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Q8IUX4 (ABC3F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA dC->dU-editing enzyme APOBEC-3F

EC=3.5.4.-
Alternative name(s):
Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F
Gene names
Name:APOBEC3F
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Host cellular restriction factor that may have antiviral activities against exogenous and endogenous viruses, as well as retrotransposons. After being packaged into HIV-1 virions, blocks productive infection by massively editing dC residues to dU on the DNA minus strand during reverse transcription. The editing of the minus strand DNA of HIV-1 during reverse transcription leads to G-to-A transitions in the plus strand. The inhibition of viral replication is either due to the degradation of the minus strand before its integration or to the lethality of the hypermutations. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. Ref.7 Ref.8 Ref.9 Ref.11

Catalytic activity

Cytidine + H2O = uridine + NH3.

Cofactor

Zinc By similarity.

Subunit structure

Forms heterodimers with APOBEC3G. Binds HIV-1 Vif. In the absence of Vif protein, specifically packaged into HIV-1 virions.

Subcellular location

Cytoplasm Ref.8.

Tissue specificity

Widely expressed. Highly expressed in ovary. Ref.5 Ref.7 Ref.10

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IUX4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8IUX4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     58-79: VYSQPEHHAEMCFLSWFCGNQL → VPPGLQSLCRQELSQLGKQTTH
     80-373: Missing.
Note: May be due to a competing donor splice site. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 373373DNA dC->dU-editing enzyme APOBEC-3F
PRO_0000171757

Sites

Active site2511Proton donor By similarity
Metal binding651Zinc By similarity
Metal binding961Zinc By similarity
Metal binding991Zinc By similarity

Natural variations

Alternative sequence58 – 7922VYSQP…CGNQL → VPPGLQSLCRQELSQLGKQT TH in isoform 2.
VSP_009803
Alternative sequence80 – 373294Missing in isoform 2.
VSP_009804
Natural variant481R → P. Ref.4
Corresponds to variant rs35053197 [ dbSNP | Ensembl ].
VAR_038355
Natural variant611Q → L.
Corresponds to variant rs2076109 [ dbSNP | Ensembl ].
VAR_018145
Natural variant971P → L.
Corresponds to variant rs2076110 [ dbSNP | Ensembl ].
VAR_018146
Natural variant1081A → S. Ref.4
Corresponds to variant rs2020390 [ dbSNP | Ensembl ].
VAR_018147
Natural variant1781A → T. Ref.1
Corresponds to variant rs34182094 [ dbSNP | Ensembl ].
VAR_025058
Natural variant2311V → I. Ref.1
Corresponds to variant rs2076101 [ dbSNP | Ensembl ].
VAR_018148
Natural variant3071Y → C. Ref.1
Corresponds to variant rs12157816 [ dbSNP | Ensembl ].
VAR_025059

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 3.
Checksum: AF1A0E13830695F4

FASTA37345,020
        10         20         30         40         50         60 
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPRLD AKIFRGQVYS 

        70         80         90        100        110        120 
QPEHHAEMCF LSWFCGNQLP AYKCFQITWF VSWTPCPDCV AKLAEFLAEH PNVTLTISAA 

       130        140        150        160        170        180 
RLYYYWERDY RRALCRLSQA GARVKIMDDE EFAYCWENFV YSEGQPFMPW YKFDDNYAFL 

       190        200        210        220        230        240 
HRTLKEILRN PMEAMYPHIF YFHFKNLRKA YGRNESWLCF TMEVVKHHSP VSWKRGVFRN 

       250        260        270        280        290        300 
QVDPETHCHA ERCFLSWFCD DILSPNTNYE VTWYTSWSPC PECAGEVAEF LARHSNVNLT 

       310        320        330        340        350        360 
IFTARLYYFW DTDYQEGLRS LSQEGASVEI MGYKDFKYCW ENFVYNDDEP FKPWKGLKYN 

       370 
FLFLDSKLQE ILE 

« Hide

Isoform 2 [UniParc].

Checksum: 03ABEACA44AB0748
Show »

FASTA799,445

References

« Hide 'large scale' references
[1]SeattleSNPs variation discovery resource
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-178; ILE-231 AND CYS-307.
[2]"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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-48 AND SER-108.
Tissue: Pancreas, Spleen and Uterus.
[5]"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, TISSUE SPECIFICITY.
[6]"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.
[7]"A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins."
Wiegand H.L., Doehle B.P., Bogerd H.P., Cullen B.R.
EMBO J. 23:2451-2458(2004) [PubMed: 15152192] [Abstract]
Cited for: FUNCTION IN HIV-1 INFECTIVITY, TISSUE SPECIFICITY.
[8]"APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons."
Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., Landau N.R., Weitzman M.D.
Curr. Biol. 16:480-485(2006) [PubMed: 16527742] [Abstract]
Cited for: FUNCTION IN RETROTRANSPOSITION, SUBCELLULAR LOCATION.
[9]"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.
[10]"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.
[11]"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain."
Guo J.U., Su Y., Zhong C., Ming G.L., Song H.
Cell 145:423-434(2011) [PubMed: 21496894] [Abstract]
Cited for: FUNCTION IN DNA DEMETHYLATION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ146365 Genomic DNA. Translation: AAZ38720.1.
AL022318 Genomic DNA. Translation: CAQ09853.1.
CH471095 Genomic DNA. Translation: EAW60289.1.
BC038808 mRNA. Translation: AAH38808.1.
BC061914 mRNA. Translation: AAH61914.1.
IPIIPI00409765.
IPI00477614.
RefSeqNP_660341.2. NM_145298.5.
UniGeneHs.659809.
Hs.660143.

3D structure databases

ProteinModelPortalQ8IUX4.
SMRQ8IUX4. Positions 10-190, 193-373.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8IUX4.

Polymorphism databases

DMDM161784334.

Proteomic databases

PRIDEQ8IUX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308521; ENSP00000309749; ENSG00000128394.
GeneID200316.
KEGGhsa:200316.
NMPDRfig|9606.3.peg.21730.
UCSCuc003aww.1. human.

Organism-specific databases

CTD200316.
GeneCardsGC22P039436.
HGNCHGNC:17356. APOBEC3F.
MIM608993. gene.
neXtProtNX_Q8IUX4.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00530000062933.
HOVERGENHBG050434.
InParanoidQ8IUX4.
OrthoDBEOG480HX1.

Enzyme and pathway databases

BRENDA3.5.4.5. 2681.

Gene expression databases

ArrayExpressQ8IUX4.
BgeeQ8IUX4.
CleanExHS_APOBEC3F.
GenevestigatorQ8IUX4.
GermOnlineENSG00000128394. Homo sapiens.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR007904. APOBEC_C.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
KOK01500.
PfamPF05240. APOBEC_C. 2 hits.
PF08210. APOBEC_N. 2 hits.
[Graphical view]
SUPFAMSSF53927. Cytidine_deaminase-like. 2 hits.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio89891.
SOURCESearch...

Entry information

Entry nameABC3F_HUMAN
AccessionPrimary (citable) accession number: Q8IUX4
Secondary accession number(s): B0QYD4 expand/collapse secondary AC list , Q45F03, Q7Z2N2, Q7Z2N5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families