Q96AK3 (ABC3D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable DNA dC->dU-editing enzyme APOBEC-3D
EC=3.5.4.-

Gene names

Name:

APOBEC3D

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	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable DNA cytidine deaminase involved in foreign DNA clearance. May provide cellular innate resistance to a specific panel of genetic invaders including endogenous retroelements and a subset of viruses. Ref.4 Ref.5
Catalytic activity	Cytidine + H2O = uridine + NH3.
Cofactor	Zinc By similarity.
Tissue specificity	Expressed in lymphoid organs. Also detected in non-lymphoid tissues including lung. Ref.6
Miscellaneous	It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of transposition Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 386	386	Probable DNA dC->dU-editing enzyme APOBEC-3D		PRO_0000171756
Sites
	Active site	264	1	Proton donor By similarity
	Metal binding	78	1	Zinc By similarity
	Metal binding	109	1	Zinc By similarity
	Metal binding	112	1	Zinc By similarity
	Metal binding	262	1	Zinc By similarity
	Metal binding	293	1	Zinc By similarity
	Metal binding	296	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q96AK3 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 94C7253BDCC85B22	FASTA	386	46,598
	10 20 30 40 50 60 MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGPVL 70 80 90 100 110 120 PKRQSNHRQE VYFRFENHAE MCFLSWFCGN RLPANRRFQI TWFVSWNPCL PCVVKVTKFL 130 140 150 160 170 180 AEHPNVTLTI SAARLYYYRD RDWRWVLLRL HKAGARVKIM DYEDFAYCWE NFVCNEGQPF 190 200 210 220 230 240 MPWYKFDDNY ASLHRTLKEI LRNPMEAMYP HIFYFHFKNL LKACGRNESW LCFTMEVTKH 250 260 270 280 290 300 HSAVFRKRGV FRNQVDPETH CHAERCFLSW FCDDILSPNT NYEVTWYTSW SPCPECAGEV 310 320 330 340 350 360 AEFLARHSNV NLTIFTARLC YFWDTDYQEG LCSLSQEGAS VKIMGYKDFV SCWKNFVYSD 370 380 DEPFKPWKGL QTNFRLLKRR LREILQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22." Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., Navaratnam N. Genomics 79:285-296(2002) [PubMed: 11863358] [Abstract] Cited for: GENE FAMILY ORGANIZATION.
[3]	"Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business." Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C. Trends Genet. 19:207-216(2003) [PubMed: 12683974] [Abstract] Cited for: REVIEW ON APOBEC FAMILIES.
[4]	"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif." Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., Muenk C., Nymark-McMahon H., Landau N.R. Cell 114:21-31(2003) [PubMed: 12859895] [Abstract] Cited for: FUNCTION IN HIV-1 INFECTIVITY.
[5]	"APOBEC3 proteins mediate the clearance of foreign DNA from human cells." Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S. Nat. Struct. Mol. Biol. 17:222-229(2010) [PubMed: 20062055] [Abstract] Cited for: FUNCTION IN RETROTRANSPOSITION.
[6]	"Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction." Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., Harris R.S. Nucleic Acids Res. 38:4274-4284(2010) [PubMed: 20308164] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL022318 Genomic DNA. Translation: CAI17899.1.
IPI	IPI00413447.
RefSeq	NP_689639.2. NM_152426.3.
UniGene	Hs.629775. Hs.658626.
3D structure databases
ProteinModelPortal	Q96AK3.
SMR	Q96AK3. Positions 11-386.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96AK3.
PTM databases
PhosphoSite	Q96AK3.
Polymorphism databases
DMDM	48474596.
Proteomic databases
PRIDE	Q96AK3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216099; ENSP00000216099; ENSG00000243811.
GeneID	140564.
KEGG	hsa:140564.
NMPDR	fig|9606.3.peg.21729.
UCSC	uc003awt.2. human.
Organism-specific databases
CTD	140564.
GeneCards	GC22P039380.
HGNC	HGNC:17354. APOBEC3D.
MIM	609900. gene.
neXtProt	NX_Q96AK3.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00530000062933.
HOVERGEN	HBG050434.
InParanoid	Q96AK3.
OrthoDB	EOG480HX1.
PhylomeDB	Q96AK3.
Gene expression databases
ArrayExpress	Q96AK3.
Bgee	Q96AK3.
Genevestigator	Q96AK3.
GermOnline	ENSG00000198904. Homo sapiens.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR007904. APOBEC_C. IPR013158. APOBEC_N. IPR016193. Cytidine_deaminase-like. [Graphical view]
Pfam	PF05240. APOBEC_C. 2 hits. PF08210. APOBEC_N. 2 hits. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 2 hits.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 2 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

ABC3D_HUMAN

Accession

Primary (citable) accession number: Q96AK3
Secondary accession number(s): Q5JZ91 , Q7Z2N2, Q7Z2N5, Q7Z2N6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.