Reviewed, UniProtKB/Swiss-Prot Q99J72 (ABEC3_MOUSE)

Names and origin

Protein names

DNA dC->dU-editing enzyme APOBEC-3
Also known as:
     EC 3.5.4.-
     Apolipoprotein B mRNA-editing complex 3
     Arp3
     CEM15
     CEM-15

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 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.
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)
None. [Check GOA]

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.
Notes: Lacks exon V. Also active in inhibiting HIV-1 in vitro.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 429	429	DNA dC->dU-editing enzyme APOBEC-3
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.
	Alternative sequence	409 – 429	21	SWGLQ…GPPMS → VRTTLLQGPAS in isoform 2.
	Alternative sequence	409 – 429	21	SWGLQ…GPPMS → SRSHAS in isoform 3.
	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.
	Natural variant	37 – 38	2	KG → ID in cell lines L1.2 and 3T3.
	Natural variant	38	1	G → K in cell line MDTF.
	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.
	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.
	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.
	Natural variant	258	1	R → G in cell line L1.2.
	Natural variant	264	1	C → F in cell line MDTF.
	Natural variant	269	1	Q → W in cell line MDTF.
	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.
	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.
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 [UniParc]. Checksum: CCD9A467001DE2C5		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		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		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

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[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.,