[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN HIV-1 INFECTION INHIBITION. TISSUE=Kidney; DOI=10.1128/JVI.77.21.11398-11407.2003; PubMed=14557625 [NCBI, ExPASy, EBI, Israel, Japan] Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A., Strebel K.; "The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity."; J. Virol. 77:11398-11407(2003).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Hematopoietic stem cell; Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.; "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."; Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Teratocarcinoma; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan] Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.; "A genome annotation-driven approach to cloning the human ORFeome."; Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-186 AND GLU-275. SeattleSNPs program for genomic applications; Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The DNA sequence of human chromosome 22."; Nature 402:489-495(1999).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). TISSUE=Skin, and Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, SUBUNIT, RNA-BINDING, AND ZINC-BINDING. DOI=10.1006/geno.2002.6718; PubMed=11863358 [NCBI, ExPASy, EBI, Israel, Japan] Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., Navaratnam N.; "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22."; Genomics 79:285-296(2002).
[9]	TISSUE SPECIFICITY, AND FUNCTION IN HIV-1 INFECTION INHIBITION. TISSUE=T-cell lymphoma; DOI=10.1038/nature00939; PubMed=12167863 [NCBI, ExPASy, EBI, Israel, Japan] Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H.; "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein."; Nature 418:646-650(2002).
[10]	SUBCELLULAR LOCATION, FUNCTION IN DNA C TO U EDITING, AND MUTAGENESIS OF GLU-67; HIS-81; GLU-85; CYS-97; CYS-100; CYS-221; HIS-257; GLU-259; CYS-288; CYS-291 AND GLU-323. DOI=10.1038/nature01709; PubMed=12808466 [NCBI, ExPASy, EBI, Israel, Japan] Mangeat B., Turelli P., Caron G., Friedli M., Perrin L., Trono D.; "Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts."; Nature 424:99-103(2003).
[11]	FUNCTION IN DNA C TO U EDITING, AND MLV INFECTION INHIBITION. DOI=10.1016/S0092-8674(03)00423-9; PubMed=12809610 [NCBI, ExPASy, EBI, Israel, Japan] Harris R.S., Bishop K.N., Sheehy A.M., Craig H.M., Petersen-Mahrt S.K., Watt I.N., Neuberger M.S., Malim M.H.; "DNA deamination mediates innate immunity to retroviral infection."; Cell 113:803-809(2003).
[12]	FUNCTION IN DNA C TO U EDITING, AND MUTAGENESIS OF HIS-81; CYS-97; CYS-100; HIS-257; CYS-288 AND CYS-291. DOI=10.1038/nature01707; PubMed=12808465 [NCBI, ExPASy, EBI, Israel, Japan] Zhang H., Yang B., Pomerantz R.J., Zhang C., Arunachalam S.C., Gao L.; "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA."; Nature 424:94-98(2003).
[13]	FUNCTION IN DNA C TO U EDITING, AND INTERACTION WITH VIF. DOI=10.1016/S0092-8674(03)00515-4; PubMed=12859895 [NCBI, ExPASy, EBI, Israel, Japan] Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.; "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif."; Cell 114:21-31(2003).
[14]	FUNCTION IN DNA C TO U EDITING, INFECTION REGULATION OF HIV-1, AND MUTAGENESIS OF GLU-67; CYS-100; GLU-259 AND CYS-291. TISSUE=T-cell lymphoma; DOI=10.1074/jbc.C300376200; PubMed=12970355 [NCBI, ExPASy, EBI, Israel, Japan] Shindo K., Takaori-Kondo A., Kobayashi M., Abudu A., Fukunaga K., Uchiyama T.; "The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity."; J. Biol. Chem. 278:44412-44416(2003).
[15]	INTERACTION WITH VIF, PROTEASOME MEDIATED DEGRADATION, AND TRANSLATION INHIBITION. DOI=10.1016/S1097-2765(03)00353-8; PubMed=14527406 [NCBI, ExPASy, EBI, Israel, Japan] Stopak K., de Noronha C., Yonemoto W., Greene W.C.; "HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability."; Mol. Cell 12:591-601(2003).
[16]	INTERACTION WITH VIF, AND UBIQUITINATION. DOI=10.1038/nm946; PubMed=14528301 [NCBI, ExPASy, EBI, Israel, Japan] Marin M., Rose K.M., Kozak S.L., Kabat D.; "HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation."; Nat. Med. 9:1398-1403(2003).
[17]	FUNCTION IN DNA C TO U EDITING, AND UBIQUITINATION. DOI=10.1038/nm945; PubMed=14528300 [NCBI, ExPASy, EBI, Israel, Japan] Sheehy A.M., Gaddis N.C., Malim M.H.; "The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif."; Nat. Med. 9:1404-1407(2003).
[18]	REVIEW ON APOBEC FAMILY. DOI=10.1016/S0168-9525(03)00054-4; PubMed=12683974 [NCBI, ExPASy, EBI, Israel, Japan] Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.; "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business."; Trends Genet. 19:207-216(2003).
[19]	REVIEW. DOI=10.1016/j.molmed.2003.08.008; PubMed=14557052 [NCBI, ExPASy, EBI, Israel, Japan] Vartanian J.P., Sommer P., Wain-Hobson S.; "Death and the retrovirus."; Trends Mol. Med. 9:409-413(2003).
[20]	REVIEW. DOI=10.1016/j.ymthe.2003.08.010; PubMed=14565218 [NCBI, ExPASy, EBI, Israel, Japan] Cullen B.R.; "HIV-1 Vif: counteracting innate antiretroviral defenses."; Mol. Ther. 8:525-527(2003).
[21]	MUTAGENESIS OF ASP-128. DOI=10.1073/pnas.0400830101; PubMed=15054139 [NCBI, ExPASy, EBI, Israel, Japan] Xu H., Svarovskaia E.S., Barr R., Zhang Y., Khan M.A., Strebel K., Pathak V.K.; "A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion."; Proc. Natl. Acad. Sci. U.S.A. 101:5652-5657(2004).
[22]	FUNCTION IN HBV INHIBITION. DOI=10.1126/science.1092066; PubMed=15031497 [NCBI, ExPASy, EBI, Israel, Japan] Turelli P., Mangeat B., Jost S., Vianin S., Trono D.; "Inhibition of hepatitis B virus replication by APOBEC3G."; Science 303:1829-1829(2004).

Comments

FUNCTION: DNA deaminase (cytidine deaminase) that mediates a form of innate resistance to retroviral infections (at least to HIV-1 infection) by triggering G-to-A hypermutation in the newly synthesized viral DNA. The replacements C-to-U in 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. Modification of both DNA strands is not excluded. This antiviral activity is neutralized by the virion infectivity factor (VIF), that prevents the incorporation of APOBEC3G into progeny HIV-1 virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome. APOBEC3G binds a variety of RNAs, but does not display detectable APOB, NF1 and NAT1 mRNA editing.
COFACTOR: Zinc.
SUBUNIT: Homodimer. Interacts with APOBEC3B, APOBEC3F and HIV-1 VIF in a species specific manner.
INTERACTION:
P12504:vif (xeno); NbExp=1; IntAct=EBI-717839, EBI-779991;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic. Small amount are found in the nucleus. During HIV-1 infection, virion-encapsidated in absence of HIV-1 VIF.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q9HC16-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9HC16-2
Note: May be due to a competing donor and acceptor splice sites and intron retentions. No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_009587, VSP_009590.

Name	3
Isoform ID	Q9HC16-3
Note: May be due to a competing donor splice site.
Features which should be applied to build the isoform sequence: VSP_009588, VSP_009589.

TISSUE SPECIFICITY: Expressed in spleen, testes, ovary and peripheral blood leukocytes and CD4+ lymphocytes. Also expressed in non-permissive peripheral blood mononuclear cells, and several tumor cell lines; no expression detected in permissive lymphoid and non-lymphoid cell lines.
PTM: Ubiquitinated in the presence of HIV-1 VIF. Association with VIF targets the protein for proteolysis by the ubiquitin-dependent proteasome pathway.
MISCELLANEOUS: Inhibits also the infectivity of retroviral particles only distantly related to HIV-1, such as the simian immunodeficiency virus (SIV), the equine infectious anemia virus (EIAV) and the murine leukemia virus (MLV).
MISCELLANEOUS: HIV-1 does not replicate productively in nonhuman primates with the exception of the chimpanzee. The primates APOBEC3G (rhesus macaque, chimpanzee and African green monkey) are active against HIV-1 without VIF. Only the chimpanzee APOBEC3G is inhibited by HIV-1 VIF.
MISCELLANEOUS: Accumulation of APOBEC3G induced non-lethal hypermutation could contribute to the genetic variation of primate lentiviral populations.
MISCELLANEOUS: It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.
SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.
SEQUENCE CAUTION:
- Sequence=CAB45274.1; Type=Erroneous gene model prediction;
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/apobec3g/";.
WEB RESOURCE: Name=Protein Spotlight; Note=Protein wars - Issue 45 of April 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt045.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF182420; AAG14956.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK022802; BAB14251.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456472; CAG30358.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ147772; AAZ38722.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022318; CAB45274.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078641; CAI21556.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022318; CAI21556.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022318; CAI17900.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078641; CAI17900.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024268; AAH24268.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061914; AAH61914.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_068594.1; -.

UniGene

Hs.659991

3D structure databases

PDB

2JYW; NMR; -; A=198-384.

[ExPASy / RCSB / EBI]

PDBsum

2JYW; -.

ModBase

Q9HC16.

Protein-protein interaction databases

IntAct

Q9HC16; -.

Enzyme and pathway databases

Reactome

REACT_6185; HIV Infection.

Organism-specific databases

H-InvDB

HIX0018289; -.
HIX0080287; -.

HGNC

HGNC:17357; APOBEC3G.

HPA001812; -.

607113; gene. [NCBI / EBI]

PharmGKB

PA24897; -.

GeneCards

Q9HC16.

Gene expression databases

ArrayExpress

Q9HC16; -.

CleanEx

HS_APOBEC3G; -.

GermOnline

ENSG00000128394; Homo sapiens.

Ontologies

GO:0030895;	Cellular component: apolipoprotein B mRNA editing enzyme complex (traceable author statement from HGNC).
GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004126;	Molecular function: cytidine deaminase activity (traceable author statement from HGNC).
GO:0042803;	Molecular function: protein homodimerization activity (non-traceable author statement from UniProtKB).
GO:0003723;	Molecular function: RNA binding (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0016553;	Biological process: base conversion or substitution editing (traceable author statement from HGNC).
GO:0045087;	Biological process: innate immune response (inferred from direct assay from HGNC).
GO:0045869;	Biological process: negative regulation of retroviral genome replication (inferred from direct assay from HGNC).
GO:0002230;	Biological process: positive regulation of defense response to virus by host (inferred from direct assay from HGNC).
GO:0006410;	Biological process: transcription, RNA-dependent (inferred from direct assay from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR007904; APOBEC_C.
IPR013158; APOBEC_N.
Graphical view of domain structure.

Pfam

PF05240; APOBEC_C; 2.
PF08210; APOBEC_N; 2.
Pfam graphical view of domain structure.

PROSITE

PS00903; CYT_DCMP_DEAMINASES; 1.

BLOCKS

Q9HC16.

Genome annotation databases

Ensembl

ENSG00000128394; Homo sapiens. [Contig view]

GeneID

60489; -.

KEGG

hsa:60489; -.

Phylogenomic databases

HOGENOM

Q9HC16; -.

HOVERGEN

Q9HC16; -.

Other

LinkHub

Q9HC16; -.

SOURCE

APOBEC3G; Homo sapiens.

ProtoNet

Q9HC16.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Antiviral defense; Cytoplasm; Host-virus interaction; Hydrolase; Metal-binding; Nucleus; Polymorphism; Ubl conjugation; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 384`	`384`	`DNA dC->dU-editing enzyme APOBEC-3G.`	`PRO_0000171761`
`ACT_SITE`	`259 259`		`Proton donor (By similarity).`
`METAL`	`65 65`		`Zinc (By similarity).`
`METAL`	`97 97`		`Zinc (By similarity).`
`METAL`	`100 100`		`Zinc (By similarity).`
`METAL`	`257 257`		`Zinc (By similarity).`
`METAL`	`288 288`		`Zinc (By similarity).`
`METAL`	`291 291`		`Zinc (By similarity).`
`VAR_SEQ`	`1 67`		`Missing (in isoform 2).`	`VSP_009587`
`VAR_SEQ`	`58 79`		`VYSELKYHPEMRFFHWFSKWRK -> VPPGLQSLCRQELSQLGKQTTH (in isoform 3).`	`VSP_009588`
`VAR_SEQ`	`80 384`		`Missing (in isoform 3).`	`VSP_009589`
`VAR_SEQ`	`195 384`		`Missing (in isoform 2).`	`VSP_009590`
`VARIANT`	`186 186`	`1`	`H -> R (in dbSNP:rs8177832 [NCBI]).`	`VAR_017837`
`VARIANT`	`275 275`	`1`	`Q -> E (in dbSNP:rs17496046 [NCBI]).`	`VAR_025060`
`MUTAGEN`	`67 67`		`E->Q: Decreases cytidine deaminase activity.`
`MUTAGEN`	`81 81`		`H->A: Decreases cytidine deaminase activity.`
`MUTAGEN`	`85 85`		`E->Q: Does not decrease cytidine deaminase activity.`
`MUTAGEN`	`97 97`		`C->A: Decreases cytidine deaminase activity.`
`MUTAGEN`	`100 100`		`C->A,S: Decreases cytidine deaminase activity.`
`MUTAGEN`	`128 128`		`D->K: Complete loss of VIF-induced degradation.`
`MUTAGEN`	`221 221`		`C->S: Does not decrease cytidine deaminase activity.`
`MUTAGEN`	`257 257`		`H->A: Decreases cytidine deaminase activity.`
`MUTAGEN`	`259 259`		`E->Q: Decreases cytidine deaminase activity.`
`MUTAGEN`	`288 288`		`C->A: Decreases cytidine deaminase activity.`
`MUTAGEN`	`291 291`		`C->A,S: Decreases cytidine deaminase activity.`
`MUTAGEN`	`323 323`		`E->Q: Does not decrease cytidine deaminase activity.`
`CONFLICT`	`162 162`		`S -> N (in Ref. 1).`
`CONFLICT`	`370 370`		`D -> Y (in Ref. 1).`

Sequence information

Length: 384 AA [This is the length of the unprocessed precursor]

Molecular weight: 46408 Da [This is the MW of the unprocessed precursor]

CRC64: 60525DC3B7D903D6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYS 

        70         80         90        100        110        120 
ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRDMATFLAE DPKVTLTIFV 

       130        140        150        160        170        180 
ARLYYFWDPD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK 

       190        200        210        220        230        240 
YYILLHIMLG EILRHSMDPP TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG 

       250        260        270        280        290        300 
FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS 

       310        320        330        340        350        360 
KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VDHQGCPFQP 

       370        380 
WDGLDEHSQD LSGRLRAILQ NQEN

Q9HC16 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools

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