ID   ABEC4_RAT               Reviewed;         388 AA.
AC   Q6AXX9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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}.
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; BC079272; AAH79272.1; -; mRNA.
DR   RefSeq; NP_001017492.1; NM_001017492.1.
DR   RefSeq; XP_008767888.1; XM_008769666.2.
DR   RefSeq; XP_008767889.1; XM_008769667.2.
DR   AlphaFoldDB; Q6AXX9; -.
DR   SMR; Q6AXX9; -.
DR   STRING; 10116.ENSRNOP00000034180; -.
DR   PaxDb; Q6AXX9; -.
DR   Ensembl; ENSRNOT00000036906; ENSRNOP00000034180; ENSRNOG00000028089.
DR   Ensembl; ENSRNOT00000100845; ENSRNOP00000077092; ENSRNOG00000028089.
DR   GeneID; 498251; -.
DR   KEGG; rno:498251; -.
DR   UCSC; RGD:1560256; rat.
DR   CTD; 403314; -.
DR   RGD; 1560256; Apobec4.
DR   eggNOG; ENOG502QQXT; Eukaryota.
DR   GeneTree; ENSGT00390000014243; -.
DR   HOGENOM; CLU_832944_0_0_1; -.
DR   InParanoid; Q6AXX9; -.
DR   OMA; VRHLNMP; -.
DR   OrthoDB; 1149880at2759; -.
DR   PhylomeDB; Q6AXX9; -.
DR   TreeFam; TF338173; -.
DR   Reactome; R-RNO-72200; mRNA Editing: C to U Conversion.
DR   Reactome; R-RNO-75094; Formation of the Editosome.
DR   PRO; PR:Q6AXX9; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000028089; Expressed in testis and 4 other tissues.
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   InterPro; IPR038953; APOBEC4.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   PANTHER; PTHR35672; PTHR35672; 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..388
FT                   /note="Putative C->U-editing enzyme APOBEC-4"
FT                   /id="PRO_0000239358"
FT   DOMAIN          60..176
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   REGION          322..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  44519 MW;  BCA0DA5452C94F1E CRC64;
     MEPLYEEYLT HSGTIVKPYY WLSVSLNCTN CPYHIRTGEE ARVPYTEFHQ TFGFPWSTYP
     QTKHLTFYEL RSSSGNLIQK GLASNCTGSH THPESMLFER DGYLDSLIFH DSNIRHIILY
     SNNSPCDEAN HCCISKMYNF LMNYPEVTLS VFFSQLYHTE NQFPTSAWNR EALRGLASLW
     PQVTLSAISG GIWQSILETF VSGISEGLTA VRPFTAGRTL TDRYNAYEIN CITEVKPYFT
     DALHSWQKEN QDQKVWAASE NQPLHNTTPA QWQPDMSQDC RTPAVFMLVP YRDLPPIHVN
     PSPQKPRTVV RHLNTLQLSA SKVKALRKSP SGRPVKKEEA RKGSTRSQEA NETNKSKWKK
     QTLFIKSNIC HLLEREQKKI GILSSWSV