CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019046
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA dC->dU-editing enzyme APOBEC-3D 
Protein Synonyms/Alias
 A3D 
Gene Name
 APOBEC3D 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
62FRGPVLPKRQSNHRQubiquitination[1]
347SVKIMGYKDFVSCWKubiquitination[1]
365YSDDEPFKPWKGLQTubiquitination[1, 2]
368DEPFKPWKGLQTNFRubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination- independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double- stranded RNA. May inhibit the mobility of LTR and non-LTR retrotransposons. 
Sequence Annotation
 DOMAIN 78 112 CMP/dCMP deaminase zinc-binding 1.
 DOMAIN 262 296 CMP/dCMP deaminase zinc-binding 2.
 ACT_SITE 264 264 Proton donor (By similarity).
 METAL 78 78 Zinc (By similarity).
 METAL 109 109 Zinc (By similarity).
 METAL 112 112 Zinc (By similarity).
 METAL 262 262 Zinc (By similarity).
 METAL 293 293 Zinc (By similarity).
 METAL 296 296 Zinc (By similarity).  
Keyword
 Antiviral defense; Complete proteome; Cytoplasm; Hydrolase; Immunity; Innate immunity; Metal-binding; Reference proteome; Repeat; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 386 AA 
Protein Sequence
MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGPVL 60
PKRQSNHRQE VYFRFENHAE MCFLSWFCGN RLPANRRFQI TWFVSWNPCL PCVVKVTKFL 120
AEHPNVTLTI SAARLYYYRD RDWRWVLLRL HKAGARVKIM DYEDFAYCWE NFVCNEGQPF 180
MPWYKFDDNY ASLHRTLKEI LRNPMEAMYP HIFYFHFKNL LKACGRNESW LCFTMEVTKH 240
HSAVFRKRGV FRNQVDPETH CHAERCFLSW FCDDILSPNT NYEVTWYTSW SPCPECAGEV 300
AEFLARHSNV NLTIFTARLC YFWDTDYQEG LCSLSQEGAS VKIMGYKDFV SCWKNFVYSD 360
DEPFKPWKGL QTNFRLLKRR LREILQ 386 
Gene Ontology
 GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB.
 GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051607; P:defense response to virus; IDA:UniProtKB.
 GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB.
 GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO:0045869; P:negative regulation of retroviral genome replication; IDA:UniProtKB.
 GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. 
Interpro
 IPR016192; APOBEC/CMP_deaminase_Zn-bd.
 IPR007904; APOBEC_C.
 IPR016193; Cytidine_deaminase-like. 
Pfam
 PF05240; APOBEC_C 
SMART
  
PROSITE
 PS00903; CYT_DCMP_DEAMINASES 
PRINTS