ABC3C_HUMAN
ID ABC3C_HUMAN Reviewed; 190 AA.
AC Q9NRW3; B2R884; Q5JZ92; Q7Z2N7; Q96F12;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3C;
DE Short=A3C;
DE EC=3.5.4.38;
DE AltName: Full=APOBEC1-like;
DE AltName: Full=Phorbolin I;
GN Name=APOBEC3C; Synonyms=APOBEC1L, PBI;
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 [LARGE SCALE MRNA].
RC TISSUE=Hematopoietic stem cell;
RA Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., Tu Y.,
RA Gu W., Fu G., Huang C.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
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 [8]
RP FUNCTION IN HIV-1 INFECTIVITY.
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 SIV RESTRICTION.
RX PubMed=15466872; DOI=10.1074/jbc.m408802200;
RA Yu Q., Chen D., Koenig R., Mariani R., Unutmaz D., Landau N.R.;
RT "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency
RT virus replication.";
RL J. Biol. Chem. 279:53379-53386(2004).
RN [10]
RP FUNCTION IN RETROTRANSPOSITION.
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 [11]
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 [12]
RP REVIEW ON FUNCTION IN HBV RESTRICTION.
RX PubMed=18448976; DOI=10.1097/qco.0b013e3282fe1bb2;
RA Bonvin M., Greeve J.;
RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases
RT as effectors in innate immunity against the hepatitis B virus.";
RL Curr. Opin. Infect. Dis. 21:298-303(2008).
RN [13]
RP INTERACTION WITH HUMAN FOAMY VIRUS PROTEIN BET (MICROBIAL INFECTION), AND
RP BET-INTERACTING REGION (MICROBIAL INFECTION).
RX PubMed=19074429; DOI=10.1074/jbc.m808853200;
RA Perkovic M., Schmidt S., Marino D., Russell R.A., Stauch B., Hofmann H.,
RA Kopietz F., Kloke B.-P., Zielonka J., Stroever H., Hermle J., Lindemann D.,
RA Pathak V.K., Schneider G., Loechelt M., Cichutek K., Muenk C.;
RT "Species-specific inhibition of APOBEC3C by the prototype foamy virus
RT protein bet.";
RL J. Biol. Chem. 284:5819-5826(2009).
RN [14]
RP FUNCTION IN RETROTRANSPOSITION.
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 [15]
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 [16]
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 [17]
RP FUNCTION IN EBV AND HHV-1 INHIBITION.
RX PubMed=21632763; DOI=10.1128/jvi.00290-11;
RA Suspene R., Aynaud M.M., Koch S., Pasdeloup D., Labetoulle M., Gaertner B.,
RA Vartanian J.P., Meyerhans A., Wain-Hobson S.;
RT "Genetic editing of herpes simplex virus 1 and Epstein-Barr herpesvirus
RT genomes by human APOBEC3 cytidine deaminases in culture and in vivo.";
RL J. Virol. 85:7594-7602(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 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 [20]
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 [21]
RP INTERACTION WITH TRIB3, SUBCELLULAR LOCATION, AND SUBUNIT.
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 [22]
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 [23]
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).
RN [24] {ECO:0007744|PDB:3VOW}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH ZINC, SUBUNIT,
RP INTERACTION WITH HIV-1 VIF (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP LEU-72; PHE-75; CYS-76; ILE-79; LEU-80; SER-81; TYR-86; GLU-106; PHE-107;
RP ALA-109; HIS-111; PRO-129 AND GLU-141.
RX PubMed=23001005; DOI=10.1038/nsmb.2378;
RA Kitamura S., Ode H., Nakashima M., Imahashi M., Naganawa Y., Kurosawa T.,
RA Yokomaku Y., Yamane T., Watanabe N., Suzuki A., Sugiura W., Iwatani Y.;
RT "The APOBEC3C crystal structure and the interface for HIV-1 Vif binding.";
RL Nat. Struct. Mol. Biol. 19:1005-1010(2012).
RN [25] {ECO:0007744|PDB:3VM8}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH ZINC.
RA Kitamura S., Ode H., Nakashima M., Imahashi M., Naganawa Y., Ibe S.,
RA Yokomaku Y., Watanabe N., Suzuki A., Sugiura W., Iwatani Y.;
RT "Crystal structure of the human APOBEC3C having HIV-1 Vif-binding
RT interface.";
RL Submitted (DEC-2011) to the PDB data bank.
CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor
CC of retrovirus replication and retrotransposon mobility via deaminase-
CC dependent and -independent mechanisms. After the penetration of
CC retroviral nucleocapsids into target cells of infection and the
CC initiation of reverse transcription, it can induce the conversion of
CC cytosine to uracil in the minus-sense single-strand viral DNA, leading
CC to G-to-A hypermutations in the subsequent plus-strand viral DNA. The
CC resultant detrimental levels of mutations in the proviral genome, along
CC with a deamination-independent mechanism that works prior to the
CC proviral integration, together exert efficient antiretroviral effects
CC in infected target cells. Selectively targets single-stranded DNA and
CC does not deaminate double-stranded DNA or single- or double-stranded
CC RNA. Exhibits antiviral activity against simian immunodeficiency virus
CC (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and
CC Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-
CC LTR retrotransposons. May also play a role in the epigenetic regulation
CC of gene expression through the process of active DNA demethylation.
CC {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:15466872,
CC ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055,
CC ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21632763}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: (Microbial infection) Antiviral activity is
CC neutralized by the HIV-1 virion infectivity factor (Vif), that prevents
CC its incorporation into progeny HIV-1 virions by both inhibiting its
CC translation and/or by inducing its ubiquitination and subsequent
CC degradation by the 26S proteasome. {ECO:0000250|UniProtKB:Q96AK3}.
CC -!- SUBUNIT: Homodimer (PubMed:22977230, PubMed:23001005). Interacts with
CC TRIB3 (PubMed:22977230). Interacts with AGO2 (PubMed:22915799).
CC {ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:22977230,
CC ECO:0000269|PubMed:23001005}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human foamy virus protein
CC Bet; this interaction does not induce APOBEC3C degradation but prevents
CC its dimerization and incorporation into the virion by binding of Bet
CC close to or within the APOBEC3C dimerization site.
CC {ECO:0000269|PubMed:19074429}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vif.
CC {ECO:0000269|PubMed:23001005}.
CC -!- INTERACTION:
CC Q9NRW3; Q9Y3Y2-3: CHTOP; NbExp=3; IntAct=EBI-1044593, EBI-11984237;
CC Q9NRW3; Q03014: HHEX; NbExp=3; IntAct=EBI-1044593, EBI-747421;
CC Q9NRW3; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-1044593, EBI-7060731;
CC Q9NRW3; P79522: PRR3; NbExp=3; IntAct=EBI-1044593, EBI-2803328;
CC Q9NRW3; P38159: RBMX; NbExp=6; IntAct=EBI-1044593, EBI-743526;
CC Q9NRW3; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-1044593, EBI-8638511;
CC Q9NRW3; Q15415: RBMY1J; NbExp=6; IntAct=EBI-1044593, EBI-8642021;
CC Q9NRW3; Q96RU7: TRIB3; NbExp=5; IntAct=EBI-1044593, EBI-492476;
CC Q9NRW3; P15622-3: ZNF250; NbExp=3; IntAct=EBI-1044593, EBI-10177272;
CC Q9NRW3; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-1044593, EBI-347633;
CC Q9NRW3; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-1044593, EBI-12006434;
CC Q9NRW3; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-1044593, EBI-745520;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21835787,
CC ECO:0000269|PubMed:22977230}. Cytoplasm {ECO:0000269|PubMed:21835787,
CC ECO:0000269|PubMed:22977230}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, testes, peripherical blood
CC lymphocytes, heart, thymus, prostate and ovary.
CC {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:20308164}.
CC -!- INDUCTION: Up-regulated by IFN-alpha.
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 -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86650.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF165520; AAF86650.1; ALT_FRAME; mRNA.
DR EMBL; CR456394; CAG30280.1; -; mRNA.
DR EMBL; AK313272; BAG36081.1; -; mRNA.
DR EMBL; AL022318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60284.1; -; Genomic_DNA.
DR EMBL; BC011739; AAH11739.1; -; mRNA.
DR EMBL; BC021080; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13983.1; -.
DR RefSeq; NP_055323.2; NM_014508.2.
DR PDB; 3VM8; X-ray; 3.00 A; A/B=1-190.
DR PDB; 3VOW; X-ray; 2.15 A; A/B=1-190.
DR PDBsum; 3VM8; -.
DR PDBsum; 3VOW; -.
DR AlphaFoldDB; Q9NRW3; -.
DR SMR; Q9NRW3; -.
DR BioGRID; 118162; 183.
DR DIP; DIP-48919N; -.
DR IntAct; Q9NRW3; 26.
DR STRING; 9606.ENSP00000355340; -.
DR GlyGen; Q9NRW3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NRW3; -.
DR PhosphoSitePlus; Q9NRW3; -.
DR BioMuta; APOBEC3C; -.
DR DMDM; 48474983; -.
DR EPD; Q9NRW3; -.
DR jPOST; Q9NRW3; -.
DR MassIVE; Q9NRW3; -.
DR MaxQB; Q9NRW3; -.
DR PaxDb; Q9NRW3; -.
DR PeptideAtlas; Q9NRW3; -.
DR PRIDE; Q9NRW3; -.
DR ProteomicsDB; 82428; -.
DR Antibodypedia; 35026; 262 antibodies from 33 providers.
DR DNASU; 27350; -.
DR Ensembl; ENST00000361441.5; ENSP00000355340.3; ENSG00000244509.4.
DR GeneID; 27350; -.
DR KEGG; hsa:27350; -.
DR MANE-Select; ENST00000361441.5; ENSP00000355340.3; NM_014508.3; NP_055323.2.
DR UCSC; uc003awr.4; human.
DR CTD; 27350; -.
DR DisGeNET; 27350; -.
DR GeneCards; APOBEC3C; -.
DR HGNC; HGNC:17353; APOBEC3C.
DR HPA; ENSG00000244509; Low tissue specificity.
DR MIM; 607750; gene.
DR neXtProt; NX_Q9NRW3; -.
DR OpenTargets; ENSG00000244509; -.
DR PharmGKB; PA24893; -.
DR VEuPathDB; HostDB:ENSG00000244509; -.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00940000162695; -.
DR HOGENOM; CLU_080056_2_0_1; -.
DR OMA; NRNETWL; -.
DR OrthoDB; 586309at2759; -.
DR PhylomeDB; Q9NRW3; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.38; 2681.
DR PathwayCommons; Q9NRW3; -.
DR Reactome; R-HSA-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-HSA-75094; Formation of the Editosome.
DR SignaLink; Q9NRW3; -.
DR SIGNOR; Q9NRW3; -.
DR BioGRID-ORCS; 27350; 17 hits in 1049 CRISPR screens.
DR ChiTaRS; APOBEC3C; human.
DR GeneWiki; APOBEC3C; -.
DR GenomeRNAi; 27350; -.
DR Pharos; Q9NRW3; Tbio.
DR PRO; PR:Q9NRW3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NRW3; protein.
DR Bgee; ENSG00000244509; Expressed in leukocyte and 185 other tissues.
DR ExpressionAtlas; Q9NRW3; baseline and differential.
DR Genevisible; Q9NRW3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009972; P:cytidine deamination; IDA:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0070383; P:DNA cytosine deamination; IBA:GO_Central.
DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; Antiviral defense; Cytoplasm; Host-virus interaction;
KW Hydrolase; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..190
FT /note="DNA dC->dU-editing enzyme APOBEC-3C"
FT /id="PRO_0000171755"
FT DOMAIN 29..138
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 40..86
FT /note="(Microbial infection) Required for interaction with
FT human foamy virus protein Bet"
FT /evidence="ECO:0000269|PubMed:19074429"
FT ACT_SITE 68
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:3VM8, ECO:0007744|PDB:3VOW"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:3VM8, ECO:0007744|PDB:3VOW"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:3VM8, ECO:0007744|PDB:3VOW"
FT MUTAGEN 72
FT /note="L->D: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 75
FT /note="F->W: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 76
FT /note="C->K: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 79
FT /note="I->A: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 80
FT /note="L->A: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 81
FT /note="S->P: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 86
FT /note="Y->A: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 106
FT /note="E->K: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 107
FT /note="F->D: Resistant to HIV-1 Vif and abolishes Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 109
FT /note="A->K: Resistant to HIV-1 Vif."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 111
FT /note="H->D: Resistant to HIV-1 Vif and reduces Vif
FT binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 129
FT /note="P->A: No effect on Vif binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT MUTAGEN 141
FT /note="E->K: Remains sensitive to HIV-1 Vif but abolishes
FT Vif binding."
FT /evidence="ECO:0000269|PubMed:23001005"
FT CONFLICT 31
FT /note="N -> D (in Ref. 6; AAH11739)"
FT /evidence="ECO:0000305"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:3VOW"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3VM8"
FT STRAND 32..43
FT /evidence="ECO:0007829|PDB:3VOW"
FT STRAND 46..58
FT /evidence="ECO:0007829|PDB:3VOW"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3VOW"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:3VOW"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:3VOW"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:3VOW"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:3VOW"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:3VOW"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:3VOW"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3VOW"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:3VOW"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:3VOW"
SQ SEQUENCE 190 AA; 22826 MW; BE49E80F95C71214 CRC64;
MNPQIRNPMK AMYPGTFYFQ FKNLWEANDR NETWLCFTVE GIKRRSVVSW KTGVFRNQVD
SETHCHAERC FLSWFCDDIL SPNTKYQVTW YTSWSPCPDC AGEVAEFLAR HSNVNLTIFT
ARLYYFQYPC YQEGLRSLSQ EGVAVEIMDY EDFKYCWENF VYNDNEPFKP WKGLKTNFRL
LKRRLRESLQ
