ID   ABEC4_MACFA             Reviewed;         363 AA.
AC   Q8WP22;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Putative C->U-editing enzyme APOBEC-4;
DE            EC=3.5.4.-;
DE   AltName: Full=Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4;
GN   Name=APOBEC4; ORFNames=QtsA-21565;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
CC   -!- FUNCTION: Putative C to U editing enzyme whose physiological substrate
CC       is not yet known. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; AB074455; BAB72086.1; -; mRNA.
DR   RefSeq; NP_001306289.1; NM_001319360.1.
DR   AlphaFoldDB; Q8WP22; -.
DR   SMR; Q8WP22; -.
DR   STRING; 9541.XP_005540275.1; -.
DR   GeneID; 102126303; -.
DR   CTD; 403314; -.
DR   eggNOG; ENOG502QQXT; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR038953; APOBEC4.
DR   InterPro; IPR013158; APOBEC_N.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   PANTHER; PTHR35672; PTHR35672; 1.
DR   Pfam; PF08210; APOBEC_N; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; mRNA processing; Reference proteome; Zinc.
FT   CHAIN           1..363
FT                   /note="Putative C->U-editing enzyme APOBEC-4"
FT                   /id="PRO_0000239356"
FT   DOMAIN          61..177
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  41300 MW;  753A3A82673EEB7C CRC64;
     MEPTYEEYLA NHGTIVKPYY WLSFSLDCSN CPYHIRTGEE ARVSLTEFCQ IFGFPYGTTY
     PQTKHLTFYE LKTSSGSLVQ KGHASSCTGN YIHPESMLFE MNGYLDSAIY NNDSIRHIIL
     YCNNSPCNEA NHCCISKVYN FLITYPGITL SIYFSQLYHT EMDFPASAWN REALRSLASL
     WPRVVLSPIS GGIWHSVLHS FVSGVSGSHV FQPILTGRAL TDRYNAYEIN AITGVKPFFT
     DVLLHTKRNP NTKAQMALES YPLNNAFPGQ SFQMTSGIPP DLRAPVVFVL LPLRDLPPMH
     MGQDPNKPRN IIRHLNMPQM SFQETKDLER LPTRRSVETV EITERFASSK QAEEKTKKKK
     GKK