Envelope glycoprotein - Human immunodeficiency virus 1

Preferred order of sections

Names and origin

Protein names

Submitted name:
Envelope glycoprotein EMBL AAK20295.1

Gene names

Name:

env EMBL AAK20295.1

Organism

Human immunodeficiency virus 1 EMBL AAK20295.1

Taxonomic identifier

11676 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group

Protein attributes

Sequence length	588 AA.
Sequence status	Fragment.
Protein existence	Evidence 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

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

Ontologies

Keywords
Biological process	Apoptosis SAAS SAAS000328 Fusion of virus membrane with host membrane SAAS SAAS000328 Host-virus interaction Initiation of viral infection Viral attachment to host cell SAAS SAAS000328 Viral penetration into host cytoplasm
Cellular component	Host cell membrane SAAS SAAS000328 Host endosome SAAS SAAS000328 Host membrane Membrane Viral envelope protein RuleBase RU003294 SAAS SAAS000328 EMBL AAK20295.1 Virion
Disease	AIDS RuleBase RU003294
Domain	Transmembrane Transmembrane helix SAAS SAAS000328
PTM	Disulfide bond SAAS SAAS000328
Technical term	3D-structure PDB 2NY1 PDB 2NY3
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell endosome Inferred from electronic annotation. Source: UniProtKB-KW host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: InterPro
Molecular function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Amino acid modifications

Glycosylation

31

1

N-linked (GlcNAc...) PDB 2NY1

Glycosylation

140

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Glycosylation

173

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Glycosylation

177

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Glycosylation

184

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Glycosylation

205

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Glycosylation

219

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Glycosylation

232

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Glycosylation

238

1

N-linked (GlcNAc...) PDB 2NY1 PDB 2NY3

Experimental info

Non-terminal residue

Non-terminal residue

1

Sequences

Sequence

Length

Mass (Da)

Tools

Q993A8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 47475A5780240AE8
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FASTA

588

65,643

        10         20         30         40         50         60 
AKAYDTEVHN VWATHACVPT DPNPQEVVLV NVTENFNMWK NDMVEQMHED IISLWDQSLK 

        70         80         90        100        110        120 
PCVKLTPLCV SLKCTDLKND TNTNSSSGRM IMEKGEIKNC SFNISTSIRG KVQKEYAFFY 

       130        140        150        160        170        180 
KLDIIPIDND TTSYTLTSCN TSVITQACPK VSFEPIPIHY CAPAGFAILK CNNKTFNGTG 

       190        200        210        220        230        240 
PCTNVSTVQC THGIRPVVST QLLLNGSLAE EEVVIRSVNF TDNAKTIIVQ LNTSVEINCT 

       250        260        270        280        290        300 
RPNNNTRKKI RIQRGPGRAF VTIGKIGNMR QAHCNISRAK WNATLKQIAS KLREQFGNNK 

       310        320        330        340        350        360 
TIIFKQSSGG DPEIVTHSFN CGGEFFYCNS TQLFNSTWFN STWSTEGSNN TEGSDTITLP 

       370        380        390        400        410        420 
CRIKQIINMW QEVGKAMYAP PISGQIRCSS NITGLLLTRD GGNSNNESEI FRPGGGDMRD 

       430        440        450        460        470        480 
NWRSELYKYK VVKIEPLGVA PTKAKRRVVQ REKRAVGIGA LFLGFLGAAG STMGAASMTL 

       490        500        510        520        530        540 
TVQARQLLSG IVQQQNNLLR AIEAQQHLLQ LTVWGIKQLQ ARILAVERYL KDQQLLGIWG 

       550        560        570        580 
CSGKLICTTA VPWNASWSNK SLEQIWNNMT WMEWDREINN YTSLIHSL

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References

[1]	"Structural features of HIV envelope defined by antibody escape mutant analysis." D'Costa S., Slobod K.S., Webster R.G., White S.W., Hurwitz J.L. AIDS Res. Hum. Retroviruses 17:1205-1209(2001) [PubMed: 11522189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	DCosta S.S., Hurwitz J.L. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Structural definition of a conserved neutralization epitope on HIV-1 gp120." Zhou T., Xu L., Dey B., Hessell A.J., Van Ryk D., Xiang S.H., Yang X., Zhang M.Y., Zwick M.B., Arthos J., Burton D.R., Dimitrov D.S., Sodroski J., Wyatt R., Nabel G.J., Kwong P.D. Nature 445:732-737(2007) [PubMed: 17301785] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 26-435, GLYCOSYLATION AT ASN-31; ASN-140; ASN-173; ASN-177; ASN-184; ASN-205; ASN-219; ASN-232 AND ASN-238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF321147 Genomic DNA. Translation: AAK20295.1.

PIR

A53591.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NY1	X-ray	1.99	A	26-435	[»]
2NY3	X-ray	2.00	A	138-435	[»]

ProteinModelPortal

Q993A8.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]

Gene3D

G3DSA:2.170.40.20. GP120. 2 hits.

Pfam

PF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]

SUPFAM

SSF56502. GP120. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q993A8_9HIV1

Accession

Primary (citable) accession number: Q993A8

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)