Reviewed,
UniProtKB/Swiss-Prot Q99J72 (ABEC3_MOUSE)
Last modified
June 16, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||
| 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 nucleusInferred 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 bindingInferred 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
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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. 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. 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 | |
|---|---|
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


