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Q0ED31 (Q0ED31_9HIV1) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Envelope glycoprotein gp160 RuleBase RU004292
Gene names
Name:env EMBL BAF31376.1
OrganismHuman immunodeficiency virus 1 EMBL BAF31376.1
Taxonomic identifier11676 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. SAAS SAAS000328 RuleBase RU004292

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 SAAS000328

Subcellular location

Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein By similarity SAAS SAAS000328.

Ontologies

Keywords
   Biological processApoptosis SAAS SAAS000328
Fusion of virus membrane with host membrane SAAS SAAS000328
Host-virus interaction
Viral attachment to host cell SAAS SAAS000328 RuleBase RU004292
Viral immunoevasion RuleBase RU004292
Viral penetration into host cytoplasm
Virus entry into host cell
   Cellular componentHost cell membrane SAAS SAAS000328
Host endosome SAAS SAAS000328
Host membrane
Membrane
Viral envelope protein SAAS SAAS000328 RuleBase RU003294
Virion
   DiseaseAIDS RuleBase RU003294
   DomainTransmembrane
Transmembrane helix SAAS SAAS000328
   LigandChloride PDB 3SE9 PDB 3U7Y
   PTMCleavage on pair of basic residues RuleBase RU004292
Disulfide bond SAAS SAAS000328
   Technical term3D-structure PDB 4DKU PDB 4DKV PDB 4DKO PDB 4I54 PDB 4DKP PDB 4JPV PDB 4DKQ PDB 4JPW PDB 4DKR PDB 4DVT PDB 3NGB PDB 4DVS PDB 3SE9 PDB 4H8W PDB 4DVW PDB 4LSP PDB 4JB9 PDB 4DVV PDB 3TGT PDB 4LSQ PDB 4LSR PDB 4DVX PDB 4JKP PDB 3U7Y PDB 3SE8 PDB 4JDT PDB 4LSU
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

evasion or tolerance by virus of host immune response

Inferred from electronic annotation. Source: UniProtKB-KW

membrane fusion involved in viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region59 – 602Sulfate 1 binding PDB 4LSP PDB 4LSR

Sites

Binding site681Chloride 1 PDB 3SE9
Binding site681Sulfate 2 PDB 4LSP
Binding site681Sulfate 3 PDB 4LSR
Binding site1091Sulfate 2 PDB 4LSP
Binding site1091Sulfate 3 PDB 4LSR
Binding site1131Sulfate 3 PDB 4LSR
Binding site2811Chloride 3 PDB 3U7Y
Binding site3771Sulfate 4 PDB 4JDT

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) PDB 3NGB PDB 4LSP PDB 3U7Y
Glycosylation1601N-linked (GlcNAc...) PDB 4I54 PDB 4JPV PDB 4JPW PDB 4LSP PDB 4JB9 PDB 4LSQ PDB 4LSR PDB 4JKP PDB 4LSU
Glycosylation1881N-linked (GlcNAc...)
Glycosylation2361N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 4DVT PDB 3NGB PDB 4DVS PDB 4DVW PDB 4DVV PDB 3U7Y
Glycosylation2431N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV
Glycosylation2641N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV PDB 3U7Y
Glycosylation2781N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV
Glycosylation2911N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV PDB 3U7Y
Glycosylation2971N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV PDB 3U7Y
Glycosylation3351N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV
Glycosylation3561N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 4DVS PDB 4DVW PDB 4DVV
Glycosylation3861N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVW PDB 4DVV PDB 3U7Y
Glycosylation3921N-linked (GlcNAc...) PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV
Glycosylation4421N-linked (GlcNAc...) PDB 4DKU PDB 4DKV PDB 3NGB PDB 4DVS PDB 4DVV

Sequences

Sequence LengthMass (Da)Tools
Q0ED31 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: AA83C4FF189CCD0E

FASTA85797,310
        10         20         30         40         50         60 
MRVKETQMNW PNLWKWGTLI LGLVIICSAS DNLWVTVYYG VPVWKDADTT LFCASDAKAH 

        70         80         90        100        110        120 
ETEVHNVWAT HACVPTDPNP QEIHLENVTE NFNMWKNNMV EQMQEDVISL WDQSLQPCVK 

       130        140        150        160        170        180 
LTPLCVTLHC TTAKLTNVTN ITNVPNIGNI TDEVRNCSFN MTTEIRDKKQ KVHALFYKLD 

       190        200        210        220        230        240 
IVQIEDKNDS SKYRLINCNT SVIKQACPKI SFDPIPIHYC TPAGYVILKC NDKNFNGTGP 

       250        260        270        280        290        300 
CKNVSSVQCT HGIKPVVSTQ LLLNGSLAEE EIIIRSENLT NNAKTIIVHL NKSVEINCTR 

       310        320        330        340        350        360 
PSNNMRTSMR IGPGQVFYRT GSITGDIRKA YCEINGTKWN KVLKQVTEKL KEHFNNKTII 

       370        380        390        400        410        420 
FQPPSGGDLE ITMHHFNCRG EFFYCNTTQL FNNTCIGNET MKGCNGTITL PCKIKQIINM 

       430        440        450        460        470        480 
WQGTGQAMYA PPIDGKINCV SNITGILLTR DGGANNTSNE TFRPGGGNIK DNWRSELYKY 

       490        500        510        520        530        540 
KVVQIEPLGI APTRAKRRVV EREKRAVGIG AMIFGFLGAA GSTMGAASIT LTVQARQLLS 

       550        560        570        580        590        600 
GIVQQQSNLL RAIEAQQHLL QLTVWGIKQL QARVLAVERY LKDQKFLGLW GCSGKIICTT 

       610        620        630        640        650        660 
AVPWNSTWSN KSFEEIWNNM TWIEWEREIS NYTNQIYEIL TESQNQQDRN EKDLLELDKW 

       670        680        690        700        710        720 
ASLWNWFDIT NWLWYIKIFI MIVGGLIGLR IIFAVLSIVN RVRQGYSPLS FQTPIHHQRE 

       730        740        750        760        770        780 
PDRPERIEEG GGEQGRDRSV RLVSGFLSLA WDDLRSLCLF SYHRLRDFIL IATRTVELLG 

       790        800        810        820        830        840 
HSSLKGLRRG WEGLKYLGNL LLYWGQELKI SAISLLNTTA IAVAGWTDRV IEVAQGAWRA 

       850 
ILHIPRRIRQ GLERTLL 

« Hide

References

[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: 93TH057 EMBL BAF31376.1.
[2]"Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01."
Zhou T., Georgiev I., Wu X., Yang Z.Y., Dai K., Finzi A., Kwon Y.D., Scheid J.F., Shi W., Xu L., Yang Y., Zhu J., Nussenzweig M.C., Sodroski J., Shapiro L., Nabel G.J., Mascola J.R., Kwong P.D.
Science 329:811-817(2010) [PubMed] [Europe PMC] [Abstract]
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]"Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing."
NISC Comparative Sequencing Program
Wu X., Zhou T., Zhu J., Zhang B., Georgiev I., Wang C., Chen X., Longo N.S., Louder M., McKee K., O'Dell S., Perfetto S., Schmidt S.D., Shi W., Wu L., Yang Y., Yang Z.Y., Yang Z. expand/collapse author list , Zhang Z., Bonsignori M., Crump J.A., Kapiga S.H., Sam N.E., Haynes B.F., Simek M., Burton D.R., Koff W.C., Doria-Rose N.A., Connors M., Mullikin J.C., Nabel G.J., Roederer M., Shapiro L., Kwong P.D., Mascola J.R.
Science 333:1593-1602(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 43-486 IN COMPLEX WITH CHLORIDE AND SULFATE, 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 IN COMPLEX WITH CHLORIDE, 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]"Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies."
NISC Comparative Sequencing Program
Zhou T., Zhu J., Wu X., Moquin S., Zhang B., Acharya P., Georgiev I.S., Altae-Tran H.R., Chuang G.Y., Joyce M.G., Do Kwon Y., Longo N.S., Louder M.K., Luongo T., McKee K., Schramm C.A., Skinner J., Yang Y. expand/collapse author list , Yang Z., Zhang Z., Zheng A., Bonsignori M., Haynes B.F., Scheid J.F., Nussenzweig M.C., Simek M., Burton D.R., Koff W.C., Mullikin J.C., Connors M., Shapiro L., Nabel G.J., Mascola J.R., Kwong P.D.
Immunity 39:245-258(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 43-486 IN COMPLEX WITH SULFATE, 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 IN COMPLEX WITH SULFATE, GLYCOSYLATION AT ASN-188.
[14]"Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization."
Georgiev I.S., Doria-Rose N.A., Zhou T., Kwon Y.D., Staupe R.P., Moquin S., Chuang G.Y., Louder M.K., Schmidt S.D., Altae-Tran H.R., Bailer R.T., McKee K., Nason M., O'Dell S., Ofek G., Pancera M., Srivatsan S., Shapiro L. expand/collapse author list , Connors M., Migueles S.A., Morris L., Nishimura Y., Martin M.A., Mascola J.R., Kwong P.D.
Science 340:751-756(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 43-486, GLYCOSYLATION AT ASN-160 AND ASN-188.
[15]"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 201-303; 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; ASN-392 AND ASN-442.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB253424 Genomic DNA. Translation: BAF31367.1.
AB253425 Genomic DNA. Translation: BAF31376.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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/B201-302[»]
A/B325-486[»]
A/B43-122[»]
4DVTX-ray2.40A/B201-303[»]
A/B325-486[»]
A/B43-122[»]
4DVVX-ray1.94A/B201-303[»]
A/B325-486[»]
A/B43-122[»]
4DVWX-ray2.20A/B201-433[»]
A/B457-486[»]
A/B88-122[»]
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[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.170.40.20. 2 hits.
InterProIPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]
PfamPF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]
SUPFAMSSF56502. SSF56502. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ0ED31.

Entry information

Entry nameQ0ED31_9HIV1
AccessionPrimary (citable) accession number: Q0ED31
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)