ID G3TH88_LOXAF Unreviewed; 224 AA.
AC G3TH88;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Apolipoprotein B mRNA editing enzyme catalytic subunit 2 {ECO:0000313|Ensembl:ENSLAFP00000013904.2};
GN Name=APOBEC2 {ECO:0000313|Ensembl:ENSLAFP00000013904.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000013904.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000013904.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013904.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000013904.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013904.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR RefSeq; XP_003403977.1; XM_003403929.2.
DR AlphaFoldDB; G3TH88; -.
DR STRING; 9785.ENSLAFP00000013904; -.
DR Ensembl; ENSLAFT00000016561.2; ENSLAFP00000013904.2; ENSLAFG00000016563.2.
DR eggNOG; ENOG502RABR; Eukaryota.
DR GeneTree; ENSGT00940000156616; -.
DR HOGENOM; CLU_080056_0_0_1; -.
DR InParanoid; G3TH88; -.
DR OMA; MAQKEET; -.
DR OrthoDB; 4187079at2759; -.
DR TreeFam; TF331356; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:Ensembl.
DR GO; GO:0080111; P:DNA demethylation; IEA:Ensembl.
DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF4; C-U-EDITING ENZYME APOBEC-2; 1.
DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1.
DR Pfam; PF18772; APOBEC2; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 64..169
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 224 AA; 25672 MW; F6F7A7155C8324F5 CRC64;
MAEKEEAAAA AAPTSQNGED AENLEDPEKL KELIELPPFE IVTGERLPVN FFKFQFRNVE
YSSGRNKTFL CYVVEAQGKG GQVQASRGYL EDEHAAAHAE EAFFNTILPA FDPALRYNVT
WYVSSSPCAA CADRIIKTLN KTKNLRLLIL VGRLFMWEEP EIQAALKKLK EAGCKLRIMK
PQDFDYVWQN FVEQEEGQSK AFEPWEDIQE NFQYYEEKLA DILK
//