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UniProtKB/Swiss-Prot entry Q99J72


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ABEC3_MOUSE
Primary accession number Q99J72
Secondary accession numbers Q8C7L0 Q8C8V7
Integrated into Swiss-Prot on April 13, 2004
Sequence was last modified on April 13, 2004 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 57)
Name and origin of the protein
Protein name DNA dC->dU-editing enzyme APOBEC-3
Synonyms EC 3.5.4.-
Apolipoprotein B mRNA-editing complex 3
Arp3
CEM-15
CEM15
Gene name
Name: Apobec3
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND 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;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 4), AND VARIANTS.
STRAIN=C57BL/6J;
TISSUE=Spleen;
Mariani R., Landau N.R.;
Submitted (FEB-2004) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE.
DOI=10.1038/nature01262; PubMed=12466850 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Initial sequencing and comparative analysis of the mouse genome.";
Nature 420:520-562(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND 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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DNA C TO U EDITING ACTIVITY, AND TISSUE SPECIFICITY.
DOI=10.1016/S0092-8674(03)00515-4; PubMed=12859895 [NCBI, ExPASy, EBI, Israel, Japan]
Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.;
"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
Cell 114:21-31(2003).
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).
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ99J72-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ99J72-2
    Features which should be applied to build the isoform sequence: VSP_009832.
    Name3
    Isoform IDQ99J72-3
    Features which should be applied to build the isoform sequence: VSP_009831, VSP_009833.
    Name4
    Isoform IDQ99J72-4
    Note: Lacks exon V. Also active in inhibiting HIV-1 in vitro.
    Features which should be applied to build the isoform sequence: VSP_009831.
  • 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.
  • SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK044394; BAC31901.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK049998; BAC34023.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC113595; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC003314; AAH03314.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.284059
3D structure databases
ModBase Q99J72.
Organism-specific databases
MGI MGI:1933111; Apobec3.
Gene expression databases
ArrayExpress 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 of domain structure.
Pfam PF05240; APOBEC_C; 2.
PF08210; APOBEC_N; 2.
Pfam graphical view of domain structure.
PROSITE PS00903; CYT_DCMP_DEAMINASES; 2.
BLOCKS Q99J72.
Genome annotation databases
Ensembl ENSMUSG00000009585; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM Q99J72; -.
HOVERGEN Q99J72; -.
Other
SOURCE Apobec3; Mus musculus.
ProtoNet Q99J72.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   429  429     DNA dC->dU-editing enzyme APOBEC-3. PRO_0000171772
ACT_SITE   73    73        Proton donor (By similarity). 
METAL   71    71        Zinc (By similarity). 
METAL   105   105        Zinc (By similarity). 
METAL   108   108        Zinc (By similarity). 
METAL   288   288        Zinc (By similarity). 
METAL   316   316        Zinc (By similarity). 
METAL   319   319        Zinc (By similarity). 
VAR_SEQ   198   230        Missing (in isoform 3 and isoform 4). VSP_009831
VAR_SEQ   409   429        SWGLQDLVNDFGNLQLGPPMS -> VRTTLLQGPAS (in isoform 2). VSP_009832
VAR_SEQ   409   429        SWGLQDLVNDFGNLQLGPPMS -> SRSHAS (in isoform 3). VSP_009833
VARIANT   20    20  1     L -> V (in cell line MDTF). 
VARIANT   31    31  1     K -> E (in cell line MDTF). 
VARIANT   34    35  2     GY -> PF (in cell line MDTF). 
VARIANT   34    34  1     G -> R (in cell lines L1.2 and 3T3). 
VARIANT   37    38  2     KG -> ID (in cell lines L1.2 and 3T3). 
VARIANT   38    38  1     G -> K (in cell line MDTF; requires 2 nucleotide substitutions). 
VARIANT   111   111  1     Q -> R (in cell line L1.2). 
VARIANT   112   113  2     IV -> VL (in cell lines L1.2 and 3T3). 
VARIANT   112   112  1     I -> V (in cell line MDTF). 
VARIANT   128   128  1     S -> F (in cell line MDTF). 
VARIANT   134   139  6     VQDPET -> IRNPEN (in cell line MDTF). 
VARIANT   134   135  2     VQ -> IR (in cell lines L1.2 and 3T3). 
VARIANT   139   140  2     TQ -> NQL (in cell line 3T3). 
VARIANT   139   139  1     T -> N (in cell line L1.2). 
VARIANT   148   148  1     Q -> L (in cell line MDTF). 
VARIANT   162   163  2     KK -> EE (in cell line MDTF). 
VARIANT   181   181  1     R -> K (in cell lines L1.2 and 3T3). 
VARIANT   198   230  33     Missing (in cell line MDTF). 
VARIANT   230   235  6     GRRMDP -> RRRVHL (in cell line 3T3). 
VARIANT   233   235  3     MDP -> VHL. 
VARIANT   234   235  2     DP -> SL (in cell line MDTF). 
VARIANT   248   248  1     Q -> L (in cell line MDTF). 
VARIANT   258   259  2     RM -> GV (in cell line 3T3). 
VARIANT   258   258  1     R -> G (in cell line L1.2). 
VARIANT   264   264  1     C -> F (in cell line MDTF). 
VARIANT   269   269  1     Q -> W (in cell line MDTF; requires 2 nucleotide substitutions). 
VARIANT   274   274  1     A -> E (in cell line MDTF). 
VARIANT   284   296  13     Missing (in cell line MDTF). 
VARIANT   306   306  1     T -> I (in cell lines L1.2 and 3T3). 
VARIANT   314   314  1     S -> G (in cell line EL4). 
VARIANT   328   328  1     R -> K (in cell line MDTF). 
VARIANT   381   381  1     N -> S (in cell line MDTF). 
VARIANT   387   387  1     W -> R (in splenocytes). 
VARIANT   394   395  2     II -> KT (in cell line MDTF). 
VARIANT   399   399  1     T -> A (in cell line L1.2). 
VARIANT   404   404  1     R -> C (in cell lines MDTF and 3T3). 
VARIANT   404   404  1     R -> H (in cell line L1.2). 
CONFLICT   203   203        P -> S (in Ref. 3). 
CONFLICT   227   227        C -> W (in Ref. 3). 
CONFLICT   230   230        G -> R (in Ref. 2). 
CONFLICT   410   414        WGLQD -> RSHAS (in Ref. 1; BAC34023). 
Sequence information
Length: 429 AA [This is the length of the unprocessed precursor] Molecular weight: 50948 Da [This is the MW of the unprocessed precursor] CRC64: 2B4361CDD81C99E5 [This is a checksum on the sequence]
        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 

Q99J72 in FASTA format

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View entry in raw text format (no links)
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