ABEC1_RAT
ID ABEC1_RAT Reviewed; 229 AA.
AC P38483;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=C->U-editing enzyme APOBEC-1;
DE EC=3.5.4.36;
DE AltName: Full=Apolipoprotein B mRNA-editing enzyme 1;
DE AltName: Full=mRNA(cytosine(6666)) deaminase 1;
GN Name=Apobec1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Small intestine;
RX PubMed=8511591; DOI=10.1126/science.8511591;
RA Teng B., Burant C.F., Davidson N.O.;
RT "Molecular cloning of an apolipoprotein B messenger RNA editing protein.";
RL Science 260:1816-1819(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH A1CF.
RX PubMed=10669759; DOI=10.1128/mcb.20.5.1846-1854.2000;
RA Mehta A., Kinter M.T., Sherman N.E., Driscoll D.M.;
RT "Molecular cloning of APOBEC-1 complementation factor, a novel RNA-binding
RT protein involved in the editing of apolipoprotein B mRNA.";
RL Mol. Cell. Biol. 20:1846-1854(2000).
RN [4]
RP INTERACTION WITH SYNCRIP.
RX PubMed=11134005; DOI=10.1074/jbc.m006435200;
RA Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A.,
RA Scott J., Davidson N.O.;
RT "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that
RT interacts with both apobec-1 and apobec-1 complementation factor to
RT modulate C to U editing.";
RL J. Biol. Chem. 276:10272-10283(2001).
CC -!- FUNCTION: Catalytic component of the apolipoprotein B mRNA editing
CC enzyme complex which is responsible for the postranscriptional editing
CC of a CAA codon for Gln to a UAA codon for stop in the APOB mRNA. May
CC also play a role in the epigenetic regulation of gene expression by
CC participating in DNA demethylation. {ECO:0000250|UniProtKB:Q9TUI7}.
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:0000250|UniProtKB:P41238};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9Y235};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Y235};
CC -!- SUBUNIT: Homodimer. Part of the apolipoprotein B mRNA editing complex
CC with A1CF. Interacts with SYNCRIP. Interacts with HNRPAB.
CC {ECO:0000250|UniProtKB:P41238}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41238}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver as well as small intestine.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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; L07114; AAA17394.1; -; mRNA.
DR EMBL; BC085335; AAH85335.1; -; mRNA.
DR PIR; I59577; I59577.
DR RefSeq; NP_037039.1; NM_012907.2.
DR RefSeq; XP_006237352.1; XM_006237290.2.
DR RefSeq; XP_006237353.1; XM_006237291.2.
DR RefSeq; XP_006237354.1; XM_006237292.2.
DR RefSeq; XP_006237355.1; XM_006237293.2.
DR RefSeq; XP_017447973.1; XM_017592484.1.
DR AlphaFoldDB; P38483; -.
DR SMR; P38483; -.
DR CORUM; P38483; -.
DR STRING; 10116.ENSRNOP00000020735; -.
DR PhosphoSitePlus; P38483; -.
DR PaxDb; P38483; -.
DR GeneID; 25383; -.
DR KEGG; rno:25383; -.
DR UCSC; RGD:2133; rat.
DR CTD; 339; -.
DR RGD; 2133; Apobec1.
DR VEuPathDB; HostDB:ENSRNOG00000015411; -.
DR eggNOG; ENOG502SNW2; Eukaryota.
DR HOGENOM; CLU_080056_3_0_1; -.
DR InParanoid; P38483; -.
DR OMA; MKLYALE; -.
DR OrthoDB; 1246623at2759; -.
DR PhylomeDB; P38483; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.36; 5301.
DR Reactome; R-RNO-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-RNO-75094; Formation of the Editosome.
DR PRO; PR:P38483; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000015411; Expressed in duodenum and 17 other tissues.
DR Genevisible; P38483; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0004126; F:cytidine deaminase activity; IDA:MGI.
DR GO; GO:0004131; F:cytosine deaminase activity; IDA:RGD.
DR GO; GO:0008047; F:enzyme activator activity; IDA:RGD.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0046087; P:cytidine metabolic process; IC:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IDA:RGD.
DR GO; GO:0051607; P:defense response to virus; IDA:RGD.
DR GO; GO:0070383; P:DNA cytosine deamination; IDA:RGD.
DR GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; ISO:RGD.
DR GO; GO:0042953; P:lipoprotein transport; ISO:RGD.
DR GO; GO:0016556; P:mRNA modification; IDA:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISO:RGD.
DR GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:RGD.
DR GO; GO:0090209; P:negative regulation of triglyceride metabolic process; ISO:RGD.
DR GO; GO:0090366; P:positive regulation of mRNA modification; IDA:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0010332; P:response to gamma radiation; ISO:RGD.
DR GO; GO:0006970; P:response to osmotic stress; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; mRNA processing; Reference proteome;
KW Zinc.
FT CHAIN 1..229
FT /note="C->U-editing enzyme APOBEC-1"
FT /id="PRO_0000171748"
FT DOMAIN 10..134
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y235"
SQ SEQUENCE 229 AA; 27274 MW; 08766441882789B3 CRC64;
MSSETGPVAV DPTLRRRIEP HEFEVFFDPR ELRKETCLLY EINWGGRHSI WRHTSQNTNK
HVEVNFIEKF TTERYFCPNT RCSITWFLSW SPCGECSRAI TEFLSRYPHV TLFIYIARLY
HHADPRNRQG LRDLISSGVT IQIMTEQESG YCWRNFVNYS PSNEAHWPRY PHLWVRLYVL
ELYCIILGLP PCLNILRRKQ PQLTFFTIAL QSCHYQRLPP HILWATGLK
