Reviewed, UniProtKB/Swiss-Prot P41238 (ABEC1_HUMAN)

Names and origin

Protein names

Recommended name:
    C->U-editing enzyme APOBEC-1
    EC=3.5.4.-
Alternative name(s):
    Apolipoprotein B mRNA-editing enzyme 1
    HEPR

Gene names

Name:

APOBEC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalytic component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the APOB mRNA. Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA.
Cofactor	Zinc By similarity.
Subunit structure	Homodimer. Part of the apolipoprotein B mRNA editing complex with APC. Found in a complex with CUGBP2 and A1CF. APC binds to APOB mRNA and is probably responsible for docking APOBEC1 to the mRNA. Interacts with HNRPAB and SYNCRIP.
Tissue specificity	Expressed exclusively in the small intestine.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Biological process	mRNA processing
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	lipid metabolic process Ref.2 Traceable author statement. Source: ProtInc mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Traceable author statement. Source: ProtInc cytidine deaminase activity Traceable author statement. Source: ProtInc zinc ion binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 236	236	C->U-editing enzyme APOBEC-1		PRO_0000171742
Regions
	Compositional bias	180 – 193	14	Leu-rich
Sites
	Active site	63	1	Proton donor By similarity
	Metal binding	61	1	Zinc; catalytic By similarity
	Metal binding	93	1	Zinc; catalytic By similarity
	Metal binding	96	1	Zinc; catalytic By similarity
Natural variations
	Natural variant	80	1	M → I: dbSNP rs2302515.		VAR_013779
Experimental info
	Sequence conflict	53	1	S → T Ref.1 Ref.5
	Sequence conflict	83	1	S → T Ref.1 Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P41238-1 [UniParc]. Last modified March 6, 2007. Version 3. Checksum: 28466B43F7FD82F7	FASTA	236	28,192
	10 20 30 40 50 60 MTSEKGPSTG DPTLRRRIEP WEFDVFYDPR ELRKEACLLY EIKWGMSRKI WRSSGKNTTN 70 80 90 100 110 120 HVEVNFIKKF TSERDFHPSM SCSITWFLSW SPCWECSQAI REFLSRHPGV TLVIYVARLF 130 140 150 160 170 180 WHMDQQNRQG LRDLVNSGVT IQIMRASEYY HCWRNFVNYP PGDEAHWPQY PPLWMMLYAL 190 200 210 220 230 ELHCIILSLP PCLKISRRWQ NHLTFFRLHL QNCHYQTIPP HILLATGLIH PSVAWR

References

[1]	"Molecular cloning of a human small intestinal apolipoprotein B mRNA editing protein." Hadjiagapiou C., Giannoni F., Funahashi T., Skarosi S.F., Davidson N.O. Nucleic Acids Res. 22:1874-1879(1994) [PubMed: 8208612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-80. Tissue: Intestine.
[2]	"Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene." Lau P.P., Zhu H.-J., Baldini A., Charnsangavej C., Chan L. Proc. Natl. Acad. Sci. U.S.A. 91:8522-8526(1994) [PubMed: 8078915] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT ILE-80. Tissue: Small intestine.
[3]	"Characterization of the human apobec-1 gene: expression in gastrointestinal tissues determined by alternative splicing with production of a novel truncated peptide." Hirano K., Min J., Funahashi T., Baunoch D.A., Davidson N.O. J. Lipid Res. 38:847-859(1997) [PubMed: 9186903] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-80. Tissue: Osteosarcoma.
[4]	"Human apolipoprotein B RNA editing deaminase gene (APOBEC1)." Fujino T., Navaratnam N., Scott J. Genomics 47:266-275(1998) [PubMed: 9479499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-80. Tissue: Peripheral blood leukocyte.
[5]	"A novel mutation in exon 3 of the human apoB editing protein gene." Hong S.H., Kim J.Q., Lee C.C. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-147.
[6]	"Cloning of an Apobec-1-binding protein that also interacts with apolipoprotein B mRNA and evidence for its involvement in RNA editing." Lau P.P., Zhu H.J., Nakamuta M., Chan L. J. Biol. Chem. 272:1452-1455(1997) [PubMed: 8999813] [Abstract] Cited for: INTERACTION WITH HNRPAB.
[7]	"Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex." Lellek H., Kirsten R., Diehl I., Apostel F., Buck F., Greeve J. J. Biol. Chem. 275:19848-19856(2000) [PubMed: 10781591] [Abstract] Cited for: INTERACTION WITH AFC.
[8]	"Molecular cloning of APOBEC-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA." Mehta A., Kinter M.T., Sherman N.E., Driscoll D.M. Mol. Cell. Biol. 20:1846-1854(2000) [PubMed: 10669759] [Abstract] Cited for: INTERACTION WITH AFC.
[9]	"Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome." Lau P.P., Chang B.-H., Chan L. Biochem. Biophys. Res. Commun. 282:977-983(2001) [PubMed: 11352648] [Abstract] Cited for: INTERACTION WITH SYNCRIP.
[10]	"Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor." Anant S., Henderson J.O., Mukhopadhyay D., Navaratnam N., Kennedy S., Min J., Davidson N.O. J. Biol. Chem. 276:47338-47351(2001) [PubMed: 11577082] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CUGBP2 AND A1CF.
[11]	"C-->U editing of neurofibromatosis 1 mRNA occurs in tumors that express both the type II transcript and apobec-1, the catalytic subunit of the apolipoprotein B mRNA-editing enzyme." Mukhopadhyay D., Anant S., Lee R.M., Kennedy S., Viskochil D., Davidson N.O. Am. J. Hum. Genet. 70:38-50(2002) [PubMed: 11727199] [Abstract] Cited for: FUNCTION IN NF1 EDITING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L25877 mRNA. Translation: AAA86766.1. L26234 mRNA. Translation: AAA64230.1. AB009426 Genomic DNA. Translation: BAA23882.1. U72891 mRNA. Translation: AAD00185.1. U78720 mRNA. Translation: AAD10701.1.
PIR	I59323.
RefSeq	NP_001635.2.
UniGene	Hs.560
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P41238.
Genome annotation databases
Ensembl	ENSG00000111701. Homo sapiens. [Contig view]
GeneID	339.
KEGG	hsa:339.
Organism-specific databases
H-InvDB	HIX0036858.
HGNC	HGNC:604. APOBEC1.
MIM	600130. gene.
PharmGKB	PA24889.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P41238.
HOVERGEN	P41238.
Enzyme and pathway databases
Reactome	REACT_1675. mRNA Processing.
Gene expression databases
ArrayExpress	P41238.
CleanEx	HS_APOBEC1.
GermOnline	ENSG00000111701. Homo sapiens.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR007904. APOBEC_C. IPR013158. APOBEC_N. [Graphical view]
Pfam	PF05240. APOBEC_C. 1 hit. PF08210. APOBEC_N. 1 hit. [Graphical view]
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	1403.
SOURCE	Search...

Entry information

Entry name

ABEC1_HUMAN

Accession

Primary (citable) accession number: P41238
Secondary accession number(s): Q9UE64, Q9UM71

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	March 6, 2007
Last modified:	November 25, 2008
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)