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Single-stranded DNA cytosine deaminase (EC 3.5.4.38) (Activation-induced cytidine deaminase) (AID) (Cytidine aminohydrolase)

 AICDA_MOUSE             Reviewed;         198 AA.
Q9WVE0;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-FEB-2018, entry version 124.
RecName: Full=Single-stranded DNA cytosine deaminase;
EC=3.5.4.38 {ECO:0000269|PubMed:12692563, ECO:0000269|PubMed:23803409};
AltName: Full=Activation-induced cytidine deaminase;
Short=AID;
AltName: Full=Cytidine aminohydrolase;
Name=Aicda; Synonyms=Aid;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10373455; DOI=10.1074/jbc.274.26.18470;
Muramatsu M., Sankaranand V.S., Anant S., Sugai M., Kinoshita K.,
Davidson N.O., Honjo T.;
"Specific expression of activation-induced cytidine deaminase (AID), a
novel member of the RNA-editing deaminase family in germinal center B
cells.";
J. Biol. Chem. 274:18470-18476(1999).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-56 AND GLU-58.
PubMed=12692563; DOI=10.1038/nature01574;
Chaudhuri J., Tian M., Khuong C., Chua K., Pinaud E., Alt F.W.;
"Transcription-targeted DNA deamination by the AID antibody
diversification enzyme.";
Nature 422:726-730(2003).
[3]
INTERACTION WITH SUPT6H; TRIM28 AND NCL.
PubMed=21518874; DOI=10.1073/pnas.1104423108;
Okazaki I.M., Okawa K., Kobayashi M., Yoshikawa K., Kawamoto S.,
Nagaoka H., Shinkura R., Kitawaki Y., Taniguchi H., Natsume T.,
Iemura S., Honjo T.;
"Histone chaperone Spt6 is required for class switch recombination but
not somatic hypermutation.";
Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011).
[4]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
PHE-15.
PubMed=23803409; DOI=10.1016/j.clim.2013.05.017;
Caratao N., Cortesao C.S., Reis P.H., Freitas R.F., Jacob C.M.,
Pastorino A.C., Carneiro-Sampaio M., Barreto V.M.;
"A novel activation-induced cytidine deaminase (AID) mutation in
Brazilian patients with hyper-IgM type 2 syndrome.";
Clin. Immunol. 148:279-286(2013).
-!- FUNCTION: Single-stranded DNA-specific cytidine deaminase.
Involved in somatic hypermutation (SHM), gene conversion, and
class-switch recombination (CSR) in B-lymphocytes by deaminating C
to U during transcription of Ig-variable (V) and Ig-switch (S)
region DNA. Required for several crucial steps of B-cell terminal
differentiation necessary for efficient antibody responses. May
also play a role in the epigenetic regulation of gene expression
by participating in DNA demethylation.
{ECO:0000269|PubMed:12692563, ECO:0000269|PubMed:23803409}.
-!- CATALYTIC ACTIVITY: Cytosine in single-stranded DNA + H(2)O =
uracil in single-stranded DNA + NH(3).
{ECO:0000269|PubMed:12692563, ECO:0000269|PubMed:23803409}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9GZX7};
-!- SUBUNIT: Interacts with CTNNBL1; the interaction is important for
the immunoglobulin switch activity of AICDA. Interacts (via its
NLS) with KPNA1. Interacts with PKA/PRKACA and PRKAR1A/PKR1 (By
similarity). Interacts with SUPT6H, TRIM28 and NCL.
{ECO:0000250|UniProtKB:Q9GZX7, ECO:0000269|PubMed:21518874}.
-!- INTERACTION:
P24522:GADD45A (xeno); NbExp=3; IntAct=EBI-3835567, EBI-448167;
Q91Z31:Ptbp2; NbExp=4; IntAct=EBI-3835567, EBI-647632;
Q64511:Top2b; NbExp=3; IntAct=EBI-3835567, EBI-2325586;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GZX7}.
Cytoplasm {ECO:0000269|PubMed:23803409}. Note=Predominantly
cytoplasmic but shuttles between the nucleus and the cytoplasm.
{ECO:0000250|UniProtKB:Q9GZX7}.
-!- PTM: Ser-38 is the major site whereas Thr-27 is the minor site of
phosphorylation. Phosphorylation regulates its class-switch
recombination activity (By similarity). {ECO:0000250}.
-!- PTM: Probably monoubiquitinated on several residues by RNF126.
{ECO:0000250|UniProtKB:Q9GZX7}.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
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EMBL; AF132979; AAD41793.1; -; mRNA.
CCDS; CCDS20497.1; -.
RefSeq; NP_033775.1; NM_009645.2.
UniGene; Mm.391503; -.
ProteinModelPortal; Q9WVE0; -.
SMR; Q9WVE0; -.
BioGrid; 198040; 5.
DIP; DIP-48714N; -.
IntAct; Q9WVE0; 54.
MINT; Q9WVE0; -.
STRING; 10090.ENSMUSP00000040524; -.
iPTMnet; Q9WVE0; -.
PhosphoSitePlus; Q9WVE0; -.
PaxDb; Q9WVE0; -.
PRIDE; Q9WVE0; -.
DNASU; 11628; -.
Ensembl; ENSMUST00000043301; ENSMUSP00000040524; ENSMUSG00000040627.
GeneID; 11628; -.
KEGG; mmu:11628; -.
UCSC; uc009dpj.1; mouse.
CTD; 57379; -.
MGI; MGI:1342279; Aicda.
eggNOG; ENOG410IFHW; Eukaryota.
eggNOG; ENOG4111HYQ; LUCA.
GeneTree; ENSGT00530000062933; -.
HOGENOM; HOG000033754; -.
HOVERGEN; HBG050434; -.
InParanoid; Q9WVE0; -.
KO; K10989; -.
OMA; RNKNGCH; -.
OrthoDB; EOG091G0J2L; -.
PhylomeDB; Q9WVE0; -.
TreeFam; TF331356; -.
BRENDA; 3.5.4.38; 3474.
PRO; PR:Q9WVE0; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000040627; -.
CleanEx; MM_AICDA; -.
ExpressionAtlas; Q9WVE0; baseline and differential.
Genevisible; Q9WVE0; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0000178; C:exosome (RNase complex); IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0004126; F:cytidine deaminase activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0009972; P:cytidine deamination; IMP:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
GO; GO:0045190; P:isotype switching; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0090310; P:negative regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
GO; GO:0097752; P:regulation of DNA stability; ISO:MGI.
GO; GO:0016445; P:somatic diversification of immunoglobulins; ISO:MGI.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISS:UniProtKB.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR013158; APOBEC_N.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF08210; APOBEC_N; 1.
SUPFAM; SSF53927; SSF53927; 1.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Metal-binding;
mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation; Zinc.
CHAIN 1 198 Single-stranded DNA cytosine deaminase.
/FTId=PRO_0000171688.
DOMAIN 23 129 CMP/dCMP-type deaminase.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
REGION 2 26 Interaction with SUPT6H.
{ECO:0000250|UniProtKB:Q9GZX7}.
REGION 39 42 Important for interaction with CTNNBL1.
{ECO:0000250|UniProtKB:Q9GZX7}.
REGION 88 116 Required for interaction with RNF126.
{ECO:0000250|UniProtKB:Q9GZX7}.
MOTIF 1 30 Bipartite nuclear localization signal.
{ECO:0000250|UniProtKB:Q9GZX7}.
MOTIF 183 198 Nuclear export signal.
{ECO:0000250|UniProtKB:Q9GZX7}.
ACT_SITE 58 58 Proton donor.
{ECO:0000250|UniProtKB:P0ABF6}.
METAL 56 56 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9GZX7}.
METAL 87 87 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9GZX7}.
METAL 90 90 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9GZX7}.
MOD_RES 27 27 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q9GZX7}.
MOD_RES 38 38 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q9GZX7}.
MUTAGEN 15 15 F->L: Severely decreased cytidine
deaminase activity. Loss of mutagenic
activity. {ECO:0000269|PubMed:23803409}.
MUTAGEN 56 56 H->R: Loss of the cytidine deaminase
activity; when associated with Q-58.
{ECO:0000269|PubMed:12692563}.
MUTAGEN 58 58 E->Q: Loss of the cytidine deaminase
activity; when associated with R-56.
{ECO:0000269|PubMed:12692563}.
SEQUENCE 198 AA; 24031 MW; 18A3BA10CA54BEB2 CRC64;
MDSLLMKQKK FLYHFKNVRW AKGRHETYLC YVVKRRDSAT SCSLDFGHLR NKSGCHVELL
FLRYISDWDL DPGRCYRVTW FTSWSPCYDC ARHVAEFLRW NPNLSLRIFT ARLYFCEDRK
AEPEGLRRLH RAGVQIGIMT FKDYFYCWNT FVENRERTFK AWEGLHENSV RLTRQLRRIL
LPLYEVDDLR DAFRMLGF


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