ID B9ZZS2_MOUSE Unreviewed; 429 AA.
AC B9ZZS2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=single-stranded DNA cytosine deaminase {ECO:0000256|ARBA:ARBA00029489};
DE EC=3.5.4.38 {ECO:0000256|ARBA:ARBA00029489};
GN Name=Apobec3 {ECO:0000313|MGI:MGI:1933111};
GN Synonyms=APOBEC3 {ECO:0000313|EMBL:BAH29958.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAH29958.1};
RN [1] {ECO:0000313|EMBL:BAH29958.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/WySnJ {ECO:0000313|EMBL:BAH29958.1};
RX PubMed=18786991; DOI=10.1128/JVI.01311-08;
RA Takeda E., Tsuji-Kawahara S., Sakamoto M., Langlois M., Neuberger M.S.,
RA Rada C., Miyazawa M.;
RT "Mouse APOBEC3 restricts friend leukemia virus infection and pathogenesis
RT in vivo.";
RL J. Virol. 82:10998-11008(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-
CC deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948,
CC Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:133902; EC=3.5.4.38;
CC Evidence={ECO:0000256|ARBA:ARBA00029350};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR EMBL; AB461446; BAH29958.1; -; mRNA.
DR AlphaFoldDB; B9ZZS2; -.
DR AGR; MGI:1933111; -.
DR MGI; MGI:1933111; Apobec3.
DR ChiTaRS; Apobec3; mouse.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01283; cytidine_deaminase; 2.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF43; DNA DC-DU-EDITING ENZYME APOBEC-3H; 1.
DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1.
DR Pfam; PF18772; APOBEC2; 1.
DR Pfam; PF18782; NAD2; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipoprotein {ECO:0000313|EMBL:BAH29958.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..154
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 238..357
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 429 AA; 51017 MW; BE44D01380AD7F6E CRC64;
MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLRYAIDRK DTFLCYEVTR KDCDSPVSLH
HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QVLRFLATHH
NLSLDIFSSR LYNIRDPENQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK
KLLTNFRYQD SKLQEILRPC YIPVPSSSSS TLSNICLTKG LPETRFCVEG RRVHLLSEEE
FYSQFYNQRV KHLCYYHGMK PYLCYQLEQF NGQAPLKGCL LSEKGKQHAE ILFLDKIRSM
ELSQVIITCY LTWSPCPNCA WQLAAFKRDR PDLILHIYTS RLYFHWKRPF QKGLCSLWQS
GILVDVMDLP QFTDCWTNFV NPKRPFWPWK GLEIISRRTQ RRLHRIKESW GLQDLVNDFG
NLQLGPPMS
//
