ABC3A_HUMAN
ID ABC3A_HUMAN Reviewed; 199 AA.
AC P31941; A0AVM1; Q12807; Q5JZ93; Q9UH18;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3A;
DE Short=A3A;
DE EC=3.5.4.38 {ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20615867, ECO:0000269|PubMed:21123384};
DE AltName: Full=Phorbolin-1;
GN Name=APOBEC3A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-27; 31-35; 53-60;
RP 112-123; 129-137 AND 192-198, AND FUNCTION.
RC TISSUE=Keratinocyte;
RX PubMed=10469298; DOI=10.1046/j.1523-1747.1999.00682.x;
RA Madsen P.P., Anant S., Rasmussen H.H., Gromov P., Vorum H., Dumanski J.P.,
RA Tommerup N., Collins J.E., Wright C.L., Dunham I., Macginnitie A.J.,
RA Davidson N.O., Celis J.E.;
RT "Psoriasis upregulated phorbolin-1 shares structural but not functional
RT similarity to the mRNA-editing protein apobec-1.";
RL J. Invest. Dermatol. 113:162-169(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 53-60; 112-121 AND 129-137.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [6]
RP GENE FAMILY ORGANIZATION, AND TISSUE SPECIFICITY.
RX PubMed=11863358; DOI=10.1006/geno.2002.6718;
RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J.,
RA Navaratnam N.;
RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on
RT chromosome 22.";
RL Genomics 79:285-296(2002).
RN [7]
RP REVIEW ON APOBEC FAMILIES.
RX PubMed=12683974; DOI=10.1016/s0168-9525(03)00054-4;
RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.;
RT "Messenger RNA editing in mammals: new members of the APOBEC family seeking
RT roles in the family business.";
RL Trends Genet. 19:207-216(2003).
RN [8]
RP FUNCTION IN HOST DEFENSE.
RX PubMed=12859895; DOI=10.1016/s0092-8674(03)00515-4;
RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B.,
RA Muenk C., Nymark-McMahon H., Landau N.R.;
RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
RL Cell 114:21-31(2003).
RN [9]
RP FUNCTION IN HOST DEFENSE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF HIS-70; GLU-72 AND CYS-106, AND TISSUE SPECIFICITY.
RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031;
RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., Landau N.R.,
RA Weitzman M.D.;
RT "APOBEC3A is a potent inhibitor of adeno-associated virus and
RT retrotransposons.";
RL Curr. Biol. 16:480-485(2006).
RN [10]
RP REVIEW.
RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
RA Chiu Y.L., Greene W.C.;
RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing
RT exogenous retroviruses and endogenous retroelements.";
RL Annu. Rev. Immunol. 26:317-353(2008).
RN [11]
RP FUNCTION IN AAV INHIBITION, AND SUBCELLULAR LOCATION.
RX PubMed=19461882; DOI=10.1371/journal.ppat.1000439;
RA Narvaiza I., Linfesty D.C., Greener B.N., Hakata Y., Pintel D.J., Logue E.,
RA Landau N.R., Weitzman M.D.;
RT "Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine
RT deaminase.";
RL PLoS Pathog. 5:E1000439-E1000439(2009).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND ALTERNATIVE SPLICING (ISOFORMS
RP 1 AND 2).
RX PubMed=20615867; DOI=10.1074/jbc.m110.102822;
RA Thielen B.K., McNevin J.P., McElrath M.J., Hunt B.V., Klein K.C.,
RA Lingappa J.R.;
RT "Innate immune signaling induces high levels of TC-specific deaminase
RT activity in primary monocyte-derived cells through expression of APOBEC3A
RT isoforms.";
RL J. Biol. Chem. 285:27753-27766(2010).
RN [13]
RP FUNCTION IN FOREIGN DNA CLEARANCE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=20062055; DOI=10.1038/nsmb.1744;
RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.;
RT "APOBEC3 proteins mediate the clearance of foreign DNA from human cells.";
RL Nat. Struct. Mol. Biol. 17:222-229(2010).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=20308164; DOI=10.1093/nar/gkq174;
RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L.,
RA Harris R.S.;
RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes
RT and tissues: implications for HIV-1 restriction.";
RL Nucleic Acids Res. 38:4274-4284(2010).
RN [15]
RP FUNCTION IN DNA DEMETHYLATION.
RX PubMed=21496894; DOI=10.1016/j.cell.2011.03.022;
RA Guo J.U., Su Y., Zhong C., Ming G.L., Song H.;
RT "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA
RT demethylation in the adult brain.";
RL Cell 145:423-434(2011).
RN [16]
RP FUNCTION.
RX PubMed=21460793; DOI=10.1038/embor.2011.46;
RA Landry S., Narvaiza I., Linfesty D.C., Weitzman M.D.;
RT "APOBEC3A can activate the DNA damage response and cause cell-cycle
RT arrest.";
RL EMBO Rep. 12:444-450(2011).
RN [17]
RP FUNCTION IN HOST DEFENSE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-28; HIS-29; LYS-30; ASN-57; LYS-60; ARG-69; GLU-72;
RP TRP-98; ARG-128; TYR-130; ASP-131; ASP-133 AND TYR-136.
RX PubMed=21123384; DOI=10.1128/jvi.01651-10;
RA Bulliard Y., Narvaiza I., Bertero A., Peddi S., Roehrig U.F., Ortiz M.,
RA Zoete V., Castro-Diaz N., Turelli P., Telenti A., Michielin O.,
RA Weitzman M.D., Trono D.;
RT "Structure-function analyses point to a polynucleotide-accommodating groove
RT essential for APOBEC3A restriction activities.";
RL J. Virol. 85:1765-1776(2011).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=21835787; DOI=10.1128/jvi.05238-11;
RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L.,
RA Brown W.L., Harris R.S.;
RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a
RT conserved capacity to restrict Vif-deficient HIV-1.";
RL J. Virol. 85:11220-11234(2011).
RN [19]
RP FUNCTION.
RX PubMed=21368204; DOI=10.1073/pnas.1009687108;
RA Suspene R., Aynaud M.M., Guetard D., Henry M., Eckhoff G., Marchio A.,
RA Pineau P., Dejean A., Vartanian J.P., Wain-Hobson S.;
RT "Somatic hypermutation of human mitochondrial and nuclear DNA by APOBEC3
RT cytidine deaminases, a pathway for DNA catabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4858-4863(2011).
RN [20]
RP REVIEW.
RA Love R.;
RT "Cytosine deaminases APOBEC3A, APOBEC3C, and APOBEC3H: Current
RT understanding of their functional roles.";
RL Student Perspec. Contemp. Virol. 0:0-0(2011).
RN [21]
RP REVIEW.
RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275;
RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.;
RT "Retroelements versus APOBEC3 family members: No great escape from the
RT magnificent seven.";
RL Front. Microbiol. 3:275-275(2012).
RN [22]
RP FUNCTION.
RX PubMed=22896697; DOI=10.1074/jbc.m112.385161;
RA Carpenter M.A., Li M., Rathore A., Lackey L., Law E.K., Land A.M.,
RA Leonard B., Shandilya S.M., Bohn M.F., Schiffer C.A., Brown W.L.,
RA Harris R.S.;
RT "Methylcytosine and normal cytosine deamination by the foreign DNA
RT restriction enzyme APOBEC3A.";
RL J. Biol. Chem. 287:34801-34808(2012).
RN [23]
RP INTERACTION WITH TRIB3, AND SUBCELLULAR LOCATION.
RX PubMed=22977230; DOI=10.1074/jbc.m112.372722;
RA Aynaud M.M., Suspene R., Vidalain P.O., Mussil B., Guetard D., Tangy F.,
RA Wain-Hobson S., Vartanian J.P.;
RT "Human Tribbles 3 protects nuclear DNA from cytidine deamination by
RT APOBEC3A.";
RL J. Biol. Chem. 287:39182-39192(2012).
RN [24]
RP FUNCTION IN HTLV-1 RESTRICTION.
RX PubMed=22457529; DOI=10.1128/jvi.06570-11;
RA Ooms M., Krikoni A., Kress A.K., Simon V., Muenk C.;
RT "APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic
RT virus type 1.";
RL J. Virol. 86:6097-6108(2012).
RN [25]
RP INTERACTION WITH AGO2.
RX PubMed=22915799; DOI=10.1128/jvi.00595-12;
RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by P
RT bodies.";
RL J. Virol. 86:11712-11724(2012).
RN [26]
RP REVIEW.
RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004;
RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.;
RT "Functions and regulation of the APOBEC family of proteins.";
RL Semin. Cell Dev. Biol. 23:258-268(2012).
CC -!- FUNCTION: DNA deaminase (cytidine deaminase) with restriction activity
CC against viruses, foreign DNA and mobility of retrotransposons. Exhibits
CC antiviral activity against adeno-associated virus (AAV) and human T-
CC cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR
CC and non-LTR retrotransposons. Selectively targets single-stranded DNA
CC and can deaminate both methylcytosine and cytosine in foreign DNA. Can
CC induce somatic hypermutation in the nuclear and mitochondrial DNA. May
CC also play a role in the epigenetic regulation of gene expression
CC through the process of active DNA demethylation.
CC {ECO:0000269|PubMed:10469298, ECO:0000269|PubMed:12859895,
CC ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:19461882,
CC ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:20615867,
CC ECO:0000269|PubMed:21123384, ECO:0000269|PubMed:21368204,
CC ECO:0000269|PubMed:21460793, ECO:0000269|PubMed:21496894,
CC ECO:0000269|PubMed:22457529, ECO:0000269|PubMed:22896697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-
CC deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948,
CC Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:133902; EC=3.5.4.38;
CC Evidence={ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055,
CC ECO:0000269|PubMed:20615867, ECO:0000269|PubMed:21123384};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with AGO2. Interacts with TRIB3 (via N-terminus).
CC {ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:22977230}.
CC -!- INTERACTION:
CC P31941; Q16775-2: HAGH; NbExp=3; IntAct=EBI-13050366, EBI-17557678;
CC P31941; O95630: STAMBP; NbExp=3; IntAct=EBI-13050366, EBI-396676;
CC P31941; Q784Z8: C; Xeno; NbExp=4; IntAct=EBI-13050366, EBI-11666471;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Phorbolin-1;
CC IsoId=P31941-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31941-2; Sequence=VSP_041723;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral leukocytes with higher
CC expression in CD14-positive phagocytic cells. Highly expressed in
CC keratinocytes and in periphery blood monocytes. Also detected in non-
CC lymphoid tissues including lung and adipose tissues. Found at high
CC levels in colorectal adenocarcinoma, Burkitt's lymphoma and chronic
CC myelogenous leukemia. {ECO:0000269|PubMed:11863358,
CC ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055,
CC ECO:0000269|PubMed:20308164}.
CC -!- INDUCTION: Up-regulated by interferon and CpG single-stranded DNA (at
CC protein level). {ECO:0000269|PubMed:20062055,
CC ECO:0000269|PubMed:20615867}.
CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes found in
CC a cluster, thought to result from gene duplication, on chromosome 22.
CC -!- MISCELLANEOUS: [Isoform 1]: Enzymatically active.
CC -!- MISCELLANEOUS: [Isoform 2]: Enzymatically active. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; U03891; AAA03706.2; -; mRNA.
DR EMBL; CR456393; CAG30279.1; -; mRNA.
DR EMBL; AL022318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126416; AAI26417.1; -; mRNA.
DR CCDS; CCDS13981.1; -. [P31941-1]
DR PIR; G01233; G01233.
DR RefSeq; NP_001180218.1; NM_001193289.1. [P31941-1]
DR RefSeq; NP_663745.1; NM_145699.3. [P31941-1]
DR PDB; 2M65; NMR; -; A=1-199.
DR PDB; 4XXO; X-ray; 2.84 A; A/B=1-199.
DR PDB; 5KEG; X-ray; 2.20 A; A=1-199.
DR PDB; 5SWW; X-ray; 3.15 A; A/B/C/D=1-196.
DR PDB; 7D3V; NMR; -; A/B=1-199.
DR PDB; 7D3W; NMR; -; A=1-199.
DR PDB; 7D3X; NMR; -; A=1-199.
DR PDBsum; 2M65; -.
DR PDBsum; 4XXO; -.
DR PDBsum; 5KEG; -.
DR PDBsum; 5SWW; -.
DR PDBsum; 7D3V; -.
DR PDBsum; 7D3W; -.
DR PDBsum; 7D3X; -.
DR AlphaFoldDB; P31941; -.
DR BMRB; P31941; -.
DR SMR; P31941; -.
DR BioGRID; 128318; 14.
DR DIP; DIP-61365N; -.
DR IntAct; P31941; 5.
DR STRING; 9606.ENSP00000384359; -.
DR BindingDB; P31941; -.
DR ChEMBL; CHEMBL1741179; -.
DR iPTMnet; P31941; -.
DR PhosphoSitePlus; P31941; -.
DR BioMuta; APOBEC3A; -.
DR DMDM; 12644206; -.
DR jPOST; P31941; -.
DR MassIVE; P31941; -.
DR MaxQB; P31941; -.
DR PaxDb; P31941; -.
DR PeptideAtlas; P31941; -.
DR PRIDE; P31941; -.
DR ProteomicsDB; 54806; -. [P31941-1]
DR ProteomicsDB; 54807; -. [P31941-2]
DR ABCD; P31941; 1 sequenced antibody.
DR Antibodypedia; 26513; 251 antibodies from 33 providers.
DR DNASU; 200315; -.
DR Ensembl; ENST00000249116.7; ENSP00000249116.2; ENSG00000128383.13. [P31941-1]
DR Ensembl; ENST00000402255.5; ENSP00000384359.1; ENSG00000128383.13. [P31941-1]
DR Ensembl; ENST00000570508.2; ENSP00000461288.1; ENSG00000262156.4. [P31941-1]
DR Ensembl; ENST00000618553.1; ENSP00000481904.1; ENSG00000128383.13. [P31941-1]
DR Ensembl; ENST00000623492.3; ENSP00000485234.1; ENSG00000262156.4. [P31941-1]
DR GeneID; 100913187; -.
DR GeneID; 200315; -.
DR KEGG; hsa:100913187; -.
DR KEGG; hsa:200315; -.
DR MANE-Select; ENST00000249116.7; ENSP00000249116.2; NM_145699.4; NP_663745.1.
DR UCSC; uc003awn.2; human. [P31941-1]
DR CTD; 100913187; -.
DR CTD; 200315; -.
DR DisGeNET; 100913187; -.
DR DisGeNET; 200315; -.
DR GeneCards; APOBEC3A; -.
DR HGNC; HGNC:17343; APOBEC3A.
DR HPA; ENSG00000128383; Group enriched (bone marrow, lymphoid tissue, urinary bladder).
DR MIM; 607109; gene.
DR neXtProt; NX_P31941; -.
DR OpenTargets; ENSG00000128383; -.
DR PharmGKB; PA24891; -.
DR VEuPathDB; HostDB:ENSG00000128383; -.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00940000164701; -.
DR HOGENOM; CLU_080056_2_0_1; -.
DR OMA; CYEVELP; -.
DR PhylomeDB; P31941; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.38; 2681.
DR PathwayCommons; P31941; -.
DR Reactome; R-HSA-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-HSA-75094; Formation of the Editosome.
DR SignaLink; P31941; -.
DR SIGNOR; P31941; -.
DR BioGRID-ORCS; 100913187; 2 hits in 77 CRISPR screens.
DR BioGRID-ORCS; 200315; 9 hits in 1063 CRISPR screens.
DR ChiTaRS; APOBEC3A; human.
DR Pharos; P31941; Tchem.
DR PRO; PR:P31941; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P31941; protein.
DR Bgee; ENSG00000128383; Expressed in monocyte and 135 other tissues.
DR ExpressionAtlas; P31941; baseline and differential.
DR Genevisible; P31941; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0004126; F:cytidine deaminase activity; IDA:UniProtKB.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0044355; P:clearance of foreign intracellular DNA; IDA:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB.
DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IBA:GO_Central.
DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Antiviral defense; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..199
FT /note="DNA dC->dU-editing enzyme APOBEC-3A"
FT /id="PRO_0000171752"
FT DOMAIN 27..143
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 72
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041723"
FT VARIANT 19
FT /note="T -> A (in dbSNP:rs17000556)"
FT /id="VAR_048721"
FT MUTAGEN 28
FT /note="R->E: No effect on deaminase activity despite an
FT altered restriction activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 29
FT /note="H->A: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 30
FT /note="K->F: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 57
FT /note="N->A: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 60
FT /note="K->A: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 69
FT /note="R->A: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 70
FT /note="H->R: Altered deaminase activity."
FT /evidence="ECO:0000269|PubMed:16527742"
FT MUTAGEN 72
FT /note="E->Q: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:16527742,
FT ECO:0000269|PubMed:21123384"
FT MUTAGEN 98
FT /note="W->L: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 106
FT /note="C->S: Altered deaminase activity."
FT /evidence="ECO:0000269|PubMed:16527742"
FT MUTAGEN 128
FT /note="R->A: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 130
FT /note="Y->A: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 131
FT /note="D->N: No effect on deaminase activity despite an
FT altered restriction activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 133
FT /note="D->N: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT MUTAGEN 136
FT /note="Y->A: Altered deaminase activity and restriction
FT activity towards genetic invaders."
FT /evidence="ECO:0000269|PubMed:21123384"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:7D3W"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:5KEG"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4XXO"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2M65"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:5KEG"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5KEG"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5KEG"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5KEG"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:5KEG"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:5KEG"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:5KEG"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2M65"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:5KEG"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5KEG"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:5KEG"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5KEG"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:5KEG"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:5KEG"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:7D3V"
SQ SEQUENCE 199 AA; 23012 MW; 42E99E0D7DF7AA14 CRC64;
MEASPASGPR HLMDPHIFTS NFNNGIGRHK TYLCYEVERL DNGTSVKMDQ HRGFLHNQAK
NLLCGFYGRH AELRFLDLVP SLQLDPAQIY RVTWFISWSP CFSWGCAGEV RAFLQENTHV
RLRIFAARIY DYDPLYKEAL QMLRDAGAQV SIMTYDEFKH CWDTFVDHQG CPFQPWDGLD
EHSQALSGRL RAILQNQGN
