ABEC1_RABIT
ID ABEC1_RABIT Reviewed; 236 AA.
AC P47855;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=C->U-editing enzyme APOBEC-1;
DE EC=3.5.4.36 {ECO:0000269|PubMed:8063816};
DE AltName: Full=Apolipoprotein B mRNA-editing enzyme 1;
DE AltName: Full=mRNA(cytosine(6666)) deaminase 1;
GN Name=APOBEC1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP MUTAGENESIS OF HIS-61; VAL-62; GLU-63; PRO-92; CYS-93 AND CYS-96.
RC STRAIN=New Zealand white; TISSUE=Small intestine;
RX PubMed=8063816; DOI=10.1016/s0021-9258(17)31865-3;
RA Yamanaka S., Poksay K.S., Balestra M.E., Zeng G.-Q., Innerarity T.L.;
RT "Cloning and mutagenesis of the rabbit ApoB mRNA editing protein. A zinc
RT motif is essential for catalytic activity, and noncatalytic auxiliary
RT factor(s) of the editing complex are widely distributed.";
RL J. Biol. Chem. 269:21725-21734(1994).
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. Also
CC involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA. May also
CC play a role in the epigenetic regulation of gene expression through the
CC process of active DNA demethylation. {ECO:0000269|PubMed:8063816}.
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:0000269|PubMed:8063816};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:8063816};
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 HNRPAB and SYNCRIP.
CC {ECO:0000250|UniProtKB:P41238}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41238}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the intestine.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; U10695; AAA56718.1; -; mRNA.
DR PIR; A53853; A53853.
DR RefSeq; NP_001075810.1; NM_001082341.1.
DR AlphaFoldDB; P47855; -.
DR SMR; P47855; -.
DR STRING; 9986.ENSOCUP00000021115; -.
DR GeneID; 100009191; -.
DR KEGG; ocu:100009191; -.
DR CTD; 339; -.
DR eggNOG; ENOG502SNW2; Eukaryota.
DR InParanoid; P47855; -.
DR OrthoDB; 1246623at2759; -.
DR BRENDA; 3.5.4.36; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
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 Pfam; PF18774; APOBEC4_like; 1.
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..236
FT /note="C->U-editing enzyme APOBEC-1"
FT /id="PRO_0000171747"
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"
FT MUTAGEN 61
FT /note="H->A: None or little editing activity."
FT /evidence="ECO:0000269|PubMed:8063816"
FT MUTAGEN 61
FT /note="H->C: Retains most editing activity."
FT /evidence="ECO:0000269|PubMed:8063816"
FT MUTAGEN 62
FT /note="V->A: Retains most editing activity."
FT /evidence="ECO:0000269|PubMed:8063816"
FT MUTAGEN 63
FT /note="E->A: None or little editing activity."
FT /evidence="ECO:0000269|PubMed:8063816"
FT MUTAGEN 92
FT /note="P->A: Retains most editing activity."
FT /evidence="ECO:0000269|PubMed:8063816"
FT MUTAGEN 93
FT /note="C->A: None or little editing activity."
FT /evidence="ECO:0000269|PubMed:8063816"
FT MUTAGEN 96
FT /note="C->A: None or little editing activity."
FT /evidence="ECO:0000269|PubMed:8063816"
SQ SEQUENCE 236 AA; 27719 MW; AB3041CA5102F1F3 CRC64;
MASEKGPSNK DYTLRRRIEP WEFEVFFDPQ ELRKEACLLY EIKWGASSKT WRSSGKNTTN
HVEVNFLEKL TSEGRLGPST CCSITWFLSW SPCWECSMAI REFLSQHPGV TLIIFVARLF
QHMDRRNRQG LKDLVTSGVT VRVMSVSEYC YCWENFVNYP PGKAAQWPRY PPRWMLMYAL
ELYCIILGLP PCLKISRRHQ KQLTFFSLTP QYCHYKMIPP YILLATGLLQ PSVPWR
