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Protein

Envelope glycoprotein gp160

Gene

env

Organism
Human immunodeficiency virus 1
Status
Unreviewed-Annotation score: 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.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein gp160UniRule annotationSAAS annotation
Alternative name(s):
Endogenous retrovirus group K member 113 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 18 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 19 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 21 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 24 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 25 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 6 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 7 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 8 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 9 Env polyproteinSAAS annotation
Envelope glycoprotein gp160
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

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Keywords - Diseasei

AIDSUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi125 ↔ 190Combined sources
Disulfide bondi130 ↔ 146Combined sources
Glycosylationi149 – 1491N-linked (GlcNAc...)Combined sources
Glycosylationi162 – 1621N-linked (GlcNAc...)Combined sources

Keywords - PTMi

Cleavage on pair of basic residuesUniRule annotation, Disulfide bondSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U2SX-ray1.80C/G125-244[»]
4DQOX-ray2.44C125-244[»]
ProteinModelPortaliQ6TCP8.
SMRiQ6TCP8. Positions 82-470, 490-568, 606-639.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q6TCP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVKGILRNC QQWWIWGILG FWMLMICNVV GNLWVTVYYG VPVWKEAKTT
60 70 80 90 100
LFCASDAKSY EREVHNVWAT HACVPTDPDP QELVMANVTE NFNMWKNDMV
110 120 130 140 150
DQMHEDIISL WDQSLKPCVK LTPLCVTLNC TSPAAHNESE TRVKHCSFNI
160 170 180 190 200
TTDVKDRKQK VNATFYDLDI VPLSSSDNSS NSSLYRLISC NTSTITQACP
210 220 230 240 250
KVSFDPIPIH YCAPAGYAIL KCNNKTFSGK GPCSNVSTVQ CTHGIRPVVS
260 270 280 290 300
TQLLLNGSLA EEEIVIRSEN LTDNAKTIIV HLNKSVEIEC IRPGNNTRKS
310 320 330 340 350
IRLGPGQTFY ATGDVIGDIR KAYCKINGSE WNETLTKVSE KLKEYFNKTI
360 370 380 390 400
RFAQHSGGDL EVTTHSFNCR GEFFYCNTSE LFNSNATESN ITLPCRIKQI
410 420 430 440 450
INMWQGVGRA MYAPPIRGEI KCTSNITGLL LTRDGGNNNN STEEIFRPEG
460 470 480 490 500
GNMRDNWRSE LYKYKVVEIK PLGIAPTEAK RRVVQREKRA VGIGAVFLGF
510 520 530 540 550
LGAAGSTMGA ASITLTVQAR QLLSGIVQQQ SNLLRAIEAQ QHLLQLTVWG
560 570 580 590 600
IKQLQARVLA IERYLQDQQL LGIWGCSGKL ICTTAVPWNS SWSNKSKEEI
610 620 630 640 650
WGNMTWMQWD KEVSNYTFTI YQLLEESQYQ QEQNEKELLA LNKWNDLWSW
660 670 680 690 700
FNITNWLWYI KIFIMIVGGL IGLRIIFAVL SIVNRVRQGY SPLSFQTLTP
710 720 730 740 750
NPGGPDRLGR IEGEGGEQDK NRSIRLVNGF LALIWDDLWS LCRFSYHLLR
760 770 780 790 800
DFILIVARAV ELLGRSSLKG LQRGWEALKY LGNLMQYWGL ELKRSAINLL
810 820 830 840
DTTAVAVAEG TDRIIELAQG IYRAICNIPR RIRQGFEAAL Q
Length:841
Mass (Da):95,156
Last modified:November 22, 2005 - v2
Checksum:i1175F660B06DD6D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY424138 Genomic DNA. Translation: AAR09542.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY424138 Genomic DNA. Translation: AAR09542.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U2SX-ray1.80C/G125-244[»]
4DQOX-ray2.44C125-244[»]
ProteinModelPortaliQ6TCP8.
SMRiQ6TCP8. Positions 82-470, 490-568, 606-639.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ZM109F.PB4Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ZM109F.PB4Imported.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 125-244, DISULFIDE BONDS, GLYCOSYLATION AT ASN-149.
  4. "Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16."
    Pancera M., Shahzad-Ul-Hussan S., Doria-Rose N.A., McLellan J.S., Bailer R.T., Dai K., Loesgen S., Louder M.K., Staupe R.P., Yang Y., Zhang B., Parks R., Eudailey J., Lloyd K.E., Blinn J., Alam S.M., Haynes B.F., Amin M.N.
    , Wang L.X., Burton D.R., Koff W.C., Nabel G.J., Mascola J.R., Bewley C.A., Kwong P.D.
    Nat. Struct. Mol. Biol. 20:804-813(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 125-244, DISULFIDE BONDS, GLYCOSYLATION AT ASN-149 AND ASN-162.

Entry informationi

Entry nameiQ6TCP8_9HIV1
AccessioniPrimary (citable) accession number: Q6TCP8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: November 22, 2005
Last modified: July 22, 2015
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.