Q99J72 (ABEC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA dC->dU-editing enzyme APOBEC-3
EC=3.5.4.-

Alternative name(s):
Apolipoprotein B mRNA-editing complex 3
Short name=Arp3
CEM-15
Short name=CEM15

Gene names

Name:

Apobec3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity against HIV-1, simian immunodeficiency viruses (SIVs), mouse mammary tumor virus (MMTV) and friend murine leukemia virus (FrMLV) and may inhibit the mobility of LTR retrotransposons. Ref.6 Ref.8 Ref.9 Ref.11
Catalytic activity	Cytidine + H2O = uridine + NH3.
Cofactor	Zinc By similarity.
Subunit structure	Homodimer. Interacts with mouse mammary tumor virus (MMTV) nucleocapsid protein p14. Ref.7 Ref.9
Subcellular location	Cytoplasm Ref.6.
Tissue specificity	Expressed in spleen, node and lung. Ref.5
Domain	The CMP/dCMP deaminase zinc-binding 1 domain confers deoxycytidine deaminase activity, whereas the CMP/dCMP deaminase zinc-binding 2 domain mediates RNA-dependent oligomerization and virion incorporation (Ref.7). Ref.7
Miscellaneous	Probable human APOBEC3G ortholog.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family. Contains 2 CMP/dCMP deaminase zinc-binding domains.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW metabolic process Inferred from electronic annotation. Source: GOC negative regulation of transposition Inferred from direct assay Ref.6. Source: UniProtKB negative regulation of viral genome replication Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99J72-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q99J72-2)

The sequence of this isoform differs from the canonical sequence as follows:
     409-429: SWGLQDLVNDFGNLQLGPPMS → VRTTLLQGPAS

Isoform 3 (identifier: Q99J72-3)

The sequence of this isoform differs from the canonical sequence as follows:
     198-230: Missing.
     409-429: SWGLQDLVNDFGNLQLGPPMS → SRSHAS

Isoform 4 (identifier: Q99J72-4)

The sequence of this isoform differs from the canonical sequence as follows:
     198-230: Missing.

Note: Lacks exon V. Found in cell line MDTF.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 429	429	DNA dC->dU-editing enzyme APOBEC-3		PRO_0000171772
Regions
	Domain	71 – 108	38	CMP/dCMP deaminase zinc-binding 1
	Domain	288 – 319	32	CMP/dCMP deaminase zinc-binding 2
Sites
	Active site	73	1	Proton donor By similarity
	Metal binding	71	1	Zinc By similarity
	Metal binding	105	1	Zinc By similarity
	Metal binding	108	1	Zinc By similarity
	Metal binding	288	1	Zinc By similarity
	Metal binding	316	1	Zinc By similarity
	Metal binding	319	1	Zinc By similarity
Natural variations
	Alternative sequence	198 – 230	33	Missing in isoform 3 and isoform 4.		VSP_009831
	Alternative sequence	409 – 429	21	SWGLQ…GPPMS → VRTTLLQGPAS in isoform 2.		VSP_009832
	Alternative sequence	409 – 429	21	SWGLQ…GPPMS → SRSHAS in isoform 3.		VSP_009833
	Natural variant	20	1	L → V in cell line MDTF.
	Natural variant	31	1	K → E in cell line MDTF.
	Natural variant	34 – 35	2	GY → PF in cell line MDTF.
	Natural variant	34	1	G → R in cell lines L1.2 and 3T3. Ref.1 Ref.4
	Natural variant	37 – 38	2	KG → ID in cell lines L1.2 and 3T3.
	Natural variant	38	1	G → K in cell line MDTF; requires 2 nucleotide substitutions.
	Natural variant	111	1	Q → R in cell line L1.2.
	Natural variant	112 – 113	2	IV → VL in cell lines L1.2 and 3T3.
	Natural variant	112	1	I → V in cell line MDTF.
	Natural variant	128	1	S → F in cell line MDTF.
	Natural variant	134 – 139	6	VQDPET → IRNPEN in cell line MDTF.
	Natural variant	134 – 135	2	VQ → IR in cell lines L1.2 and 3T3.
	Natural variant	139 – 140	2	TQ → NQL in cell line 3T3.
	Natural variant	139	1	T → N in cell line L1.2. Ref.1 Ref.4
	Natural variant	148	1	Q → L in cell line MDTF.
	Natural variant	162 – 163	2	KK → EE in cell line MDTF.
	Natural variant	181	1	R → K in cell lines L1.2 and 3T3. Ref.1 Ref.4
	Natural variant	230 – 235	6	GRRMDP → RRRVHL in cell line 3T3.
	Natural variant	233 – 235	3	MDP → VHL.
	Natural variant	234 – 235	2	DP → SL in cell line MDTF.
	Natural variant	248	1	Q → L in cell line MDTF.
	Natural variant	258 – 259	2	RM → GV in cell line 3T3.
	Natural variant	258	1	R → G in cell line L1.2. Ref.1 Ref.4
	Natural variant	264	1	C → F in cell line MDTF.
	Natural variant	269	1	Q → W in cell line MDTF; requires 2 nucleotide substitutions.
	Natural variant	274	1	A → E in cell line MDTF.
	Natural variant	284 – 296	13	Missing in cell line MDTF.
	Natural variant	306	1	T → I in cell lines L1.2 and 3T3. Ref.1 Ref.4
	Natural variant	314	1	S → G in cell line EL4.
	Natural variant	328	1	R → K in cell line MDTF.
	Natural variant	381	1	N → S in cell line MDTF.
	Natural variant	387	1	W → R in splenocytes.
	Natural variant	394 – 395	2	II → KT in cell line MDTF.
	Natural variant	399	1	T → A in cell line L1.2.
	Natural variant	404	1	R → C in cell lines MDTF and 3T3.
	Natural variant	404	1	R → H in cell line L1.2. Ref.1 Ref.4
Experimental info
	Mutagenesis	73	1	E → A: Decrease in cytidine deaminase and antiviral activity. Ref.7
	Mutagenesis	73	1	E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-290.
	Mutagenesis	290	1	E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-73. Ref.7
	Mutagenesis	290	1	E → A: No effect on cytidine deaminase and antiviral activity. Ref.7
	Sequence conflict	203	1	P → S in AC113595. Ref.3
	Sequence conflict	227	1	C → W in AC113595. Ref.3
	Sequence conflict	230	1	G → R no nucleotide entry Ref.2
	Sequence conflict	410 – 414	5	WGLQD → RSHAS in BAC34023. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: 2B4361CDD81C99E5	FASTA	429	50,948
	10 20 30 40 50 60 MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLGYAKGRK DTFLCYEVTR KDCDSPVSLH 70 80 90 100 110 120 HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QIVRFLATHH 130 140 150 160 170 180 NLSLDIFSSR LYNVQDPETQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK 190 200 210 220 230 240 RLLTNFRYQD SKLQEILRPC YIPVPSSSSS TLSNICLTKG LPETRFCVEG RRMDPLSEEE 250 260 270 280 290 300 FYSQFYNQRV KHLCYYHRMK PYLCYQLEQF NGQAPLKGCL LSEKGKQHAE ILFLDKIRSM 310 320 330 340 350 360 ELSQVTITCY LTWSPCPNCA WQLAAFKRDR PDLILHIYTS RLYFHWKRPF QKGLCSLWQS 370 380 390 400 410 420 GILVDVMDLP QFTDCWTNFV NPKRPFWPWK GLEIISRRTQ RRLRRIKESW GLQDLVNDFG NLQLGPPMS
	Isoform 2 [UniParc]. Checksum: CCD9A467001DE2C5	FASTA	419	49,802
	10 20 30 40 50 60 MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLGYAKGRK DTFLCYEVTR KDCDSPVSLH 70 80 90 100 110 120 HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QIVRFLATHH 130 140 150 160 170 180 NLSLDIFSSR LYNVQDPETQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK 190 200 210 220 230 240 RLLTNFRYQD SKLQEILRPC YIPVPSSSSS TLSNICLTKG LPETRFCVEG RRMDPLSEEE 250 260 270 280 290 300 FYSQFYNQRV KHLCYYHRMK PYLCYQLEQF NGQAPLKGCL LSEKGKQHAE ILFLDKIRSM 310 320 330 340 350 360 ELSQVTITCY LTWSPCPNCA WQLAAFKRDR PDLILHIYTS RLYFHWKRPF QKGLCSLWQS 370 380 390 400 410 GILVDVMDLP QFTDCWTNFV NPKRPFWPWK GLEIISRRTQ RRLRRIKEVR TTLLQGPAS
	Isoform 3 [UniParc]. Checksum: 3C04E693DFD85F91	FASTA	381	45,778
	10 20 30 40 50 60 MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLGYAKGRK DTFLCYEVTR KDCDSPVSLH 70 80 90 100 110 120 HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QIVRFLATHH 130 140 150 160 170 180 NLSLDIFSSR LYNVQDPETQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK 190 200 210 220 230 240 RLLTNFRYQD SKLQEILRRM DPLSEEEFYS QFYNQRVKHL CYYHRMKPYL CYQLEQFNGQ 250 260 270 280 290 300 APLKGCLLSE KGKQHAEILF LDKIRSMELS QVTITCYLTW SPCPNCAWQL AAFKRDRPDL 310 320 330 340 350 360 ILHIYTSRLY FHWKRPFQKG LCSLWQSGIL VDVMDLPQFT DCWTNFVNPK RPFWPWKGLE 370 380 IISRRTQRRL RRIKESRSHA S
	Isoform 4 [UniParc]. Checksum: E63F76159882B20A	FASTA	396	47,423
	10 20 30 40 50 60 MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLGYAKGRK DTFLCYEVTR KDCDSPVSLH 70 80 90 100 110 120 HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QIVRFLATHH 130 140 150 160 170 180 NLSLDIFSSR LYNVQDPETQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK 190 200 210 220 230 240 RLLTNFRYQD SKLQEILRRM DPLSEEEFYS QFYNQRVKHL CYYHRMKPYL CYQLEQFNGQ 250 260 270 280 290 300 APLKGCLLSE KGKQHAEILF LDKIRSMELS QVTITCYLTW SPCPNCAWQL AAFKRDRPDL 310 320 330 340 350 360 ILHIYTSRLY FHWKRPFQKG LCSLWQSGIL VDVMDLPQFT DCWTNFVNPK RPFWPWKGLE 370 380 390 IISRRTQRRL RRIKESWGLQ DLVNDFGNLQ LGPPMS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANTS ARG-34; 37-ILE-ASP-38; 112-VAL-LEU-113; 134-ILE-ARG-135; ASN-139; LYS-181; 233-VAL-HIS-LEU-235; GLY-258; ILE-306 AND HIS-404. Strain: C57BL/6J. Tissue: Hippocampus and Retina.
[2]	Mariani R., Landau N.R. Submitted (FEB-2004) to UniProtKB Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 4), VARIANTS. Strain: C57BL/6J. Tissue: Spleen.
[3]	"Initial sequencing and comparative analysis of the mouse genome." Waterston R.H., Lindblad-Toh K., Birney E., Rogers J., Abril J.F., Agarwal P., Agarwala R., Ainscough R., Alexandersson M., An P., Antonarakis S.E., Attwood J., Baertsch R., Bailey J., Barlow K., Beck S., Berry E., Birren B. , Bloom T., Bork P., Botcherby M., Bray N., Brent M.R., Brown D.G., Brown S.D., Bult C., Burton J., Butler J., Campbell R.D., Carninci P., Cawley S., Chiaromonte F., Chinwalla A.T., Church D.M., Clamp M., Clee C., Collins F.S., Cook L.L., Copley R.R., Coulson A., Couronne O., Cuff J., Curwen V., Cutts T., Daly M., David R., Davies J., Delehaunty K.D., Deri J., Dermitzakis E.T., Dewey C., Dickens N.J., Diekhans M., Dodge S., Dubchak I., Dunn D.M., Eddy S.R., Elnitski L., Emes R.D., Eswara P., Eyras E., Felsenfeld A., Fewell G.A., Flicek P., Foley K., Frankel W.N., Fulton L.A., Fulton R.S., Furey T.S., Gage D., Gibbs R.A., Glusman G., Gnerre S., Goldman N., Goodstadt L., Grafham D., Graves T.A., Green E.D., Gregory S., Guigo R., Guyer M., Hardison R.C., Haussler D., Hayashizaki Y., Hillier L.W., Hinrichs A., Hlavina W., Holzer T., Hsu F., Hua A., Hubbard T., Hunt A., Jackson I., Jaffe D.B., Johnson L.S., Jones M., Jones T.A., Joy A., Kamal M., Karlsson E.K., Karolchik D., Kasprzyk A., Kawai J., Keibler E., Kells C., Kent W.J., Kirby A., Kolbe D.L., Korf I., Kucherlapati R.S., Kulbokas E.J., Kulp D., Landers T., Leger J.P., Leonard S., Letunic I., Levine R., Li J., Li M., Lloyd C., Lucas S., Ma B., Maglott D.R., Mardis E.R., Matthews L., Mauceli E., Mayer J.H., McCarthy M., McCombie W.R., McLaren S., McLay K., McPherson J.D., Meldrim J., Meredith B., Mesirov J.P., Miller W., Miner T.L., Mongin E., Montgomery K.T., Morgan M., Mott R., Mullikin J.C., Muzny D.M., Nash W.E., Nelson J.O., Nhan M.N., Nicol R., Ning Z., Nusbaum C., O'Connor M.J., Okazaki Y., Oliver K., Overton-Larty E., Pachter L., Parra G., Pepin K.H., Peterson J., Pevzner P., Plumb R., Pohl C.S., Poliakov A., Ponce T.C., Ponting C.P., Potter S., Quail M., Reymond A., Roe B.A., Roskin K.M., Rubin E.M., Rust A.G., Santos R., Sapojnikov V., Schultz B., Schultz J., Schwartz M.S., Schwartz S., Scott C., Seaman S., Searle S., Sharpe T., Sheridan A., Shownkeen R., Sims S., Singer J.B., Slater G., Smit A., Smith D.R., Spencer B., Stabenau A., Stange-Thomann N., Sugnet C., Suyama M., Tesler G., Thompson J., Torrents D., Trevaskis E., Tromp J., Ucla C., Ureta-Vidal A., Vinson J.P., Von Niederhausern A.C., Wade C.M., Wall M., Weber R.J., Weiss R.B., Wendl M.C., West A.P., Wetterstrand K., Wheeler R., Whelan S., Wierzbowski J., Willey D., Williams S., Wilson R.K., Winter E., Worley K.C., Wyman D., Yang S., Yang S.P., Zdobnov E.M., Zody M.C., Lander E.S. Nature 420:520-562(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ARG-34; 37-ILE-ASP-38; 112-VAL-LEU-113; 134-ILE-ARG-135; ASN-139; LYS-181; 233-VAL-HIS-LEU-235; GLY-258; ILE-306 AND HIS-404. Tissue: Mammary tumor.
[5]	"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif." Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., Muenk C., Nymark-McMahon H., Landau N.R. Cell 114:21-31(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DNA C TO U EDITING ACTIVITY, TISSUE SPECIFICITY.
[6]	"APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons." Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., Landau N.R., Weitzman M.D. Curr. Biol. 16:480-485(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN RETROTRANSPOSITION, SUBCELLULAR LOCATION.
[7]	"Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains." Hakata Y., Landau N.R. J. Biol. Chem. 281:36624-36631(2006) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING, SUBUNIT, MUTAGENESIS OF GLU-73 AND GLU-290.
[8]	"Restriction of foamy viruses by APOBEC cytidine deaminases." Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A., Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O. J. Virol. 80:605-614(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SFV RESTRICTION.
[9]	"APOBEC3 inhibits mouse mammary tumour virus replication in vivo." Okeoma C.M., Lovsin N., Peterlin B.M., Ross S.R. Nature 445:927-930(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MMTV RESTRICTION, INTERACTION WITH MMTV NUCLEOCAPSID PROTEIN P14.
[10]	"The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements." Chiu Y.L., Greene W.C. Annu. Rev. Immunol. 26:317-353(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[11]	"Mouse APOBEC3 restricts friend leukemia virus infection and pathogenesis in vivo." Takeda E., Tsuji-Kawahara S., Sakamoto M., Langlois M.A., Neuberger M.S., Rada C., Miyazawa M. J. Virol. 82:10998-11008(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN FRMLV RESTRICTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK044394 mRNA. Translation: BAC31901.1. AK049998 mRNA. Translation: BAC34023.1. AC113595 Genomic DNA. No translation available. BC003314 mRNA. Translation: AAH03314.1.
IPI	IPI00406662. IPI00411147. IPI00411148. IPI00411149.
UniGene	Mm.284059. Mm.432615.
3D structure databases
ProteinModelPortal	Q99J72.
SMR	Q99J72. Positions 25-198, 258-406.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000105249.
PTM databases
PhosphoSite	Q99J72.
Proteomic databases
PRIDE	Q99J72.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000165537; ENSMUSP00000132391; ENSMUSG00000009585.
UCSC	uc007wur.2. mouse. uc007wut.2. mouse.
Organism-specific databases
MGI	MGI:1933111. Apobec3.
Phylogenomic databases
eggNOG	NOG135704.
GeneTree	ENSGT00530000062933.
HOGENOM	HOG000033755.
HOVERGEN	HBG050434.
InParanoid	Q99J72.
OrthoDB	EOG480HX1.
Gene expression databases
ArrayExpress	Q99J72.
Bgee	Q99J72.
CleanEx	MM_APOBEC3.
Genevestigator	Q99J72.
GermOnline	ENSMUSG00000009585. Mus musculus.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR013158. APOBEC_N. IPR016193. Cytidine_deaminase-like. [Graphical view]
Pfam	PF08210. APOBEC_N. 2 hits. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 2 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

ABEC3_MOUSE

Accession

Primary (citable) accession number: Q99J72
Secondary accession number(s): Q8C7L0, Q8C8V7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program