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 27-MAR-2024, entry version 71.
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 eggNOG; ENOG502QQXT; Eukaryota.
DR OrthoDB; 68574at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR038953; APOBEC4.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR PANTHER; PTHR35672; C-U-EDITING ENZYME APOBEC-4-RELATED; 1.
DR PANTHER; PTHR35672:SF1; C-U-EDITING ENZYME APOBEC-4-RELATED; 1.
DR Pfam; PF18778; NAD1; 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
//
