo H and Harris RS.
TITLE Two regions within the amino-terminal half of APOBEC3G cooperate to
determine cytoplasmic localization
JOURNAL J. Virol. 82 (19), 9591-9599 (2008)
PUBMED 18667511
REMARK GeneRIF: two regions of APOBEC3G combine to mediate an
intermolecular interaction that controls subcellular localization
REFERENCE 5 (residues 1 to 373)
AUTHORS Gooch BD and Cullen BR.
TITLE Functional domain organization of human APOBEC3G
JOURNAL Virology 379 (1), 118-124 (2008)
PUBMED 18639915
REMARK GeneRIF: Here, the authors demonstrate that the ability to bind to
Gag and package into HIV-1 virions is entirely contained within the
amino-terminal half of A3G.
REFERENCE 6 (residues 1 to 373)
AUTHORS Zhang KL, Mangeat B, Ortiz M, Zoete V, Trono D, Telenti A and
Michielin O.
TITLE Model structure of human APOBEC3G
JOURNAL PLoS ONE 2 (4), e378 (2007)
PUBMED 17440614
REMARK GeneRIF: structure model identifies a cluster of residues important
for packaging of APOBEC3G into virions, and may serve to guide
functional analysis of APOBEC3G
Publication Status: Online-Only
REFERENCE 7 (residues 1 to 373)
AUTHORS Chelico L, Pham P, Calabrese P and Goodman MF.
TITLE APOBEC3G DNA deaminase acts processively 3' --> 5' on
single-stranded DNA
JOURNAL Nat. Struct. Mol. Biol. 13 (5), 392-399 (2006)
PUBMED 16622407
REMARK GeneRIF: G --> A mutational gradient generated in viral genomic DNA
in vivo could result from an intrinsic processive directional
attack by APOBEC3G on single-stranded cDNA
REFERENCE 8 (residues 1 to 373)
AUTHORS An P, Bleiber G, Duggal P, Nelson G, May M, Mangeat B, Alobwede I,
Trono D, Vlahov D, Donfield S, Goedert JJ, Phair J, Buchbinder S,
O'Brien SJ, Telenti A and Winkler CA.
TITLE APOBEC3G genetic variants and their influence on the progression to
AIDS
JOURNAL J. Virol. 78 (20), 11070-11076 (2004)
PUBMED 15452227
REMARK GeneRIF: Observational study of gene-disease association. (HuGE
Navigator)
REFERENCE 9 (residues 1 to 373)
AUTHORS Li J, Potash MJ and Volsky DJ.
TITLE Functional domains of APOBEC3G required for antiviral activity
JOURNAL J. Cell. Biochem. 92 (3), 560-572 (2004)
PUBMED 15156567
REMARK GeneRIF: APOBEC3G inhibits HIV-1 infection through interference
with reverse transcription.
REFERENCE 10 (residues 1 to 373)
AUTHORS Wedekind JE, Dance GS, Sowden MP and Smith HC.
TITLE Messenger RNA editing in mammals: new members of the APOBEC family
seeking roles in the family business
JOURNAL Trends Genet. 19 (4), 207-216 (2003)
PUBMED 12683974
REMARK Review article
Erratum:[Trends Genet. 2003 Jul;19(7):369]
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AL022318.2 and AL078641.2.
Summary: This gene is a member of the cytidine deaminase gene
family. It is one of seven related genes or pseudogenes found in a
cluster, thought to result from gene duplication, on chromosome 22.
Members of the cluster encode proteins that are structurally and
functionally related to the C to U RNA-editing cytidine deaminase
APOBEC1. The protein encoded by this gene catalyzes site-specific
deamination of both RNA and single-stranded DNA. The encoded
protein has been found to be a specific inhibitor of human
immunodeficiency virus-1 (HIV-1) infectivity. [provided by RefSeq,
Mar 2017].
Transcript Variant: This variant (2) differs in the 5' UTR and
coding sequence compared to variant 1. The resulting isoform (2) is
shorter at the N-terminus compared to isoform 1.
Sequence Note: The RefSeq transcript and protein were derived from
genomic sequence to make the sequence consistent with the reference
genome assembly. The genomic coordinates used for the transcript
record were based on alignments.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
CDS exon combination :: BC009683.1, SRR1163657.107174.1
[ECO:0000331]
RNAseq introns :: single sample supports all introns
SAMEA2148093, SAMEA2158800 [ECO:0000348]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..373
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="22"
/map="22q13.1"
Protein 1..373
/product="DNA dC->dU-editing enzyme APOBEC-3G isoform 2"
/EC_number="3.5.4.5"
/note="phorbolin-like protein MDS019; deoxycytidine
deaminase; apolipoprotein B editing enzyme catalytic
polypeptide-like 3G; apolipoprotein B mRNA-editing enzyme
catalytic polypeptide 3G; apolipoprotein B mRNA editing
enzyme, catalytic polypeptide-like 3G; DNA dC->dU-editing
enzyme APOBEC-3G; DNA dC->dU editing enzyme;
APOBEC-related protein 9; APOBEC-related cytidine
deaminase; apolipoprotein B mRNA editing enzyme cytidine
deaminase"
/calculated_mol_wt=44880
Region 6..167
/region_name="APOBEC_N"
/note="APOBEC-like N-terminal domain; pfam08210"
/db_xref="CDD:311913"
Region 191..365
/region_name="APOBEC_N"
/note="APOBEC-like N-terminal domain; pfam08210"
/db_xref="CDD:311913"
CDS 1..373
/gene="APOBEC3G"
/gene_synonym="A3G; ARCD; ARP-9; ARP9; bK150C2.7; CEM-15;
CEM15; dJ494G10.1; MDS019"
/coded_by="NM_001349436.1:181..1302"
/note="isoform 2 is encoded by transcript variant 2"
/db_xref="GeneID:60489"
/db_xref="HGNC:HGNC:17357"
/db_xref="MIM:607113"
ORIGIN
1 myrdtfsynf ynrpilsrrn tvwlcyevkt kgpsrpplda kifrgqvyse lkyhpemrff
61 hwfskwrklh rdqeyevtwy iswspctkct rdmatflaed pkvtltifva rlyyfwdpdy
121 qealrslcqk rdgpratmki mnydefqhcw skfvysqrel fepwnnlpky yillhimlge
181 ilrhsmdppt ftfnfnnepw vrgrhetylc yevermhndt wvllnqrrgf lcnqaphkhg
241 flegrhaelc fldvipfwkl dldqdyrvtc ftswspcfsc aqemakfisk nkhvslcift
301 ariyddqgrc qeglrtlaea gakisimtys efkhcwdtfv dhqgcpfqpw dgldehsqdl
361 sgrlrailqn qen
NCBI Reference Sequence: NP_001336365.1
Preferred Names
- DNA dC->dU-editing enzyme
APOBEC-3G
-
Names
- APOBEC-related cytidine deaminase
- APOBEC-related protein 9
- DNA dC->dU editing enzyme
- apolipoprotein B editing enzyme catalytic polypeptide-like 3G
- apolipoprotein B mRNA editing enzyme cytidine deaminase
- apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G
- apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3G
- deoxycytidine deaminase
- phorbolin-like protein MDS019
Related articles in PubMed
-
-
-
-
-
APOBEC3G-Mediated
G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in
Antiviral Molecular Mechanisms. Okada A, et al. Front
Microbiol, 2016. PMID 28066353, Free
PMC Article
See
all (574) citations in PubMed
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