HV1H2:ENV

Species (Taxon ID)	Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)(HIV-1). (11706)
Gene Name(s)	env
Protein Name(s)	Envelope glycoprotein gp160 Env polyprotein Surface protein gp120 SU Glycoprotein 120 gp120 Transmembrane protein gp41 TM Glycoprotein 41 gp41
External Links
UniProt	P04578
EMBL	K03455 AF038399 AF033819
RefSeq	NP_057856.1
PDB	1AIK 1DF4 1DF5 1DLB 1G9M 1GC1 1GZL 1K33 1K34 1MZI 1OPN 1OPT 1OPW 1RZJ 2CMR 2ME1 2NY7 2PV6 2XRA 3D0V 3DNL 3DNN 3DNO 3IDX 3IDY 3TYG 3VIE 4JPJ 4JPK
PDBsum	1AIK 1DF4 1DF5 1DLB 1G9M 1GC1 1GZL 1K33 1K34 1MZI 1OPN 1OPT 1OPW 1RZJ 2CMR 2ME1 2NY7 2PV6 2XRA 3D0V 3DNL 3DNN 3DNO 3IDX 3IDY 3TYG 3VIE 4JPJ 4JPK
ProteinModelPortal	P04578
SMR	P04578
DIP	DIP-58525N
IntAct	P04578
MINT	MINT-7968605
BindingDB	P04578
ChEMBL	CHEMBL3520
GeneID	155971
Reactome	REACT_115574 REACT_163660 REACT_6359 REACT_6818 REACT_6903
EvolutionaryTrace	P04578
Proteomes	UP000002241
GO	GO:0044175 GO:0020002 GO:0016021 GO:0019031 GO:0055036 GO:0005198 GO:0006915 GO:0075512 GO:0030260 GO:0030683 GO:0039654 GO:0045087 GO:0019058 GO:0016032 GO:0019082 GO:0019068 GO:0019062
Gene3D	2.170.40.20
InterPro	IPR000777 IPR000328
Pfam	PF00516 PF00517
SUPFAM	SSF56502

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0019031	viral envelope	PMID:20471426^[1]	ECO:0000315			C		Fig. 3. Recognition of gp120 variants by CD4 and monoclonal antibodies. Note: gp160 cleaves into gp120 which is a surface protein and into gp41 which is a transmembrane protein.	complete
	GO:0070206	protein trimerization	PMID:24154805^[2]	ECO:0000314			P		Supplementary Figure 1. (available through PMC) shows electron micrographs of the protein and demonstrates it can be found in a trimeric form.	complete CACAO 10430
involved_in	GO:1903911	positive regulation of receptor clustering	PMID:23575248^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:1903908	positive regulation of plasma membrane raft polarization	PMID:23575248^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:1903905	positive regulation of establishment of T cell polarity	PMID:23575248^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0090527	actin filament reorganization	PMID:23575248^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	results_in_movement_of:(GO:0030864) part_of:(CL:0000084)	Seeded From UniProt	complete
enables	GO:0005198	structural molecule activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000328	F		Seeded From UniProt	complete
part_of	GO:0019031	viral envelope	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000777 InterPro:IPR036377	C		Seeded From UniProt	complete
enables	GO:0005198	structural molecule activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	F		Seeded From UniProt	complete
involved_in	GO:0019082	viral protein processing	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
involved_in	GO:1903911	positive regulation of receptor clustering	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
involved_in	GO:0019064	fusion of virus membrane with host plasma membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	C		Seeded From UniProt	complete
involved_in	GO:0075512	clathrin-dependent endocytosis of virus by host cell	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
part_of	GO:0019012	virion	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	C		Seeded From UniProt	complete
part_of	GO:0055036	virion membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	C		Seeded From UniProt	complete
involved_in	GO:1903908	positive regulation of plasma membrane raft polarization	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
involved_in	GO:0090527	actin filament reorganization	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
involved_in	GO:0019062	virion attachment to host cell	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
involved_in	GO:0039654	fusion of virus membrane with host endosome membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	C		Seeded From UniProt	complete
involved_in	GO:0030683	evasion or tolerance by virus of host immune response	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
part_of	GO:0044175	host cell endosome membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	C		Seeded From UniProt	complete
involved_in	GO:1903905	positive regulation of establishment of T cell polarity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000613575	P		Seeded From UniProt	complete
involved_in	GO:0019062	virion attachment to host cell	PMID:8906795^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0019012	virion	PMID:14668432^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0020002	host cell plasma membrane	PMID:9110072^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0075512	clathrin-dependent endocytosis of virus by host cell	PMID:19410541^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019064	fusion of virus membrane with host plasma membrane	PMID:2191297^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0019012	virion	PMID:14668432^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0075512	clathrin-dependent endocytosis of virus by host cell	PMID:19410541^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25132083^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04578:PRO_0000038428	F		Seeded From UniProt	complete
involved_in	GO:0019082	viral protein processing	PMID:2182911^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030260	entry into host cell	Reactome:R-HSA-173107	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019082	viral protein processing	Reactome:R-HSA-171286	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019068	virion assembly	Reactome:R-HSA-175474	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019064	fusion of virus membrane with host plasma membrane	Reactome:R-HSA-164524	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019058	viral life cycle	Reactome:R-HSA-162588	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002223	stimulatory C-type lectin receptor signaling pathway	Reactome:R-HSA-5621481	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0019031	viral envelope	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0261	C		Seeded From UniProt	complete
involved_in	GO:0030683	evasion or tolerance by virus of host immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0899	P		Seeded From UniProt	complete
part_of	GO:0019012	virion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0946	C		Seeded From UniProt	complete
involved_in	GO:0075512	clathrin-dependent endocytosis of virus by host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1165	P		Seeded From UniProt	complete
part_of	GO:0033644	host cell membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1043	C		Seeded From UniProt	complete
involved_in	GO:0039654	fusion of virus membrane with host endosome membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1170	P		Seeded From UniProt	complete
involved_in	GO:0039663	membrane fusion involved in viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1168	P		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
part_of	GO:0044174	host cell endosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1039	C		Seeded From UniProt	complete
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1032 UniProtKB-SubCell:SL-0375	C		Seeded From UniProt	complete
involved_in	GO:0075509	endocytosis involved in viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1164	P		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1160 UniProtKB-KW:KW-1162	P		Seeded From UniProt	complete
involved_in	GO:0019062	virion attachment to host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1161	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0055036	virion membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0275	C		Seeded From UniProt	complete
part_of	GO:0044175	host cell endosome membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0394	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Finzi, A et al. (2010) Conformational characterization of aberrant disulfide-linked HIV-1 gp120 dimers secreted from overexpressing cells. J. Virol. Methods 168 155-61 PubMed GONUTS page
↑ Bartesaghi, A et al. (2013) Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat. Struct. Mol. Biol. 20 1352-7 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 García-Expósito, L et al. (2013) Gelsolin activity controls efficient early HIV-1 infection. Retrovirology 10 39 PubMed GONUTS page
↑ Wu, L et al. (1996) CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature 384 179-83 PubMed GONUTS page
↑ ^5.0 ^5.1 Zhu, P et al. (2003) Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions. Proc. Natl. Acad. Sci. U.S.A. 100 15812-7 PubMed GONUTS page
↑ Sunila, I et al. (1997) gp120 is present on the plasma membrane of apoptotic CD4 cells prepared from lymph nodes of HIV-1-infected individuals: an immunoelectron microscopic study. AIDS 11 27-32 PubMed GONUTS page
↑ ^7.0 ^7.1 Miyauchi, K et al. (2009) HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137 433-44 PubMed GONUTS page
↑ Freed, EO et al. (1990) Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc. Natl. Acad. Sci. U.S.A. 87 4650-4 PubMed GONUTS page
↑ Lakomek, NA et al. (2014) HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation. Structure 22 1311-1321 PubMed GONUTS page
↑ Bosch, V & Pawlita, M (1990) Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site. J. Virol. 64 2337-44 PubMed GONUTS page

[PMID:20471426-1] Finzi, A et al. (2010) Conformational characterization of aberrant disulfide-linked HIV-1 gp120 dimers secreted from overexpressing cells. J. Virol. Methods 168 155-61 PubMed GONUTS page

[PMID:24154805-2] Bartesaghi, A et al. (2013) Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat. Struct. Mol. Biol. 20 1352-7 PubMed GONUTS page

[PMID:23575248-3] 3.0 ^3.1 ^3.2 ^3.3 García-Expósito, L et al. (2013) Gelsolin activity controls efficient early HIV-1 infection. Retrovirology 10 39 PubMed GONUTS page

[PMID:8906795-4] Wu, L et al. (1996) CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature 384 179-83 PubMed GONUTS page

[PMID:14668432-5] 5.0 ^5.1 Zhu, P et al. (2003) Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions. Proc. Natl. Acad. Sci. U.S.A. 100 15812-7 PubMed GONUTS page

[PMID:9110072-6] Sunila, I et al. (1997) gp120 is present on the plasma membrane of apoptotic CD4 cells prepared from lymph nodes of HIV-1-infected individuals: an immunoelectron microscopic study. AIDS 11 27-32 PubMed GONUTS page

[PMID:19410541-7] 7.0 ^7.1 Miyauchi, K et al. (2009) HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137 433-44 PubMed GONUTS page

[PMID:2191297-8] Freed, EO et al. (1990) Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc. Natl. Acad. Sci. U.S.A. 87 4650-4 PubMed GONUTS page

[PMID:25132083-9] Lakomek, NA et al. (2014) HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation. Structure 22 1311-1321 PubMed GONUTS page

[PMID:2182911-10] Bosch, V & Pawlita, M (1990) Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site. J. Virol. 64 2337-44 PubMed GONUTS page

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HV1H2:ENV

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