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måndag 28 maj 2018

APOBEC4 (Kr.1q25.39, C1Orf169 APOBEC, jolla ei ole antiretrovirusominaisuuksia.

APOBEC4  kuuluu AID/APOBEC perheeseen, joka on  polynukleotidi (deoxy)sytidiini deaminaasi entsyymeitä. mRNA.ta editoidessa en muutavat C-sytidiinin  U- uridiiniksi. AID   tarkoittta aktivaatiosta induoituvaa sytidiinideaminaasia. (APOBEC nimi taitaa viitata   ApoB mRNA:n Cytosiinin editoimiseen).
Virallisen nimen suomennosta : " apolipoproteiini  B  mRNA:ta oletettavasti  editoiva entsyymi, joka  muuttaa Cytosiinin Uridiiniksi;  katalyyttinen polypeptidin kaltainen proteiini  4 ".  Tunnetaan myös nimellä C1orf169. 
Muut perheen jäsenet osallistuvat  mRNA-editoimiseen, somaattiseen hypermutaatioon ja immunoglobuliinigeenien rekombinaatioon ja  retrovirusinfektion  luonnolliseen immuunipuolustukseen.  Tätä ABOBEC4 geeniä  esiintyy restriktiivisesti testiksessä.
LÄHDE: 
  • https://www.ncbi.nlm.nih.gov/gene/403314#gene-expression
  • Also known as C1orf169
  • Summary This gene encodes a member of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases, which convert cytidine to uridine. Other AID/APOBEC family members are involved in mRNA editing, somatic hypermutation and recombination of immunoglobulin genes, and innate immunity to retroviral infection. [provided by RefSeq, Jul 2008]
  • Expression Restricted expression toward testis (RPKM 6.1) See more

Preferred Names

putative C to U-editing enzyme APOBEC-4
Names
apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 4 (putative)

Peptide sequence and history

https://www.ncbi.nlm.nih.gov/protein/NP_982279.1

Related articles in PubMed

  1. APOBEC4 Enhances the Replication of HIV-1. Marino D, et al. PLoS One, 2016. PMID 27249646 (SUOMENNOSTA:) APOBEC4 kuuluu AID/ABOBEC sytidiinideaminaasi perheeseen. Tutkijat havaitsivat  korkean mRNA pitoisuuden testiksessä, mutta vain hyvin matalan pitoisuuden A4 mRNA:ta   293T:ssa   ym tutkimukseen kuuluneissa soluissa. Ektooppinen A4 (ABOBEC4)  ilmenemä johti proteiinin sytoplasmiseen sijaintiin. He halusivat tietää, olisiko tällä proteiinilla myös antivirusvaikutusta kuten  A3-alaperheellä ja he testasivat HIV-1 viruksen suhteen.  He huomasivat, että  A4 ei pystynyt estämään HIV-1 viruksen replikaatiota, vaan päinvastoin lisäsi HIV-1 virustuotantoa annoksesta riippuvalla tavalla ja näytti  vaikuttavan viruksen LTR- domeeniin. A4 ei myöskään osoittanut havaittavaa sytidiinideaminaasiaktiivisuutta koeputkessa ja reagoi vain  heikosti ssDNA:ta kohtaan.  A4 läsnäolo  lisäsi HIV-1 replikaatiota.  Samalla tavalla A4 pystyi  nopeuttamaan monien promoottorien transkriptiota oli sitten viruksesta tai ihmettäväissolusta kyse. Tutkijat olettavat, että ABOBEC4:n  luonnollinen tehtävä on moduloida  isäntäsolun promoottoreita tai endogeenisia LTR promoottoreita.
    • APOBEC4 (A4) is a member of the AID/APOBEC family of cytidine deaminases. In this study we found a high mRNA expression of A4 in human testis. In contrast, there were only low levels of A4 mRNA detectable in 293T, HeLa, Jurkat or A3.01 cells. Ectopic expression of A4 in HeLa cells resulted in mostly cytoplasmic localization of the protein. To test whether A4 has antiviral activity similar to that of proteins of the APOBEC3 (A3) subfamily, A4 was co-expressed in 293T cells with wild type HIV-1 and HIV-1 luciferase reporter viruses. We found that A4 did not inhibit the replication of HIV-1 but instead enhanced the production of HIV-1 in a dose-dependent manner and seemed to act on the viral LTR. A4 did not show detectable cytidine deamination activity in vitro and weakly interacted with single-stranded DNA. The presence of A4 in virus producer cells enhanced HIV-1 replication by transiently transfected A4 or stably expressed A4 in HIV-susceptible cells. APOBEC4 was capable of similarly enhancing transcription from a broad spectrum of promoters, regardless of whether they were viral or mammalian. We hypothesize that A4 may have a natural role in modulating host promoters or endogenous LTR promoters.
     Free PMC Article
  2. APOBEC deaminases-mutases with defensive roles for immunity. Prochnow C, et al. Sci China C Life Sci, 2009 Oct. PMID 19911124
  3. The DNA sequence and biological annotation of human chromosome 1. Gregory SG, et al. Nature, 2006 May 18. PMID 16710414 (Kommentti: APOBEC4 omaa geeninsä 1-kromosomissa poikkeuksena  muista  APOBEC-perheenjäsensitä. Kuitenkin APOBEC4 ja APOBEC1 joka on kromosomista  12 katsotaan klusteriksi ja toinen  klusteri on APOBEC2 kromosomista  6 ja APOBEC3 kromosomista 22)

    The reference sequence for each human chromosome provides the framework for understanding genome function, variation and evolution. Here we report the finished sequence and biological annotation of human chromosome 1. Chromosome 1 is gene-dense, with 3,141 genes and 991 pseudogenes, and many coding sequences overlap. Rearrangements and mutations of chromosome 1 are prevalent in cancer and many other diseases. Patterns of sequence variation reveal signals of recent selection in specific genes that may contribute to human fitness, and also in regions where no function is evident. Fine-scale recombination occurs in hotspots of varying intensity along the sequence, and is enriched near genes. These and other studies of human biology and disease encoded within chromosome 1 are made possible with the highly accurate annotated sequence, as part of the completed set of chromosome sequences that comprise the reference human genome.
See all (8) citations in PubMed
See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

  1. APOBEC4 is expressed primarily in testis which suggests the possibility that it is an editing enzyme for mRNAs involved in spermatogenesis 
  2.  
  3. Abstract ( SUOMENNOSTA. Varsinainen APOBEC4  geenin normaali funktio) . APOBEC4- proteiinin sinkkipitoinen  koordinoiva  motiivi osallistuu katalyysiin ja sekundääristruktuurit ovat  aktiivia polynukleotidi(deoxy)sytosiinideaminaaseja.  Fylogeneettisesti APOBEC4 on selvästi eri ryhmä:  APOBEC4 ja APOBEC1 muodostavat  oman klusterinsa, joka eroaa AID, APOBEC2 ja APOBEC3 alaryhmistä. Imettäväisissä APOBEC4 ilmenee primääristi testiksessä, mikä viittaa siihen amhdollisuuteen, että se on spermatogeneesiin osallistuva mRN:.ta editoiva entsyymi.  (Kommenttini:  Tavallaan HIV-1 virus voi ilmeisesti  kaapata tämän  virusreplikaation eduksi evaasiostrategioissaan).
    • Using iterative database searches, we identified a new subfamily of the AID/APOBEC family of RNA/DNA editing cytidine deaminases. The new subfamily, which is represented by readily identifiable orthologs in mammals, chicken, and frog, but not fishes, was designated APOBEC4. The zinc-coordinating motifs involved in catalysis and the secondary structure of the APOBEC4 deaminase domain are evolutionarily conserved, suggesting that APOBEC4 proteins are active polynucleotide (deoxy)cytidine deaminases. In reconstructed maximum likelihood phylogenetic trees, APOBEC4 forms a distinct clade with a high statistical support. APOBEC4 and APOBEC1 are joined in a moderately supported cluster clearly separated from AID, APOBEC2 and APOBEC3 subfamilies. In mammals, APOBEC4 is expressed primarily in testis which suggests the possibility that it is an editing enzyme for mRNAs involved in spermatogenesis.

Peptidesequence

GenPept
putative C->U-editing enzyme APOBEC-4 [Homo sapiens]
NCBI Reference Sequence: NP_982279.1
Identical Proteins FASTA Graphics
LOCUS       NP_982279                367 aa            linear   PRI 10-MAY-2018
DEFINITION  putative C-to U-editing enzyme APOBEC-4 [Homo sapiens].
ACCESSION   NP_982279
VERSION     NP_982279.1
DBSOURCE    REFSEQ: accession NM_203454.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Marino D, Perkovic M, Hain A, Jaguva Vasudevan AA, Hofmann H,
            Hanschmann KM, Muhlebach MD, Schumann GG, Konig R, Cichutek K,
            Haussinger D and Munk C.
  TITLE     APOBEC4 Enhances the Replication of HIV-1
  JOURNAL   PLoS ONE 11 (6), e0155422 (2016)
   PUBMED   27249646
  REMARK    GeneRIF: APOBEC4 was capable of similarly enhancing transcription
            from a broad spectrum of promoters, regardless of whether they were
            viral or mammalian
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Yang W, Tang H, Zhang Y, Tang X, Zhang J, Sun L, Yang J, Cui Y,
            Zhang L, Hirankarn N, Cheng H, Pan HF, Gao J, Lee TL, Sheng Y, Lau
            CS, Li Y, Chan TM, Yin X, Ying D, Lu Q, Leung AM, Zuo X, Chen X,
            Tong KL, Zhou F, Diao Q, Tse NK, Xie H, Mok CC, Hao F, Wong SN, Shi
            B, Lee KW, Hui Y, Ho MH, Liang B, Lee PP, Cui H, Guo Q, Chung BH,
            Pu X, Liu Q, Zhang X, Zhang C, Chong CY, Fang H, Wong RW, Sun Y,
            Mok MY, Li XP, Avihingsanon Y, Zhai Z, Rianthavorn P, Deekajorndej
            T, Suphapeetiporn K, Gao F, Shotelersuk V, Kang X, Ying SK, Zhang
            L, Wong WH, Zhu D, Fung SK, Zeng F, Lai WM, Wong CM, Ng IO,
            Garcia-Barcelo MM, Cherny SS, Shen N, Tam PK, Sham PC, Ye DQ, Yang
            S, Zhang X and Lau YL.
  TITLE     Meta-analysis followed by replication identifies loci in or near
            CDKN1B, TET3, CD80, DRAM1, and ARID5B as associated with systemic
            lupus erythematosus in Asians
  JOURNAL   Am. J. Hum. Genet. 92 (1), 41-51 (2013)
   PUBMED   23273568
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Prochnow C, Bransteitter R and Chen XS.
  TITLE     APOBEC deaminases-mutases with defensive roles for immunity
  JOURNAL   Sci. China, C, Life Sci. 52 (10), 893-902 (2009)
   PUBMED   19911124
  REMARK    GeneRIF: Studies indicate the APOBEC family consists of 11 members:
            APOBEC-1 (Apo1), APOBEC-2 (Apo2), activation induced cytidine
            deaminase (AID), APOBEC- 3A, -3B, -3C, -3DE, -3F, -3H (Apo3A-H) and
            APOBEC- 4 (Apo4).
            Review article
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Rogozin IB, Basu MK, Jordan IK, Pavlov YI and Koonin EV.
  TITLE     APOBEC4, a new member of the AID/APOBEC family of polynucleotide
            (deoxy)cytidine deaminases predicted by computational analysis
  JOURNAL   Cell Cycle 4 (9), 1281-1285 (2005)
   PUBMED   16082223
  REMARK    GeneRIF: APOBEC4 is expressed primarily in testis which suggests
            the possibility that it is an editing enzyme for mRNAs involved in
            spermatogenesis
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC021711.2 and AI961390.1.
            
            Summary: This gene encodes a member of the AID/APOBEC family of
            polynucleotide (deoxy)cytidine deaminases, which convert cytidine
            to uridine. Other AID/APOBEC family members are involved in mRNA
            editing, somatic hypermutation and recombination of immunoglobulin
            genes, and innate immunity to retroviral infection. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021711.2, AK098557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..367
                     /product="putative C->U-editing enzyme APOBEC-4"
                     /note="apolipoprotein B mRNA editing enzyme, catalytic
                     polypeptide-like 4 (putative)"
                     /calculated_mol_wt=41450
     Region          47..213
                     /region_name="APOBEC_N"
                     /note="APOBEC-like N-terminal domain; pfam08210"
                     /db_xref="CDD:285428"
     CDS             1..367
                     /gene="APOBEC4"
                     /gene_synonym="C1orf169"
                     /coded_by="NM_203454.2:273..1376"
                     /db_xref="CCDS:CCDS1358.1"
                     /db_xref="GeneID:403314"
                     /db_xref="HGNC:HGNC:32152"
                     /db_xref="MIM:609908"
ORIGIN      
        1 mepiyeeyla nhgtivkpyy wlsfsldcsn cpyhirtgee arvsltefcq ifgfpygttf
       61 pqtkhltfye lktssgslvq kghassctgn yihpesmlfe mngyldsaiy nndsirhiil
      121 ysnnspcnea nhcciskmyn flitypgitl siyfsqlyht emdfpasawn realrslasl
      181 wprvvlspis ggiwhsvlhs fisgvsgshv fqpiltgral adrhnayein aitgvkpyft
      241 dvllqtkrnp ntkaqeales yplnnafpgq ffqmpsgqlq pnlppdlrap vvfvlvplrd
      301 lppmhmgqnp nkprnivrhl nmpqmsfqet kdlgrlptgr sveiveiteq fasskeadek
      361 kkkkgkk
//
Päivitys. Suomennosta muutamiin artikkeleihin 9.6. 2018 ,08:36.
Päivitys 26.11. 2019 . Löytyi maininta CLR5- pohjaisesta  E3-ubikitiiniligasikompleksista, joka  voi säätää APOBEC  antiretroviraalista proteiinia ja miten retrovirus voi  suorittaa evaasion APOBEC- proteiinista.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4812663/

Näkökohtia rokotteista ja vaikutuksesta APOBEC järjestelmään

https://www.ncbi.nlm.nih.gov/pubmed/25953029
Immunol Cell Biol. 2015 Nov;93(10):868-76. doi: 10.1038/icb.2015.53. Epub 2015 May 8.

Modulating APOBEC expression enhances DNA vaccine immunogenicity.

Abstract

DNA vaccines have failed to induce satisfactory immune responses in humans. Several mechanisms of double-stranded DNA (dsDNA) sensing have been described, and modulate DNA vaccine immunogenicity at many levels. We hypothesized that the immunogenicity of DNA vaccines in humans is suppressed by APOBEC (apolipoprotein B (APOB) mRNA-editing, catalytic polypeptide)-mediated plasmid degradation. We showed that plasmid sensing via STING (stimulator of interferon (IFN) genes) and TBK-1 (TANK-binding kinase 1) leads to IFN-β induction, which results in APOBEC3A mRNA upregulation through a mechanism involving protein kinase C signaling. We also showed that murine APOBEC2 expression in HEK293T cells led to a 10-fold reduction in intracellular plasmid levels and plasmid-encoded mRNA, and a 2.6-fold reduction in GFP-expressing cells. A bicistronic DNA vaccine expressing an immunogen and an APOBEC2-specific shRNA efficiently silenced APOBEC2 both in vitro and in vivo, increasing the frequency of induced IFN-γ-secreting T cells. Our study brings new insights into the intracellular machinery involved in dsDNA sensing and how to modulate it to improve DNA vaccine immunogenicity in humans.
PMID:
25953029
DOI:
10.1038/icb.2015.53
[Indexed for MEDLINE]

APOBEC3H (Kr.22q13.1) A3H, ARCD, ARP-10,

APOBEC3H  ), A3H, ARCD, ARP9


https://www.ncbi.nlm.nih.gov/gene/164668
Also known as A3H; ARP10; ARP-10
Summary This gene encodes a member of the apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3 family of proteins. The encoded protein is a cytidine deaminase that has antiretroviral activity by generating lethal hypermutations in viral genomes. Polymorphisms and alternative splicing in this gene influence its antiretroviral activity and are associated with increased resistence to human immunodeficiency virus type 1 infection in certain populations. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Oct 2009]
Expression Broad expression in lymph node (RPKM 1.2), colon (RPKM 1.0) and 22 other tissues See more Orthologs mouse all

Preferred Names

DNA dC->dU-editing enzyme APOBEC-3H
Names
APOBEC-related protein 10
apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3H

Peptide sequence and history

https://www.ncbi.nlm.nih.gov/protein/NP_001159474.2
DNA dC->dU-editing enzyme APOBEC-3H isoform SV-182 [Homo sapiens]
NCBI Reference Sequence: NP_001159474.2
Identical Proteins FASTA Graphics
LOCUS       NP_001159474             182 aa            linear   PRI 02-APR-2018
DEFINITION  DNA dC->dU-editing enzyme APOBEC-3H isoform SV-182 [Homo sapiens].
ACCESSION   NP_001159474
VERSION     NP_001159474.2
DBSOURCE    REFSEQ: accession NM_001166002.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Zhang Z, Gu Q, de Manuel Montero M, Bravo IG, Marques-Bonet T,
            Haussinger D and Munk C.
  TITLE     Stably expressed APOBEC3H forms a barrier for cross-species
            transmission of simian immunodeficiency virus of chimpanzee to
            humans
  JOURNAL   PLoS Pathog. 13 (12), e1006746 (2017)
   PUBMED   29267382
  REMARK    GeneRIF: we speculate that stably expressed human A3H protects
            humans against the cross-species transmission of zoonotic infection
            of SIV of chimpanzee
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Nakano Y, Misawa N, Juarez-Fernandez G, Moriwaki M, Nakaoka S, Funo
            T, Yamada E, Soper A, Yoshikawa R, Ebrahimi D, Tachiki Y, Iwami S,
            Harris RS, Koyanagi Y and Sato K.
  TITLE     HIV-1 competition experiments in humanized mice show that APOBEC3H
            imposes selective pressure and promotes virus adaptation
  JOURNAL   PLoS Pathog. 13 (5), e1006348 (2017)
   PUBMED   28475648
  REMARK    GeneRIF: Stable variants of APOBEC3H impose selective pressure on
            HIV-1.
            Erratum:[PLoS Pathog. 2017 Sep 7;13(9):e1006606. PMID: 28880964]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Nakashima M, Tsuzuki S, Awazu H, Hamano A, Okada A, Ode H, Maejima
            M, Hachiya A, Yokomaku Y, Watanabe N, Akari H and Iwatani Y.
  TITLE     Mapping Region of Human Restriction Factor APOBEC3H Critical for
            Interaction with HIV-1 Vif
  JOURNAL   J. Mol. Biol. 429 (8), 1262-1276 (2017)
   PUBMED   28336404
  REMARK    GeneRIF: There are 10 APOBEC3H residues required for the HIV-1 Vif
            susceptibility and Vif binding.
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Gu J, Chen Q, Xiao X, Ito F, Wolfe A and Chen XS.
  TITLE     Biochemical Characterization of APOBEC3H Variants: Implications for
            Their HIV-1 Restriction Activity and mC Modification
  JOURNAL   J. Mol. Biol. 428 (23), 4626-4638 (2016)
   PUBMED   27534815
  REMARK    GeneRIF: The deamination activity of these APOBEC3H variants
            correlates well with their reported anti-HIV activity for the
            different haplotypes, suggesting that deaminase activity may be an
            important factor in determining their respective anti-HIV
            activities.
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Desimmie BA, Burdick RC, Izumi T, Doi H, Shao W, Alvord WG, Sato K,
            Koyanagi Y, Jones S, Wilson E, Hill S, Maldarelli F, Hu WS and
            Pathak VK.
  TITLE     APOBEC3 proteins can copackage and comutate HIV-1 genomes
  JOURNAL   Nucleic Acids Res. 44 (16), 7848-7865 (2016)
   PUBMED   27439715
  REMARK    GeneRIF: These results indicate that APOBEC3 proteins can be
            copackaged and can comutate the same genomes, and can cooperate to
            inhibit HIV replication.
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Harari A, Ooms M, Mulder LC and Simon V.
  TITLE     Polymorphisms and splice variants influence the antiretroviral
            activity of human APOBEC3H
  JOURNAL   J. Virol. 83 (1), 295-303 (2009)
   PUBMED   18945781
  REMARK    GeneRIF: the anti-HIV activity of APOBEC3H seems to be regulated by
            a combination of genomic variation and alternative splicing.
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Dang Y, Siew LM, Wang X, Han Y, Lampen R and Zheng YH.
  TITLE     Human cytidine deaminase APOBEC3H restricts HIV-1 replication
  JOURNAL   J. Biol. Chem. 283 (17), 11606-11614 (2008)
   PUBMED   18299330
  REMARK    GeneRIF: A3H inhibits HIV-1 replication potently by a cytidine
            deamination-independent mechanism
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Vartanian JP, Guetard D, Henry M and Wain-Hobson S.
  TITLE     Evidence for editing of human papillomavirus DNA by APOBEC3 in
            benign and precancerous lesions
  JOURNAL   Science 320 (5873), 230-233 (2008)
   PUBMED   18403710
  REMARK    GeneRIF: study provides evidence of editing of human papillomavirus
            1a and 16 DNA by APOBEC3 in plantar warts and precancerous cervix
            biopsies
REFERENCE   9  (residues 1 to 182)
  AUTHORS   OhAinle M, Kerns JA, Malik HS and Emerman M.
  TITLE     Adaptive evolution and antiviral activity of the conserved
            mammalian cytidine deaminase APOBEC3H
  JOURNAL   J. Virol. 80 (8), 3853-3862 (2006)
   PUBMED   16571802
REFERENCE   10 (residues 1 to 182)
  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 BU585251.1 and BC069023.1.
            On Jul 31, 2014 this sequence version replaced NP_001159474.1.
            
            Summary: This gene encodes a member of the apolipoprotein B
            mRNA-editing enzyme catalytic polypeptide 3 family of proteins. The
            encoded protein is a cytidine deaminase that has antiretroviral
            activity by generating lethal hypermutations in viral genomes.
            Polymorphisms and alternative splicing in this gene influence its
            antiretroviral activity and are associated with increased
            resistence to human immunodeficiency virus type 1 infection in
            certain populations. Alternative splicing results in multiple
            transcript variants.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (SV-182) lacks an alternate exon
            and uses an alternate splice site, resulting in an alternate 3'
            coding region and 3' UTR, compared to variant SV-200. The encoded
            isoform (SV-182) has a distinct C-terminus and is shorter than
            isoform SV-200.
            
            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##
            Transcript exon combination :: BC069023.1, SRR1163655.209075.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..182
                     /product="DNA dC->dU-editing enzyme APOBEC-3H isoform
                     SV-182"
                     /note="DNA dC->dU-editing enzyme APOBEC-3H; APOBEC-related
                     protein 10; apolipoprotein B mRNA editing enzyme,
                     catalytic polypeptide-like 3H"
                     /calculated_mol_wt=21400
     Region          27..179
                     /region_name="APOBEC_N"
          
           /db_xref="CDD:311913"
     CDS             1..182
                     /gene="APOBEC3H"
                     /gene_synonym="A3H; ARP-10; ARP10"
                     /coded_by="NM_001166002.2:128..676"
                     /note="isoform SV-182 is encoded by transcript variant
                     SV-182"
                     /db_xref="CCDS:CCDS54531.1"
                     /db_xref="GeneID:164668"
                     /db_xref="HGNC:HGNC:24100"
                     /db_xref="MIM:610976"
ORIGIN      
        1 malltaetfr lqfnnkrrlr rpyyprkall cyqltpqngs tptrgyfenk kkchaeicfi
       61 neiksmglde tqcyqvtcyl twspcsscaw elvdfikahd hlnlgifasr lyyhwckpqq
      121 kglrllcgsq vpvevmgfpe fadcwenfvd hekplsfnpy kmleeldkns raikrrleri
      181 ks
//

Related articles in PubMed

  1. APOBEC3H polymorphisms and susceptibility to HIV-1 infection in an Indian population. Naruse TK, et al. J Hum Genet, 2016 Mar. PMID 26559750
  2. The eQTL-missense polymorphisms of APOBEC3H are associated with lung cancer risk in a Han Chinese population. Zhu M, et al. Sci Rep, 2015 Oct 13. PMID 26459911, Free PMC Article
See all (72) citations in PubMed

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

  1. Importantly, APOBEC3H appears to use both deaminase-dependent and -independent mechanisms to target reverse transcription and restrict HIV-1 replication.

( Näissä ei nyt  ole vielä mitään suomennoslyhennelmiä) .

APOBEC3G (Kr.22.q13.1), A3G, ARCD, ARP9, CEM15

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

  1. Moderate of mouse mammary tumour virus to inhibition by human APOBEC3G. Konstantoulas CJ, et al. J Gen Virol, 2017 Sep. PMID 28809145
  2. 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