ID Q3U9G8_MOUSE Unreviewed; 229 AA. AC Q3U9G8; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 147. 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|MGI:MGI:103298}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE30699.1}; RN [1] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE30699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30699.1}, and DBA/2 RC {ECO:0000313|EMBL:BAE27161.1}; RC TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30699.1}, and Spleen RC {ECO:0000313|EMBL:BAE38079.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK146427; BAE27161.1; -; mRNA. DR EMBL; AK151799; BAE30699.1; -; mRNA. DR EMBL; AK165209; BAE38079.1; -; mRNA. DR RefSeq; NP_001127863.1; NM_001134391.1. DR RefSeq; NP_112436.1; NM_031159.3. DR RefSeq; XP_006505464.1; XM_006505401.2. DR RefSeq; XP_011239461.1; XM_011241159.2. DR AlphaFoldDB; Q3U9G8; -. DR SMR; Q3U9G8; -. DR MaxQB; Q3U9G8; -. DR Antibodypedia; 22955; 177 antibodies from 27 providers. DR DNASU; 11810; -. DR GeneID; 11810; -. DR KEGG; mmu:11810; -. DR AGR; MGI:103298; -. DR CTD; 339; -. DR MGI; MGI:103298; Apobec1. DR VEuPathDB; HostDB:ENSMUSG00000040613; -. DR HOGENOM; CLU_080056_3_0_1; -. DR OMA; MKLYALE; -. DR OrthoDB; 5296257at2759; -. DR BioGRID-ORCS; 11810; 0 hits in 118 CRISPR screens. DR ChiTaRS; Apobec1; mouse. DR ExpressionAtlas; Q3U9G8; baseline and differential. 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:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016554; P:cytidine to uridine editing; IEA:Ensembl. DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; 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 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 10..134 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" SQ SEQUENCE 229 AA; 27522 MW; 1CBCF9929066ABAD CRC64; MSSETGPVAV DPTLRRRIEP HEFEVFFDPR ELRKETCLLY EINWGGRHSV WRHTSQNTSN HVEVNFLEKF TTERYFRPNT RCSITWFLSW SPCGECSRAI TEFLSRHPYV TLFIYIARLY HHTDQRNRQG LRDLISSGVT IQIMTEQEYC YCWRNFVNYP PSNEAYWPRY PHLWVKLYVL ELYCIILGLP PCLKILRRKQ PQLTFFTITL QTCHYQRIPP HLLWATGLK //