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Q99J72 (ABEC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429DNA dC->dU-editing enzyme APOBEC-3
PRO_0000171772

Regions

Domain71 – 10838CMP/dCMP deaminase zinc-binding 1
Domain288 – 31932CMP/dCMP deaminase zinc-binding 2

Sites

Active site731Proton donor By similarity
Metal binding711Zinc By similarity
Metal binding1051Zinc By similarity
Metal binding1081Zinc By similarity
Metal binding2881Zinc By similarity
Metal binding3161Zinc By similarity
Metal binding3191Zinc By similarity

Natural variations

Alternative sequence198 – 23033Missing in isoform 3 and isoform 4.
VSP_009831
Alternative sequence409 – 42921SWGLQ…GPPMS → VRTTLLQGPAS in isoform 2.
VSP_009832
Alternative sequence409 – 42921SWGLQ…GPPMS → SRSHAS in isoform 3.
VSP_009833
Natural variant201L → V in cell line MDTF.
Natural variant311K → E in cell line MDTF.
Natural variant34 – 352GY → PF in cell line MDTF.
Natural variant341G → R in cell lines L1.2 and 3T3. Ref.1 Ref.4
Natural variant37 – 382KG → ID in cell lines L1.2 and 3T3.
Natural variant381G → K in cell line MDTF; requires 2 nucleotide substitutions.
Natural variant1111Q → R in cell line L1.2.
Natural variant112 – 1132IV → VL in cell lines L1.2 and 3T3.
Natural variant1121I → V in cell line MDTF.
Natural variant1281S → F in cell line MDTF.
Natural variant134 – 1396VQDPET → IRNPEN in cell line MDTF.
Natural variant134 – 1352VQ → IR in cell lines L1.2 and 3T3.
Natural variant139 – 1402TQ → NQL in cell line 3T3.
Natural variant1391T → N in cell line L1.2. Ref.1 Ref.4
Natural variant1481Q → L in cell line MDTF.
Natural variant162 – 1632KK → EE in cell line MDTF.
Natural variant1811R → K in cell lines L1.2 and 3T3. Ref.1 Ref.4
Natural variant230 – 2356GRRMDP → RRRVHL in cell line 3T3.
Natural variant233 – 2353MDP → VHL.
Natural variant234 – 2352DP → SL in cell line MDTF.
Natural variant2481Q → L in cell line MDTF.
Natural variant258 – 2592RM → GV in cell line 3T3.
Natural variant2581R → G in cell line L1.2. Ref.1 Ref.4
Natural variant2641C → F in cell line MDTF.
Natural variant2691Q → W in cell line MDTF; requires 2 nucleotide substitutions.
Natural variant2741A → E in cell line MDTF.
Natural variant284 – 29613Missing in cell line MDTF.
Natural variant3061T → I in cell lines L1.2 and 3T3. Ref.1 Ref.4
Natural variant3141S → G in cell line EL4.
Natural variant3281R → K in cell line MDTF.
Natural variant3811N → S in cell line MDTF.
Natural variant3871W → R in splenocytes.
Natural variant394 – 3952II → KT in cell line MDTF.
Natural variant3991T → A in cell line L1.2.
Natural variant4041R → C in cell lines MDTF and 3T3.
Natural variant4041R → H in cell line L1.2. Ref.1 Ref.4

Experimental info

Mutagenesis731E → A: Decrease in cytidine deaminase and antiviral activity. Ref.7
Mutagenesis731E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-290.
Mutagenesis2901E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-73. Ref.7
Mutagenesis2901E → A: No effect on cytidine deaminase and antiviral activity. Ref.7
Sequence conflict2031P → S in AC113595. Ref.3
Sequence conflict2271C → W in AC113595. Ref.3
Sequence conflict2301G → R no nucleotide entry Ref.2
Sequence conflict410 – 4145WGLQD → RSHAS in BAC34023. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 2B4361CDD81C99E5

FASTA42950,948
        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 

« Hide

Isoform 2 [UniParc].

Checksum: CCD9A467001DE2C5
Show »

FASTA41949,802
Isoform 3 [UniParc].

Checksum: 3C04E693DFD85F91
Show »

FASTA38145,778
Isoform 4 [UniParc].

Checksum: E63F76159882B20A
Show »

FASTA39647,423

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
IPIIPI00406662.
IPI00411147.
IPI00411148.
IPI00411149.
UniGeneMm.284059.
Mm.432615.

3D structure databases

ProteinModelPortalQ99J72.
SMRQ99J72. Positions 25-198, 258-406.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000105249.

PTM databases

PhosphoSiteQ99J72.

Proteomic databases

PRIDEQ99J72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000165537; ENSMUSP00000132391; ENSMUSG00000009585.
UCSCuc007wur.2. mouse.
uc007wut.2. mouse.

Organism-specific databases

MGIMGI:1933111. Apobec3.

Phylogenomic databases

eggNOGNOG135704.
GeneTreeENSGT00530000062933.
HOGENOMHOG000033755.
HOVERGENHBG050434.
InParanoidQ99J72.
OrthoDBEOG480HX1.

Gene expression databases

ArrayExpressQ99J72.
BgeeQ99J72.
CleanExMM_APOBEC3.
GenevestigatorQ99J72.
GermOnlineENSMUSG00000009585. Mus musculus.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamPF08210. APOBEC_N. 2 hits.
[Graphical view]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameABEC3_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families