APOBEC3C, A3C, ARP5
Samassa Kr.22
klusterissa seitsemän samantapaisen geenin kanssa
geeniduplikaatiolla muodostuneen geenin tai pseudogeenin kanssa, ne
koodaavat rakenteellisesti ja toiminnallisesti samantapaisia
sydidiini C- deaminaaseja kuin APOBEC1 ja tuottavat urasiilia U. On
ajateltu näiden proteiinien muovaaman entsymaattisesti RNA:ta ja
osallistuvan kasvuun tai solusyklin kontrolliin.Tätä geeniä
esiintyy yleisesti lymfasolmukkeissa, testiksessä ja 24 muusas
kudoksessa.Tämän geenin deleetio ei näytä olevan hyödyksi ainakaan rintasyövässä. retrovirusvastaista merkitsytä lienee tälläkin Apobec3C- lajilla, vaikka ei niin selvästi kuin jollain muulla tässä klusterissa. Sisältää kuitenkin merkitseviä motiiveja kuten f-y-v-e-
Mitään silmiinpistävän suurta muuta erityismerkitystä en löydä tästä geenist, mikä ei olisi muiten APOBEC3- proteiinien kattamatonta. Molekyyli on 190 aminohappoa sisältävä.
Mitään silmiinpistävän suurta muuta erityismerkitystä en löydä tästä geenist, mikä ei olisi muiten APOBEC3- proteiinien kattamatonta. Molekyyli on 190 aminohappoa sisältävä.
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https://www.ncbi.nlm.nih.gov/gene/27350 Also known as A3C; PBI; ARP5; ARDC2; ARDC4; APOBEC1L; bK150C2.3 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. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. [provided by RefSeq, Jul 2008] Expression Ubiquitous expression in lymph node (RPKM 33.1), testis (RPKM 26.8) and 24 other tissues See more Orthologs all
Preferred Names
- DNA dC->dU-editing enzyme APOBEC-3C
- Names
- apolipoprotein B editing enzyme catalytic polypeptide-like 3C
- apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C
- phorbolin I
- probable DNA dC->dU-editing enzyme APOBEC-3C
Conserved Domains (3) summary
- cd01283
Location:8 → 158 - cytidine_deaminase; Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on ...
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pfam05240
Location:129 → 174 - APOBEC_C; APOBEC-like C-terminal domain
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pfam08210
Location:17 → 187 - APOBEC_N; APOBEC-like N-terminal domain
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PEPTIDE sequence and history
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DNA C-to U -editing enzyme APOBEC-3C [Homo sapiens]NCBI Reference Sequence: NP_055323.2
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LOCUS NP_055323 190 aa linear PRI 01-APR-2018 DEFINITION DNA dC->dU-editing enzyme APOBEC-3C [Homo sapiens]. ACCESSION NP_055323 VERSION NP_055323.2 DBSOURCE REFSEQ: accession NM_014508.2 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 190) AUTHORS Chen Z, Eggerman TL, Bocharov AV, Baranova IN, Vishnyakova TG, Kurlander R and Patterson AP. TITLE Heat shock proteins stimulate APOBEC-3-mediated cytidine deamination in the hepatitis B virus JOURNAL J. Biol. Chem. 292 (32), 13459-13479 (2017) PUBMED 28637869 REMARK GeneRIF: Data suggest that heat shock proteins, in particular Hsp90, stimulate APOBEC3-mediated DNA deamination activity toward hepatitis B viral DNA, suggesting a potential physiological role in mutagenesis/carcinogenesis and viral innate immunity; Hsp90 stimulates deamination activity of APOBEC3G, APOBEC3B, and APOBEC3C during co-expression in human liver HepG2 cells. REFERENCE 2 (residues 1 to 190) AUTHORS Jaguva Vasudevan AA, Hofmann H, Willbold D, Haussinger D, Koenig BW and Munk C. TITLE Enhancing the Catalytic Deamination Activity of APOBEC3C Is Insufficient to Inhibit Vif-Deficient HIV-1 JOURNAL J. Mol. Biol. 429 (8), 1171-1191 (2017) PUBMED 28315663 REMARK GeneRIF: Antiviral functions of APOBEC3C against HIV-1 and APOBEC3C binding capacity REFERENCE 3 (residues 1 to 190) AUTHORS Middlebrooks CD, Banday AR, Matsuda K, Udquim KI, Onabajo OO, Paquin A, Figueroa JD, Zhu B, Koutros S, Kubo M, Shuin T, Freedman ND, Kogevinas M, Malats N, Chanock SJ, Garcia-Closas M, Silverman DT, Rothman N and Prokunina-Olsson L. TITLE Association of germline variants in the APOBEC3 region with cancer risk and enrichment with APOBEC-signature mutations in tumors JOURNAL Nat. Genet. 48 (11), 1330-1338 (2016) PUBMED 27643540 REFERENCE 4 (residues 1 to 190) AUTHORS Wittkopp CJ, Adolph MB, Wu LI, Chelico L and Emerman M. TITLE A Single Nucleotide Polymorphism in Human APOBEC3C Enhances Restriction of Lentiviruses JOURNAL PLoS Pathog. 12 (10), e1005865 (2016) PUBMED 27732658 REMARK GeneRIF: our results suggest that APOBEC3C is in fact involved in protecting hosts from lentiviruses. Publication Status: Online-Only REFERENCE 5 (residues 1 to 190) AUTHORS Zhang Y, Delahanty R, Guo X, Zheng W and Long J. TITLE Integrative genomic analysis reveals functional diversification of APOBEC gene family in breast cancer JOURNAL Hum. Genomics 9, 34 (2015) PUBMED 26682542 REMARK GeneRIF: These results suggest that functional potential of APOBEC3B and APOBEC3C involved in cancer mutagenesis is associated with estrogen receptor status. Publication Status: Online-Only REFERENCE 6 (residues 1 to 190) AUTHORS Mariani R, Chen D, Schrofelbauer B, Navarro F, Konig R, Bollman B, Munk C, Nymark-McMahon H and Landau NR. TITLE Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif JOURNAL Cell 114 (1), 21-31 (2003) PUBMED 12859895 REFERENCE 7 (residues 1 to 190) 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] REFERENCE 8 (residues 1 to 190) AUTHORS Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J and Navaratnam N. TITLE An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22 JOURNAL Genomics 79 (3), 285-296 (2002) PUBMED 11863358 REFERENCE 9 (residues 1 to 190) AUTHORS Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP et al. TITLE The DNA sequence of human chromosome 22 JOURNAL Nature 402 (6761), 489-495 (1999) PUBMED 10591208 REMARK Erratum:[Nature 2000 Apr 20;404(6780):904] REFERENCE 10 (residues 1 to 190) AUTHORS Madsen P, Anant S, Rasmussen HH, Gromov P, Vorum H, Dumanski JP, Tommerup N, Collins JE, Wright CL, Dunham I, MacGinnitie AJ, Davidson NO and Celis JE. TITLE Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1 JOURNAL J. Invest. Dermatol. 113 (2), 162-169 (1999) PUBMED 10469298 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from BC011739.2. On Sep 16, 2002 this sequence version replaced NP_055323.1. 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. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. [provided by RefSeq, Jul 2008]. 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 :: BC011739.2, SRR1163655.295268.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..190 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="22" /map="22q13.1" Protein 1..190 /product="DNA dC->dU-editing enzyme APOBEC-3C" /note="probable DNA dC->dU-editing enzyme APOBEC-3C; phorbolin I; apolipoprotein B editing enzyme catalytic polypeptide-like 3C; apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C" /calculated_mol_wt=22695 Region 8..158 /region_name="cytidine_deaminase" /note="Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on...; cd01283" /db_xref="CDD:238610" Region 17..187 /region_name="APOBEC_N" /note="APOBEC-like N-terminal domain; pfam08210" /db_xref="CDD:285428" Site order(32,34,55,57,66..68,97,100) /site_type="active" /db_xref="CDD:238610" Site order(66..68,96..97,100) /site_type="active" /note="catalytic motif [active]" /db_xref="CDD:238610" Site order(66,68,97,100) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:238610" Region 129..174 /region_name="APOBEC_C" /note="APOBEC-like C-terminal domain; pfam05240" /db_xref="CDD:283020" CDS 1..190 /gene="APOBEC3C" /gene_synonym="A3C; APOBEC1L; ARDC2; ARDC4; ARP5; bK150C2.3; PBI" /coded_by="NM_014508.2:104..676" /db_xref="CCDS:CCDS13983.1" /db_xref="GeneID:27350" /db_xref="HGNC:HGNC:17353" /db_xref="MIM:607750" ORIGIN 1 mnpqirnpmk amypgtfyfq fknlweandr netwlcftve gikrrsvvsw ktgvfrnqvd 61 sethchaerc flswfcddil spntkyqvtw ytswspcpdc agevaeflar hsnvnltift 121 arlyyfqypc yqeglrslsq egvaveimdy edfkycwenf vyndnepfkp wkglktnfrl 181 lkrrlreslq //
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