ID Q59GY0_HUMAN Unreviewed; 212 AA. AC Q59GY0; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 24-JAN-2024, entry version 81. DE SubName: Full=Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C variant {ECO:0000313|EMBL:BAD92216.1}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD92216.1}; RN [1] {ECO:0000313|EMBL:BAD92216.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:BAD92216.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. 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}. 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; AB208979; BAD92216.1; -; mRNA. DR AlphaFoldDB; Q59GY0; -. DR SMR; Q59GY0; -. DR IntAct; Q59GY0; 1. DR MINT; Q59GY0; -. DR PeptideAtlas; Q59GY0; -. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd01283; cytidine_deaminase; 1. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR016193; Cytidine_deaminase-like. DR PANTHER; PTHR13857:SF46; DNA DC-DU-EDITING ENZYME APOBEC-3C; 1. DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1. DR Pfam; PF18782; NAD2; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 2: Evidence at transcript level; KW Lipoprotein {ECO:0000313|EMBL:BAD92216.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 51..160 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD92216.1" SQ SEQUENCE 212 AA; 25196 MW; D8B4CC2B887DA4FC CRC64; RKRSHSASEK SGTGTSISKR LNMNPQIRNP MKAMYPGTFY FQFKNLWEAN DRNETWLCFT VEGIKRRSVV SWKTGVFRNQ VDSETHCHAE RCFLSWFCDD ILSPNTKYQV TWYTSWSPCP DCAGEVAEFL ARHSNVNLTI FTARLYYFQY PCYQEGLRSL SQEGVAVEIM DYEDFKYCWE NFVYNDNEPF KPWKGLKTNF RLLKRRLRES LQ //