Reviewed, UniProtKB/Swiss-Prot Q99J72 (ABEC3_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Probable human APOBEC3G ortholog. Has DNA deaminase (cytidine deaminase) activity. Mediates G-to-A hypermutation in newly synthesized HIV-1 viral DNA and is thus able to prevent HIV-1 infectivity in vitro, in the presence and absence of HIV-1 VIF (virion infectivity factor).
Cofactor	Zinc By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Mainly cytoplasmic, small amount are found in the nucleus By similarity.
Tissue specificity	Expressed in spleen, node and lung. Ref.5
Polymorphism	Polymorphism seems to be an important factor for the ability of the protein to prevent HIV-1 infectivity in vitro. The protein derived from MDTF and EL4 cell lines are unable to reduce HIV-1 infectivity, while the protein derived from L1.2, 3T3 and splenocytes are able to do it, in the presence and absence of HIV-1 VIF (virion infectivity factor).
Miscellaneous	HIV-1 VIF (virion infectivity factor) does not bind to mouse APOBEC3.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
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: UniProtKB-KW
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. Also active in inhibiting HIV-1 in vitro.

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
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. Ref.1 Ref.4
	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. Ref.1 Ref.4
	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. Ref.1 Ref.4
	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	198 – 230	33	Missing in cell line MDTF.
	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. Ref.1 Ref.4
	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. Ref.1 Ref.4
	Natural variant	404	1	R → H in cell line L1.2. Ref.1 Ref.4
Experimental info
	Sequence conflict	203	1	P → S Ref.3
	Sequence conflict	227	1	C → W Ref.3
	Sequence conflict	230	1	G → R 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. 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. 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. 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: 16141072] [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: 12466850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[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: 15489334] [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: 12859895] [Abstract] Cited for: DNA C TO U EDITING ACTIVITY, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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
ModBase	Search...
PTM databases
PhosphoSite	Q99J72.
Genome annotation databases
Ensembl	ENSMUSG00000009585. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:1933111. Apobec3.
Phylogenomic databases
HOGENOM	Q99J72.
HOVERGEN	Q99J72.
Gene expression databases
ArrayExpress	Q99J72.
Bgee	Q99J72.
CleanEx	MM_APOBEC3.
GermOnline	ENSMUSG00000009585. Mus musculus.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR007904. APOBEC_C. IPR013158. APOBEC_N. [Graphical view]
Pfam	PF05240. APOBEC_C. 2 hits. PF08210. APOBEC_N. 2 hits. [Graphical view]
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)