Q0ED31 (Q0ED31_9HIV1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Envelope glycoprotein gp160 RuleBase RU004292

Gene names

Name:

env EMBL BAF31376.1

Organism

Human immunodeficiency virus 1 EMBL BAF31376.1

Taxonomic identifier

11676 [NCBI]

Taxonomic lineage

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

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	857 AA.
Sequence status	Complete.
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 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

Ontologies

Keywords
Biological process	Apoptosis 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 component	Host cell membrane SAAS SAAS000328 Host endosome SAAS SAAS000328 Host membrane Membrane Viral envelope protein SAAS SAAS000328 RuleBase RU003294 Virion
Disease	AIDS RuleBase RU003294
Domain	Transmembrane Transmembrane helix SAAS SAAS000328
PTM	Cleavage on pair of basic residues RuleBase RU004292 Disulfide bond SAAS SAAS000328
Technical term	3D-structure PDB 4DKU PDB 4DKV PDB 4DKO PDB 4DKP PDB 4DKQ PDB 4DKR PDB 4DVT PDB 3NGB PDB 4DVS PDB 3SE9 PDB 4DVW PDB 4DVV PDB 4DVX PDB 3SE8 PDB 4JDT
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW evasion or tolerance by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell 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: UniProtKB-KW
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	87	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	236	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	243	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	264	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	278	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	291	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	297	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	335	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	386	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	392	1	N-linked (GlcNAc...) PDB 3NGB
	Glycosylation	442	1	N-linked (GlcNAc...) PDB 3NGB

Sequences

	Sequence		Length	Mass (Da)
	Q0ED31 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: AA83C4FF189CCD0E	FASTA	857	97,310
	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

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 43-486, 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. , 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.
[4]	"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.
[5]	"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 43-486.
[6]	"Crystal Structures of HIV-1 gp120 Envelope Glycoprotein in Complex with Small Molecule Inhibitors 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 3rd A.B., Debnath A.K., Kwong P.D. Submitted (FEB-2012) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 43-486.

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NGB	X-ray	2.68	A/D/G/I	43-486	[»]
3SE8	X-ray	1.90	G	43-486	[»]
3SE9	X-ray	2.00	G	43-486	[»]
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	43-486	[»]
4DKV	X-ray	2.18	A/B	43-486	[»]
4DVS	X-ray	2.10	A/B	43-486	[»]
4DVT	X-ray	2.40	A/B	43-486	[»]
4DVV	X-ray	1.94	A/B	43-486	[»]
4DVW	X-ray	2.20	A/B	43-486	[»]
4DVX	X-ray	2.40	A/B	43-486	[»]
4JDT	X-ray	3.26	G	43-486	[»]

SMR

Q0ED31. Positions 82-486, 499-584.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.170.40.20. 2 hits.

InterPro

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

Pfam

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

SUPFAM

SSF56502. GP120. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q0ED31.

Entry information

Entry name

Q0ED31_9HIV1

Accession

Primary (citable) accession number: Q0ED31

Entry history

Integrated into UniProtKB/TrEMBL:	October 17, 2006
Last sequence update:	October 17, 2006
Last modified:	May 29, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)