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Protein

DNA dC->dU-editing enzyme APOBEC-3

Gene

Apobec3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.4 Publications

Miscellaneous

Probable human APOBEC3G ortholog.

Catalytic activityi

Cytidine + H2O = uridine + NH3.

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi82ZincBy similarity1
Active sitei84Proton donorBy similarity1
Metal bindingi116ZincBy similarity1
Metal bindingi119ZincBy similarity1
Metal bindingi299ZincBy similarity1
Metal bindingi327ZincBy similarity1
Metal bindingi330ZincBy similarity1

GO - Molecular functioni

  • cytidine deaminase activity Source: GO_Central
  • deoxycytidine deaminase activity Source: MGI
  • RNA binding Source: GO_Central
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cytidine to uridine editing Source: GO_Central
  • defense response to virus Source: MGI
  • DNA demethylation Source: GO_Central
  • hematopoietic progenitor cell differentiation Source: MGI
  • innate immune response Source: UniProtKB-KW
  • negative regulation of transposition Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
  • regulation of defense response to virus Source: MGI
  • regulation of viral life cycle Source: MGI

Keywordsi

Molecular functionHydrolase
Biological processAntiviral defense, Immunity, Innate immunity
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.1 3474
ReactomeiR-MMU-72200 mRNA Editing: C to U Conversion
R-MMU-75094 Formation of the Editosome

Names & Taxonomyi

Protein namesi
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 namesi
Name:Apobec3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1933111 Apobec3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi84E → A: Decrease in cytidine deaminase and antiviral activity. 1 Publication1
Mutagenesisi84E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-301. 1 Publication1
Mutagenesisi301E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-84. 1 Publication1
Mutagenesisi301E → A: No effect on cytidine deaminase and antiviral activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001717721 – 440DNA dC->dU-editing enzyme APOBEC-3Add BLAST440

Proteomic databases

MaxQBiQ99J72
PaxDbiQ99J72
PRIDEiQ99J72

PTM databases

iPTMnetiQ99J72
PhosphoSitePlusiQ99J72

Expressioni

Tissue specificityi

Expressed in spleen, node and lung.1 Publication

Gene expression databases

BgeeiENSMUSG00000009585 Expressed in 195 organ(s), highest expression level in bone marrow
CleanExiMM_APOBEC3
ExpressionAtlasiQ99J72 baseline and differential
GenevisibleiQ99J72 MM

Interactioni

Subunit structurei

Homodimer. Interacts with mouse mammary tumor virus (MMTV) nucleocapsid protein p14.2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000105249

Structurei

3D structure databases

ProteinModelPortaliQ99J72
SMRiQ99J72
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 165CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd BLAST117
Domaini249 – 368CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd BLAST120

Domaini

The CMP/dCMP deaminase domain 1 confers deoxycytidine deaminase activity, whereas the CMP/dCMP deaminase domain 2 mediates RNA-dependent oligomerization and virion incorporation.1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410JBA1 Eukaryota
ENOG41119MS LUCA
GeneTreeiENSGT00530000062933
HOGENOMiHOG000033755
HOVERGENiHBG050434
InParanoidiQ99J72
OrthoDBiEOG091G0J2L
PhylomeDBiQ99J72
TreeFamiTF331356

Family and domain databases

InterProiView protein in InterPro
IPR016192 APOBEC/CMP_deaminase_Zn-bd
IPR013158 APOBEC_N
IPR002125 CMP_dCMP_dom
IPR016193 Cytidine_deaminase-like
PfamiView protein in Pfam
PF08210 APOBEC_N, 2 hits
SUPFAMiSSF53927 SSF53927, 2 hits
PROSITEiView protein in PROSITE
PS00903 CYT_DCMP_DEAMINASES_1, 2 hits
PS51747 CYT_DCMP_DEAMINASES_2, 2 hits

Sequences (4+)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q99J72-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MQPQRLGPRA GMGPFCLGCS HRKCYSPIRN LISQETFKFH FKNLGYAKGR
60 70 80 90 100
KDTFLCYEVT RKDCDSPVSL HHGVFKNKDN IHAEICFLYW FHDKVLKVLS
110 120 130 140 150
PREEFKITWY MSWSPCFECA EQIVRFLATH HNLSLDIFSS RLYNVQDPET
160 170 180 190 200
QQNLCRLVQE GAQVAAMDLY EFKKCWKKFV DNGGRRFRPW KRLLTNFRYQ
210 220 230 240 250
DSKLQEILRP CYISVPSSSS STLSNICLTK GLPETRFWVE GRRMDPLSEE
260 270 280 290 300
EFYSQFYNQR VKHLCYYHRM KPYLCYQLEQ FNGQAPLKGC LLSEKGKQHA
310 320 330 340 350
EILFLDKIRS MELSQVTITC YLTWSPCPNC AWQLAAFKRD RPDLILHIYT
360 370 380 390 400
SRLYFHWKRP FQKGLCSLWQ SGILVDVMDL PQFTDCWTNF VNPKRPFWPW
410 420 430 440
KGLEIISRRT QRRLRRIKES WGLQDLVNDF GNLQLGPPMS
Length:440
Mass (Da):52,213
Last modified:December 20, 2017 - v3
Checksum:iAA0DA7AC616252E9
GO
Isoform 2 (identifier: Q99J72-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     420-440: SWGLQDLVNDFGNLQLGPPMS → VRTTLLQGPAS

Show »
Length:430
Mass (Da):51,067
Checksum:i236E70AA28F7E16C
GO
Isoform 3 (identifier: Q99J72-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-241: Missing.
     420-440: SWGLQDLVNDFGNLQLGPPMS → SRSHAS

Show »
Length:392
Mass (Da):46,970
Checksum:i457EC3A5D3B011E8
GO
Isoform 4 (identifier: Q99J72-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-241: Missing.

Note: Lacks exon V. Found in cell line MDTF.
Show »
Length:407
Mass (Da):48,615
Checksum:iAE01BC74D716229A
GO

Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3U5C5Q3U5C5_MOUSE
Apolipoprotein B mRNA editing enzym...
Apobec3 APOBEC3
396Annotation score:
E9QMH1E9QMH1_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
429Annotation score:
Q3TI69Q3TI69_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
297Annotation score:
H3BKS1H3BKS1_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
85Annotation score:
H3BJJ6H3BJJ6_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
151Annotation score:
H3BJD1H3BJD1_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
166Annotation score:
H3BL97H3BL97_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
79Annotation score:
A0A2R8VKS7A0A2R8VKS7_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
97Annotation score:
H3BKS5H3BKS5_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
46Annotation score:
A0A2R8VHT8A0A2R8VHT8_MOUSE
DNA dC->dU-editing enzyme APOBEC-3
Apobec3
62Annotation score:

Sequence cautioni

The sequence AAH03314 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC31901 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC34023 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6L → M in BAC31901 (PubMed:16141072).Curated1
Sequence conflicti6L → M in AAH03314 (PubMed:15489334).Curated1
Sequence conflicti214S → P in BAC31901 (PubMed:16141072).Curated1
Sequence conflicti214S → P in AAH03314 (PubMed:15489334).Curated1
Sequence conflicti238W → C in BAC31901 (PubMed:16141072).Curated1
Sequence conflicti238W → C in AAH03314 (PubMed:15489334).Curated1
Sequence conflicti241G → R no nucleotide entry (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti31L → V in cell line MDTF. 1
Natural varianti42K → E in cell line MDTF. 1
Natural varianti45 – 46GY → PF in cell line MDTF. 2
Natural varianti45G → R in cell lines L1.2 and 3T3. 2 Publications1
Natural varianti48 – 49KG → ID in cell lines L1.2 and 3T3. 2 Publications2
Natural varianti49G → K in cell line MDTF; requires 2 nucleotide substitutions. 1
Natural varianti122Q → R in cell line L1.2. 1
Natural varianti123 – 124IV → VL in cell lines L1.2 and 3T3. 2 Publications2
Natural varianti123I → V in cell line MDTF. 1
Natural varianti139S → F in cell line MDTF. 1
Natural varianti145 – 150VQDPET → IRNPEN in cell line MDTF. 6
Natural varianti145 – 146VQ → IR in cell lines L1.2 and 3T3. 2 Publications2
Natural varianti150 – 151TQ → NQL in cell line 3T3. 2
Natural varianti150T → N in cell line L1.2. 2 Publications1
Natural varianti159Q → L in cell line MDTF. 1
Natural varianti173 – 174KK → EE in cell line MDTF. 2
Natural varianti192R → K in cell lines L1.2 and 3T3. 2 Publications1
Natural varianti241 – 246GRRMDP → RRRVHL in cell line 3T3. 6
Natural varianti244 – 246MDP → VHL2 Publications3
Natural varianti245 – 246DP → SL in cell line MDTF. 2
Natural varianti259Q → L in cell line MDTF. 1
Natural varianti269 – 270RM → GV in cell line 3T3. 2
Natural varianti269R → G in cell line L1.2. 2 Publications1
Natural varianti275C → F in cell line MDTF. 1
Natural varianti280Q → W in cell line MDTF; requires 2 nucleotide substitutions. 1
Natural varianti285A → E in cell line MDTF. 1
Natural varianti295 – 307Missing in cell line MDTF. Add BLAST13
Natural varianti317T → I in cell lines L1.2 and 3T3. 2 Publications1
Natural varianti325S → G in cell line EL4. 1
Natural varianti339R → K in cell line MDTF. 1
Natural varianti392N → S in cell line MDTF. 1
Natural varianti398W → R in splenocytes. 1
Natural varianti405 – 406II → KT in cell line MDTF. 2
Natural varianti410T → A in cell line L1.2. 1
Natural varianti415R → C in cell lines MDTF and 3T3. 1
Natural varianti415R → H in cell line L1.2. 2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009831209 – 241Missing in isoform 3 and isoform 4. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_009832420 – 440SWGLQ…GPPMS → VRTTLLQGPAS in isoform 2. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_009833420 – 440SWGLQ…GPPMS → SRSHAS in isoform 3. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044394 mRNA Translation: BAC31901.1 Different initiation.
AK049998 mRNA Translation: BAC34023.1 Different initiation.
AC113595 Genomic DNA No translation available.
BC003314 mRNA Translation: AAH03314.1 Different initiation.
RefSeqiXP_017172295.1, XM_017316806.1 [Q99J72-3]
UniGeneiMm.284059
Mm.432615

Genome annotation databases

EnsembliENSMUST00000175714; ENSMUSP00000135027; ENSMUSG00000009585 [Q99J72-1]
ENSMUST00000175752; ENSMUSP00000135358; ENSMUSG00000009585 [Q99J72-4]
ENSMUST00000176325; ENSMUSP00000134838; ENSMUSG00000009585 [Q99J72-2]
ENSMUST00000177098; ENSMUSP00000135079; ENSMUSG00000009585 [Q99J72-3]
GeneIDi80287

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044394 mRNA Translation: BAC31901.1 Different initiation.
AK049998 mRNA Translation: BAC34023.1 Different initiation.
AC113595 Genomic DNA No translation available.
BC003314 mRNA Translation: AAH03314.1 Different initiation.
RefSeqiXP_017172295.1, XM_017316806.1 [Q99J72-3]
UniGeneiMm.284059
Mm.432615

3D structure databases

ProteinModelPortaliQ99J72
SMRiQ99J72
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000105249

PTM databases

iPTMnetiQ99J72
PhosphoSitePlusiQ99J72

Proteomic databases

MaxQBiQ99J72
PaxDbiQ99J72
PRIDEiQ99J72

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000175714; ENSMUSP00000135027; ENSMUSG00000009585 [Q99J72-1]
ENSMUST00000175752; ENSMUSP00000135358; ENSMUSG00000009585 [Q99J72-4]
ENSMUST00000176325; ENSMUSP00000134838; ENSMUSG00000009585 [Q99J72-2]
ENSMUST00000177098; ENSMUSP00000135079; ENSMUSG00000009585 [Q99J72-3]
GeneIDi80287

Organism-specific databases

CTDi80287
MGIiMGI:1933111 Apobec3

Phylogenomic databases

eggNOGiENOG410JBA1 Eukaryota
ENOG41119MS LUCA
GeneTreeiENSGT00530000062933
HOGENOMiHOG000033755
HOVERGENiHBG050434
InParanoidiQ99J72
OrthoDBiEOG091G0J2L
PhylomeDBiQ99J72
TreeFamiTF331356

Enzyme and pathway databases

BRENDAi3.5.4.1 3474
ReactomeiR-MMU-72200 mRNA Editing: C to U Conversion
R-MMU-75094 Formation of the Editosome

Miscellaneous databases

PROiPR:Q99J72
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000009585 Expressed in 195 organ(s), highest expression level in bone marrow
CleanExiMM_APOBEC3
ExpressionAtlasiQ99J72 baseline and differential
GenevisibleiQ99J72 MM

Family and domain databases

InterProiView protein in InterPro
IPR016192 APOBEC/CMP_deaminase_Zn-bd
IPR013158 APOBEC_N
IPR002125 CMP_dCMP_dom
IPR016193 Cytidine_deaminase-like
PfamiView protein in Pfam
PF08210 APOBEC_N, 2 hits
SUPFAMiSSF53927 SSF53927, 2 hits
PROSITEiView protein in PROSITE
PS00903 CYT_DCMP_DEAMINASES_1, 2 hits
PS51747 CYT_DCMP_DEAMINASES_2, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiABEC3_MOUSE
AccessioniPrimary (citable) accession number: Q99J72
Secondary accession number(s): H3BJL0, Q8C7L0, Q8C8V7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: December 20, 2017
Last modified: November 7, 2018
This is version 130 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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