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C6G099 (C6G099_9HIV1) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 38. 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 ACS67968.1
OrganismHuman immunodeficiency virus 1 EMBL ACS67968.1
Taxonomic identifier11676 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length849 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 EMBL ACS67968.1
Virion
   DiseaseAIDS RuleBase RU003294
   DomainTransmembrane
Transmembrane helix SAAS SAAS000328
   PTMCleavage on pair of basic residues RuleBase RU004292
Disulfide bond SAAS SAAS000328
   Technical term3D-structure PDB 3TGR PDB 3TGS PDB 4I53 PDB 4LSV
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

Amino acid modifications

Glycosylation1841N-linked (GlcNAc...) PDB 3TGR PDB 3TGS PDB 4I53 PDB 4LSV
Glycosylation2911N-linked (GlcNAc...) PDB 3TGR PDB 3TGS PDB 4I53 PDB 4LSV

Sequences

Sequence LengthMass (Da)Tools
C6G099 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: AE4C240E240E501F

FASTA84996,054
        10         20         30         40         50         60 
MRVRGIWKNW PQWLIWSILG FWIGNMEGSW VTVYYGVPVW KEAKTTLFCA SDAKAYEKEV 

        70         80         90        100        110        120 
HNVWATHACV PTDPNPQEMV LANVTENFNM WKNDMVEQMH EDIISLWDES LKPCVKLTPL 

       130        140        150        160        170        180 
CVTLNCTNVK GNESDTSEVM KNCSFKATTE LKDKKHKVHA LFYKLDVVPL NGNSSSSGEY 

       190        200        210        220        230        240 
RLINCNTSAI TQACPKVSFD PIPLHYCAPA GFAILKCNNK TFNGTGPCRN VSTVQCTHGI 

       250        260        270        280        290        300 
KPVVSTQLLL NGSLAEEEII IRSENLTNNA KTIIVHLNES VNIVCTRPNN NTRKSIRIGP 

       310        320        330        340        350        360 
GQTFYATGDI IGNIRQAHCN INESKWNNTL QKVGEELAKH FPSKTIKFEP SSGGDLEITT 

       370        380        390        400        410        420 
HSFNCRGEFF YCNTSDLFNG TYRNGTYNHT GRSSNGTITL QCKIKQIINM WQEVGRAIYA 

       430        440        450        460        470        480 
PPIEGEITCN SNITGLLLLR DGGQSNETND TETFRPGGGD MRDNWRSELY KYKVVEIKPL 

       490        500        510        520        530        540 
GVAPTEAKRR VVEREKRAVG IGAVFLGFLG AAGSTMGAAS MTLTVQARQL LSGIVQQQSN 

       550        560        570        580        590        600 
LLRAIEAQQH MLQLTVWGIK QLQARVLAIE RYLKDQQLLG MWGCSGKLIC TTAVPWNSSW 

       610        620        630        640        650        660 
SNKSQNEIWG NMTWMQWDRE INNYTNTIYR LLEDSQNQQE KNEKDLLALD SWKNLWNWFD 

       670        680        690        700        710        720 
ISKWLWYIKI FIMIIGGLIG LRIIFAVLSI VKRVRQGYSP LSFQTLTPNP RGPDRPGGIE 

       730        740        750        760        770        780 
EEGGEQDRDR SARLASGFLT LVWDDLRSLC LFSYHLLRDF ILVATRTVEL LGRSSLKGLQ 

       790        800        810        820        830        840 
RGWEILRYLG SLVQYWGLEL KKSAISLIDT IAIAVAERTD RIIEIVQRIC RAIRNIPRRI 


RQGFETALL 

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References

[1]Hraber P.T.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 1086-B12 EMBL ACS67968.1, 1086-B2 EMBL ACS67969.1, 1086-B5 EMBL ACS67970.1, 1086-C2 EMBL ACS67972.1, 1086-E12 EMBL ACS67973.1, 1086-F8 EMBL ACS67976.1, 1086-G1 EMBL ACS67978.1, 1086-G12 EMBL ACS67979.1, 1086-G2 EMBL ACS67980.1, 1086-H1 EMBL ACS67982.1 and 1086-H9 EMBL ACS67983.1.
[2]"Quantitating the multiplicity of infection with human immunodeficiency virus type 1 subtype C reveals a non-poisson distribution of transmitted variants."
CAPRISA Acute Infection Study Team, Center for HIV-AIDS Vaccine Immunology Consortium
Abrahams M.R., Anderson J.A., Giorgi E.E., Seoighe C., Mlisana K., Ping L.H., Athreya G.S., Treurnicht F.K., Keele B.F., Wood N., Salazar-Gonzalez J.F., Bhattacharya T., Chu H., Hoffman I., Galvin S., Mapanje C., Kazembe P., Thebus R. expand/collapse author list , Fiscus S., Hide W., Cohen M.S., Karim S.A., Haynes B.F., Shaw G.M., Hahn B.H., Korber B.T., Swanstrom R., Williamson C.
J. Virol. 83:3556-3567(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 1086-B12 EMBL ACS67968.1, 1086-B2 EMBL ACS67969.1, 1086-B5 EMBL ACS67970.1, 1086-C2 EMBL ACS67972.1, 1086-E12 EMBL ACS67973.1, 1086-F8 EMBL ACS67976.1, 1086-G1 EMBL ACS67978.1, 1086-G12 EMBL ACS67979.1, 1086-G2 EMBL ACS67980.1, 1086-H1 EMBL ACS67982.1 and 1086-H9 EMBL ACS67983.1.
[3]"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 (2.70 ANGSTROMS) OF 39-478, GLYCOSYLATION AT ASN-184 AND ASN-291.
[4]"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 39-478, GLYCOSYLATION AT ASN-184 AND ASN-291.
[5]"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 (3.00 ANGSTROMS) OF 39-478, GLYCOSYLATION AT ASN-184 AND ASN-291.
[6]"Comparison of viral Env proteins from acute and chronic infections with subtype C human immunodeficiency virus type 1 identifies differences in glycosylation and CCR5 utilization and suggests a new strategy for immunogen design."
Ping L.H., Joseph S.B., Anderson J.A., Abrahams M.R., Salazar-Gonzalez J.F., Kincer L.P., Treurnicht F.K., Arney L., Ojeda S., Zhang M., Keys J., Potter E.L., Chu H., Moore P., Salazar M.G., Iyer S., Jabara C., Kirchherr J. expand/collapse author list , Mapanje C., Ngandu N., Seoighe C., Hoffman I., Gao F., Tang Y., Labranche C., Lee B., Saville A., Vermeulen M., Fiscus S., Morris L., Karim S.A., Haynes B.F., Shaw G.M., Korber B.T., Hahn B.H., Cohen M.S., Montefiori D., Williamson C., Swanstrom R.
J. Virol. 87:7218-7233(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 1086-B2 EMBL AGV38303.1.
[7]Ping L.-H.
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 1086-B2 EMBL AGV38303.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ444394 Genomic DNA. Translation: ACS67968.1.
FJ444395 Genomic DNA. Translation: ACS67969.1.
FJ444396 Genomic DNA. Translation: ACS67970.1.
FJ444399 Genomic DNA. Translation: ACS67972.1.
FJ444404 Genomic DNA. Translation: ACS67973.1.
FJ444407 Genomic DNA. Translation: ACS67976.1.
FJ444409 Genomic DNA. Translation: ACS67978.1.
FJ444410 Genomic DNA. Translation: ACS67979.1.
FJ444411 Genomic DNA. Translation: ACS67980.1.
FJ444414 Genomic DNA. Translation: ACS67982.1.
FJ444415 Genomic DNA. Translation: ACS67983.1.
KC894079 Genomic RNA. Translation: AGV38303.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TGRX-ray2.80A/B39-478[»]
3TGSX-ray2.70A/B39-478[»]
4I53X-ray2.50A/B39-478[»]
4LSVX-ray3.00G39-478[»]
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...

Entry information

Entry nameC6G099_9HIV1
AccessionPrimary (citable) accession number: C6G099
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)