ABEC4_MOUSE
ID ABEC4_MOUSE Reviewed; 374 AA.
AC Q497M3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 96.
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 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-350.
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).
RN [3]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=16082223; DOI=10.4161/cc.4.9.1994;
RA Rogozin I.B., Basu M.K., Jordan I.K., Pavlov Y.I., Koonin E.V.;
RT "APOBEC4, a new member of the AID/APOBEC family of polynucleotide
RT (deoxy)cytidine deaminases predicted by computational analysis.";
RL Cell Cycle 4:1281-1285(2005).
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 -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC {ECO:0000269|PubMed:16082223}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00466.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK017014; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC100465; AAI00466.1; ALT_SEQ; mRNA.
DR CCDS; CCDS35738.1; -.
DR AlphaFoldDB; Q497M3; -.
DR STRING; 10090.ENSMUSP00000069723; -.
DR PhosphoSitePlus; Q497M3; -.
DR PaxDb; Q497M3; -.
DR PRIDE; Q497M3; -.
DR ProteomicsDB; 285905; -.
DR Antibodypedia; 2817; 267 antibodies from 28 providers.
DR Ensembl; ENSMUST00000068875; ENSMUSP00000069723; ENSMUSG00000055547.
DR UCSC; uc007czi.1; mouse.
DR MGI; MGI:1918531; Apobec4.
DR VEuPathDB; HostDB:ENSMUSG00000055547; -.
DR eggNOG; ENOG502QQXT; Eukaryota.
DR GeneTree; ENSGT00390000014243; -.
DR HOGENOM; CLU_832944_0_0_1; -.
DR InParanoid; Q497M3; -.
DR OMA; VRHLNMP; -.
DR OrthoDB; 1149880at2759; -.
DR PhylomeDB; Q497M3; -.
DR TreeFam; TF338173; -.
DR Reactome; R-MMU-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-MMU-75094; Formation of the Editosome.
DR PRO; PR:Q497M3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q497M3; protein.
DR Bgee; ENSMUSG00000055547; Expressed in seminiferous tubule of testis and 5 other tissues.
DR Genevisible; Q497M3; MM.
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..374
FT /note="Putative C->U-editing enzyme APOBEC-4"
FT /id="PRO_0000239357"
FT DOMAIN 60..176
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 259..280
FT /note="Disordered"
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 374 AA; 42721 MW; 43AC40F70049F9CD CRC64;
MEPLYEEILT QGGTIVKPYY WLSLSLGCTN CPYHIRTGEE ARVPYTEFHQ TFGFPWSTYP
QTKHLTFYEL RSSSKNLIQK GLASNCTGSH NHPEAMLFEK NGYLDAVIFH NSNIRHIILY
SNNSPCNEAK HCCISKMYNF LMNYPEVTLS VFFSQLYHTE KQFPTSAWNR KALQSLASLW
PQVTLSPICG GLWHAILEKF VSNISGSTVP QPFIAGRILA DRYNTYEINS IIAAKPYFTD
GLLSRQKENQ NREAWAAFEK HPLGSAAPAQ RQPTRGQDPR TPAVLMLVSN RDLPPIHVGS
TPQKPRTVVR HLNMLQLSSF KVKDVKKPPS GRPVEEVEVM KESARSQKAN KKNRSQWKKQ
TLVIKPRICR LLER
