CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022093
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA dC->dU-editing enzyme APOBEC-3C 
Protein Synonyms/Alias
 A3C; APOBEC1-like; Phorbolin I 
Gene Name
 APOBEC3C 
Gene Synonyms/Alias
 APOBEC1L; PBI 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10PQIRNPMKAMYPGTFubiquitination[1]
51RRSVVSWKTGVFRNQubiquitination[1, 2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. 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. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. 
Sequence Annotation
 DOMAIN 66 100 CMP/dCMP deaminase zinc-binding.
 ACT_SITE 68 68 Proton donor (By similarity).
 METAL 66 66 Zinc; catalytic (By similarity).
 METAL 97 97 Zinc; catalytic (By similarity).
 METAL 100 100 Zinc; catalytic (By similarity).  
Keyword
 3D-structure; Antiviral defense; Complete proteome; Cytoplasm; Host-virus interaction; Hydrolase; Immunity; Innate immunity; Metal-binding; Nucleus; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 190 AA 
Protein Sequence
MNPQIRNPMK AMYPGTFYFQ FKNLWEANDR NETWLCFTVE GIKRRSVVSW KTGVFRNQVD 60
SETHCHAERC FLSWFCDDIL SPNTKYQVTW YTSWSPCPDC AGEVAEFLAR HSNVNLTIFT 120
ARLYYFQYPC YQEGLRSLSQ EGVAVEIMDY EDFKYCWENF VYNDNEPFKP WKGLKTNFRL 180
LKRRLRESLQ 190 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; 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:0009972; P:cytidine deamination; IDA:UniProtKB.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0080111; P:DNA demethylation; IDA:UniProtKB.
 GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
 GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
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