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Q0ED31

- Q0ED31_9HIV1

UniProt

Q0ED31 - Q0ED31_9HIV1

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Protein
Envelope glycoprotein gp160
Gene
env
Organism
Human immunodeficiency virus 1
Status
Unreviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

The envelope glyprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface By similarity.UniRule annotationSAAS annotations
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves By similarity.SAAS annotations

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. evasion or tolerance by virus of host immune response Source: UniProtKB-KW
  3. membrane fusion involved in viral entry into host cell Source: UniProtKB-KW
  4. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ApoptosisSAAS annotations, Fusion of virus membrane with host membraneSAAS annotations, Host-virus interaction, Viral attachment to host cellUniRule annotationSAAS annotations, Viral immunoevasionUniRule annotation, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein gp160UniRule annotation
Gene namesi
Name:envImported
OrganismiHuman immunodeficiency virus 1Imported
Taxonomic identifieri11676 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

GO - Cellular componenti

  1. host cell endosome membrane Source: UniProtKB-SubCell
  2. host cell plasma membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. viral envelope Source: UniProtKB-KW
  5. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneSAAS annotations, Host endosomeSAAS annotations, Host membrane, Membrane, Viral envelope proteinUniRule annotationSAAS annotations, Virion

Pathology & Biotechi

Keywords - Diseasei

AIDSUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...)Imported
Glycosylationi160 – 1601N-linked (GlcNAc...)Imported
Glycosylationi188 – 1881N-linked (GlcNAc...)Imported
Glycosylationi236 – 2361N-linked (GlcNAc...)Imported
Glycosylationi243 – 2431N-linked (GlcNAc...)Imported
Glycosylationi264 – 2641N-linked (GlcNAc...)Imported
Glycosylationi278 – 2781N-linked (GlcNAc...)Imported
Glycosylationi291 – 2911N-linked (GlcNAc...)Imported
Glycosylationi297 – 2971N-linked (GlcNAc...)Imported
Glycosylationi335 – 3351N-linked (GlcNAc...)Imported
Glycosylationi356 – 3561N-linked (GlcNAc...)Imported
Glycosylationi386 – 3861N-linked (GlcNAc...)Imported
Glycosylationi392 – 3921N-linked (GlcNAc...)Imported
Glycosylationi442 – 4421N-linked (GlcNAc...)Imported

Keywords - PTMi

Cleavage on pair of basic residuesUniRule annotation, Disulfide bondSAAS annotations

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NGBX-ray2.68A/D/G/I201-303[»]
A/D/G/I325-486[»]
A/D/G/I43-122[»]
3SE8X-ray1.90G43-486[»]
3SE9X-ray2.00G43-486[»]
3TGTX-ray1.90A43-486[»]
3U7YX-ray2.45G201-303[»]
G325-486[»]
G43-122[»]
4DKOX-ray1.98A/C43-486[»]
4DKPX-ray1.80A/C43-486[»]
4DKQX-ray1.89A43-486[»]
4DKRX-ray1.80A/C43-486[»]
4DKUX-ray2.49A/B201-303[»]
A/B325-486[»]
A/B43-122[»]
4DKVX-ray2.18A/B201-303[»]
A/B325-486[»]
A/B43-122[»]
4DVSX-ray2.10A/B201-303[»]
A/B325-486[»]
A/B43-122[»]
4DVTX-ray2.40A/B201-341[»]
A/B457-486[»]
A/B88-122[»]
4DVVX-ray1.94A/B201-433[»]
A/B325-486[»]
A/B43-122[»]
4DVWX-ray2.20A/B201-303[»]
A/B325-486[»]
A/B43-122[»]
4DVXX-ray2.40A/B201-303[»]
A/B325-486[»]
A/B43-122[»]
4H8WX-ray1.85G43-486[»]
4I54X-ray2.50A/B43-486[»]
4JB9X-ray2.60G43-486[»]
4JDTX-ray3.26G43-486[»]
4JKPX-ray2.82G43-486[»]
4JPVX-ray2.83G43-486[»]
4JPWX-ray2.90G43-486[»]
4LSPX-ray2.15G43-486[»]
4LSQX-ray2.25G43-486[»]
4LSRX-ray2.28G43-486[»]
4LSUX-ray2.30G43-486[»]
4P9HX-ray3.00G201-303[»]
G325-486[»]
G43-122[»]

Miscellaneous databases

EvolutionaryTraceiQ0ED31.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotations

Family and domain databases

Gene3Di2.170.40.20. 2 hits.
InterProiIPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]
PfamiPF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]
SUPFAMiSSF56502. SSF56502. 2 hits.

Sequencei

Sequence statusi: Complete.

Q0ED31-1 [UniParc]FASTAAdd to Basket

« Hide

MRVKETQMNW PNLWKWGTLI LGLVIICSAS DNLWVTVYYG VPVWKDADTT    50
LFCASDAKAH ETEVHNVWAT HACVPTDPNP QEIHLENVTE NFNMWKNNMV 100
EQMQEDVISL WDQSLQPCVK LTPLCVTLHC TTAKLTNVTN ITNVPNIGNI 150
TDEVRNCSFN MTTEIRDKKQ KVHALFYKLD IVQIEDKNDS SKYRLINCNT 200
SVIKQACPKI SFDPIPIHYC TPAGYVILKC NDKNFNGTGP CKNVSSVQCT 250
HGIKPVVSTQ LLLNGSLAEE EIIIRSENLT NNAKTIIVHL NKSVEINCTR 300
PSNNMRTSMR IGPGQVFYRT GSITGDIRKA YCEINGTKWN KVLKQVTEKL 350
KEHFNNKTII FQPPSGGDLE ITMHHFNCRG EFFYCNTTQL FNNTCIGNET 400
MKGCNGTITL PCKIKQIINM WQGTGQAMYA PPIDGKINCV SNITGILLTR 450
DGGANNTSNE TFRPGGGNIK DNWRSELYKY KVVQIEPLGI APTRAKRRVV 500
EREKRAVGIG AMIFGFLGAA GSTMGAASIT LTVQARQLLS GIVQQQSNLL 550
RAIEAQQHLL QLTVWGIKQL QARVLAVERY LKDQKFLGLW GCSGKIICTT 600
AVPWNSTWSN KSFEEIWNNM TWIEWEREIS NYTNQIYEIL TESQNQQDRN 650
EKDLLELDKW ASLWNWFDIT NWLWYIKIFI MIVGGLIGLR IIFAVLSIVN 700
RVRQGYSPLS FQTPIHHQRE PDRPERIEEG GGEQGRDRSV RLVSGFLSLA 750
WDDLRSLCLF SYHRLRDFIL IATRTVELLG HSSLKGLRRG WEGLKYLGNL 800
LLYWGQELKI SAISLLNTTA IAVAGWTDRV IEVAQGAWRA ILHIPRRIRQ 850
GLERTLL 857
Length:857
Mass (Da):97,310
Last modified:October 17, 2006 - v1
Checksum:iAA83C4FF189CCD0E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB253424 Genomic DNA. Translation: BAF31367.1.
AB253425 Genomic DNA. Translation: BAF31376.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB253424 Genomic DNA. Translation: BAF31367.1 .
AB253425 Genomic DNA. Translation: BAF31376.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NGB X-ray 2.68 A/D/G/I 201-303 [» ]
A/D/G/I 325-486 [» ]
A/D/G/I 43-122 [» ]
3SE8 X-ray 1.90 G 43-486 [» ]
3SE9 X-ray 2.00 G 43-486 [» ]
3TGT X-ray 1.90 A 43-486 [» ]
3U7Y X-ray 2.45 G 201-303 [» ]
G 325-486 [» ]
G 43-122 [» ]
4DKO X-ray 1.98 A/C 43-486 [» ]
4DKP X-ray 1.80 A/C 43-486 [» ]
4DKQ X-ray 1.89 A 43-486 [» ]
4DKR X-ray 1.80 A/C 43-486 [» ]
4DKU X-ray 2.49 A/B 201-303 [» ]
A/B 325-486 [» ]
A/B 43-122 [» ]
4DKV X-ray 2.18 A/B 201-303 [» ]
A/B 325-486 [» ]
A/B 43-122 [» ]
4DVS X-ray 2.10 A/B 201-303 [» ]
A/B 325-486 [» ]
A/B 43-122 [» ]
4DVT X-ray 2.40 A/B 201-341 [» ]
A/B 457-486 [» ]
A/B 88-122 [» ]
4DVV X-ray 1.94 A/B 201-433 [» ]
A/B 325-486 [» ]
A/B 43-122 [» ]
4DVW X-ray 2.20 A/B 201-303 [» ]
A/B 325-486 [» ]
A/B 43-122 [» ]
4DVX X-ray 2.40 A/B 201-303 [» ]
A/B 325-486 [» ]
A/B 43-122 [» ]
4H8W X-ray 1.85 G 43-486 [» ]
4I54 X-ray 2.50 A/B 43-486 [» ]
4JB9 X-ray 2.60 G 43-486 [» ]
4JDT X-ray 3.26 G 43-486 [» ]
4JKP X-ray 2.82 G 43-486 [» ]
4JPV X-ray 2.83 G 43-486 [» ]
4JPW X-ray 2.90 G 43-486 [» ]
4LSP X-ray 2.15 G 43-486 [» ]
4LSQ X-ray 2.25 G 43-486 [» ]
4LSR X-ray 2.28 G 43-486 [» ]
4LSU X-ray 2.30 G 43-486 [» ]
4P9H X-ray 3.00 G 201-303 [» ]
G 325-486 [» ]
G 43-122 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q0ED31.

Family and domain databases

Gene3Di 2.170.40.20. 2 hits.
InterProi IPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view ]
Pfami PF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view ]
SUPFAMi SSF56502. SSF56502. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "Construction and characterization of HIV-1 CRF01_AE infectious molecular clones."
    Sakamoto Y., Takekawa N., Tatsumi M.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 93TH057Imported.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 201-303; 325-486 AND 43-122, GLYCOSYLATION AT ASN-87; ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297; ASN-335; ASN-386; ASN-392 AND ASN-442.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-87; ASN-160 AND ASN-188.
  4. "Increasing the potency and breadth of an HIV antibody by using structure-based rational design."
    Diskin R., Scheid J.F., Marcovecchio P.M., West A.P., Klein F., Gao H., Gnanapragasam P.N., Abadir A., Seaman M.S., Nussenzweig M.C., Bjorkman P.J.
    Science 334:1289-1293(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 201-303; 325-486 AND 43-122, GLYCOSYLATION AT ASN-87; ASN-236; ASN-264; ASN-291; ASN-297 AND ASN-386.
  5. "Structure-based design, synthesis, and characterization of dual hotspot small-molecule HIV-1 entry inhibitors."
    LaLonde J.M., Kwon Y.D., Jones D.M., Sun A.W., Courter J.R., Soeta T., Kobayashi T., Princiotto A.M., Wu X., Schon A., Freire E., Kwong P.D., Mascola J.R., Sodroski J., Madani N., Smith A.B.
    J. Med. Chem. 55:4382-4396(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-160 AND ASN-188.
  6. "Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops."
    Kwon Y.D., Finzi A., Wu X., Dogo-Isonagie C., Lee L.K., Moore L.R., Schmidt S.D., Stuckey J., Yang Y., Zhou T., Zhu J., Vicic D.A., Debnath A.K., Shapiro L., Bewley C.A., Mascola J.R., Sodroski J.G., Kwong P.D.
    Proc. Natl. Acad. Sci. U.S.A. 109:5663-5668(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-160 AND ASN-188.
  7. "Antiviral activity and binding mode of next generation CD4-mimetics."
    Curreli F., Kwon Y.D., Zhang H, Kwong P.D., Debnath A.K.
    Submitted (FEB-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 201-303; 325-486 AND 43-122, GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297; ASN-335; ASN-356; ASN-386 AND ASN-442.
  8. "Structural definition of new transitional epitopes exposed by CD4 binding to HIV-1."
    Pazgier M., Acharya P., Tolbert W.D., Gohain N., Meginstu M., Wu X., Sajadi M., Robinson J., Kamin-Lewis R., Kwong P.D., Guan J., DeVico A.L., Lewis G.K.
    Submitted (SEP-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-188.
  9. "Structure-Based Design and Synthesis of an HIV-1 Entry Inhibitor Exploiting X-Ray and Thermodynamic Characterization."
    Lalonde J.M., Le-Khac M., Jones D.M., Courter J.R., Park J., Schon A., Princiotto A.M., Wu X., Mascola J.R., Freire E., Sodroski J., Madani N., Hendrickson W.A., Smith A.B.
    ACS Med. Chem. Lett. 4:338-343(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-160 AND ASN-188.
  10. "Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization."
    Klein F., Diskin R., Scheid J.F., Gaebler C., Mouquet H., Georgiev I.S., Pancera M., Zhou T., Incesu R.B., Fu B.Z., Gnanapragasam P.N., Oliveira T.Y., Seaman M.S., Kwong P.D., Bjorkman P.J., Nussenzweig M.C.
    Cell 153:126-138(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-160 AND ASN-188.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-87; ASN-160 AND ASN-188.
  12. "Restricting HIV-1 pathways for escape using rationally designed anti-HIV-1 antibodies."
    Diskin R., Klein F., Horwitz J.A., Halper-Stromberg A., Sather D.N., Marcovecchio P.M., Lee T., West A.P., Gao H., Seaman M.S., Stamatatos L., Nussenzweig M.C., Bjorkman P.J.
    J. Exp. Med. 210:1235-1249(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-160 AND ASN-188.
  13. "Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody."
    Scharf L., West A.P., Gao H., Lee T., Scheid J.F., Nussenzweig M.C., Bjorkman P.J., Diskin R.
    Proc. Natl. Acad. Sci. U.S.A. 110:6049-6054(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.26 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-188.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-160 AND ASN-188.
  15. "Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike."
    Scharf L., Scheid J.F., Lee J.H., West A.P., Chen C., Gao H., Gnanapragasam P.N., Mares R., Seaman M.S., Ward A.B., Nussenzweig M.C., Bjorkman P.J.
    Cell Rep. 7:785-795(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 201-303; 325-486 AND 43-122.
  16. "Crystal structures of HIV-1 gp120 envelope glycoprotein in complex with NBD analogues that target the CD4-binding site."
    Kwon Y.D., LaLonde J.M., Yang Y., Elban M.A., Sugawara A., Courter J.R., Jones D.M., Smith A.B., Debnath A.K., Kwong P.D.
    PLoS ONE 9:e85940-e85940(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 201-293; 341-433; 457-486 AND 88-122, GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297; ASN-335; ASN-356; ASN-386; ASN-392 AND ASN-442.

Entry informationi

Entry nameiQ0ED31_9HIV1
AccessioniPrimary (citable) accession number: Q0ED31
Entry historyi
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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