ID G1QZV0_NOMLE Unreviewed; 236 AA.
AC G1QZV0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=C->U-editing enzyme APOBEC-1 {ECO:0000256|ARBA:ARBA00014786};
DE EC=3.5.4.36 {ECO:0000256|ARBA:ARBA00012742};
DE AltName: Full=mRNA(cytosine(6666)) deaminase 1 {ECO:0000256|ARBA:ARBA00031639};
GN Name=APOBEC1 {ECO:0000313|Ensembl:ENSNLEP00000006471.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000006471.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000006471.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000006471.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in mRNA + H(+) + H2O = a uridine in mRNA + NH4(+);
CC Xref=Rhea:RHEA:74355, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:15145,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00034649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74356;
CC Evidence={ECO:0000256|ARBA:ARBA00034649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) +
CC uridine(6666) in apoB mRNA; Xref=Rhea:RHEA:21772, Rhea:RHEA-
CC COMP:13888, Rhea:RHEA-COMP:13889, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:65315,
CC ChEBI:CHEBI:82748; EC=3.5.4.36;
CC Evidence={ECO:0000256|ARBA:ARBA00034615};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21773;
CC Evidence={ECO:0000256|ARBA:ARBA00034615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR EMBL; ADFV01078557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QZV0; -.
DR STRING; 61853.ENSNLEP00000006471; -.
DR Ensembl; ENSNLET00000006799.2; ENSNLEP00000006471.1; ENSNLEG00000005342.2.
DR eggNOG; ENOG502SNW2; Eukaryota.
DR GeneTree; ENSGT00940000161190; -.
DR HOGENOM; CLU_080056_3_0_1; -.
DR InParanoid; G1QZV0; -.
DR OMA; MKLYALE; -.
DR OrthoDB; 5296257at2759; -.
DR TreeFam; TF331356; -.
DR Proteomes; UP000001073; Chromosome 23.
DR GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:Ensembl.
DR GO; GO:0080111; P:DNA demethylation; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IEA:Ensembl.
DR GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:Ensembl.
DR GO; GO:0090209; P:negative regulation of triglyceride metabolic process; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR CDD; cd01283; cytidine_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR041547; APOBEC1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF26; C-U-EDITING ENZYME APOBEC-1; 1.
DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1.
DR Pfam; PF18774; APOBEC4_like; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 10..134
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 236 AA; 28098 MW; A0CA8AB7AFCABC6F CRC64;
MTSEKGPSTG DPTLRRRIEP WEFDVFYDPR ELRKEACLLY EIKWGMSQKI WRSSGKNTTN
HVEVNFIKKF TSEGRFQSSI SCSITWFLSW SPCWECSQAI REFLSQHPGV TLVIYVARLF
WHMDQQNRQG LRDLVNSGVT IQIMRASEYY HCWRNFVNYP PGDEAHWPRY PPLWMMLYAL
ELHCIILSLP PCLKISRRWQ NHLTFFRLHL QNCHYQTIPP HILLATGLIH PSVTWR
//
