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Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

 A7KW27_9HIV1            Unreviewed;       853 AA.
A7KW27;
11-SEP-2007, integrated into UniProtKB/TrEMBL.
11-SEP-2007, sequence version 1.
11-DEC-2019, entry version 89.
RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|HAMAP-Rule:MF_04083};
AltName: Full=Env polyprotein {ECO:0000256|HAMAP-Rule:MF_04083};
Contains:
RecName: Full=Surface protein gp120 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=SU {ECO:0000256|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 120 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=gp120 {ECO:0000256|HAMAP-Rule:MF_04083};
Contains:
RecName: Full=Transmembrane protein gp41 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=TM {ECO:0000256|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 41 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=gp41 {ECO:0000256|HAMAP-Rule:MF_04083};
Name=env {ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000313|EMBL:ABS53229.1};
Human immunodeficiency virus 1.
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11676 {ECO:0000313|EMBL:ABS53229.1};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:ABS53229.1}
NUCLEOTIDE SEQUENCE.
STRAIN=TT113PC_DUK50105_2B4 {ECO:0000313|EMBL:ABS53229.1};
Trinidad Acute Infection Cohort;
Keele B.F., Hahn B.H., Tamaras G.D., Greenberg M.L., Weinhold K.J.,
Blattner W.A., Cleghorn F., Jack N.;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:ACD34556.1}
NUCLEOTIDE SEQUENCE.
STRAIN=TT113PC_2B4 {ECO:0000313|EMBL:ACD34556.1};
PubMed=18490657; DOI=10.1073/pnas.0802203105;
Keele B.F., Giorgi E.E., Salazar-Gonzalez J.F., Decker J.M., Pham K.T.,
Salazar M.G., Sun C., Grayson T., Wang S., Li H., Wei X., Jiang C.,
Kirchherr J.L., Gao F., Anderson J.A., Ping L.H., Swanstrom R.,
Tomaras G.D., Blattner W.A., Goepfert P.A., Kilby J.M., Saag M.S.,
Delwart E.L., Busch M.P., Cohen M.S., Montefiori D.C., Haynes B.F.,
Gaschen B., Athreya G.S., Lee H.Y., Wood N., Seoighe C., Perelson A.S.,
Bhattacharya T., Korber B.T., Hahn B.H., Shaw G.M.;
"Identification and characterization of transmitted and early founder virus
envelopes in primary HIV-1 infection.";
Proc. Natl. Acad. Sci. U.S.A. 105:7552-7557(2008).
-!- FUNCTION: Envelope glycoprotein gp160: Oligomerizes in the host
endoplasmic reticulum into predominantly trimers. In a second time,
gp160 transits in the host Golgi, where glycosylation is completed. The
precursor is then proteolytically cleaved in the trans-Golgi and
thereby activated by cellular furin or furin-like proteases to produce
gp120 and gp41. {ECO:0000256|HAMAP-Rule:MF_04083}.
-!- FUNCTION: Surface protein gp120: Attaches the virus to the host
lymphoid cell by binding to the primary receptor CD4. This interaction
induces a structural rearrangement creating a high affinity binding
site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a
ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively
found on dendritic cells (DCs), and on endothelial cells of liver
sinusoids and lymph node sinuses. These interactions allow capture of
viral particles at mucosal surfaces by these cells and subsequent
transmission to permissive cells. HIV subverts the migration properties
of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus
transmission to permissive T-cells occurs either in trans (without DCs
infection, through viral capture and transmission), or in cis
(following DCs productive infection, through the usual CD4-gp120
interaction), thereby inducing a robust infection. In trans infection,
bound virions remain infectious over days and it is proposed that they
are not degraded, but protected in non-lysosomal acidic organelles
within the DCs close to the cell membrane thus contributing to the
viral infectious potential during DCs' migration from the periphery to
the lymphoid tissues. On arrival at lymphoid tissues, intact virions
recycle back to DCs' cell surface allowing virus transmission to CD4+
T-cells. {ECO:0000256|HAMAP-Rule:MF_04083}.
-!- FUNCTION: Transmembrane protein gp41: Acts as a class I viral fusion
protein. Under the current model, the protein has at least 3
conformational states: pre-fusion native state, pre-hairpin
intermediate state, and post-fusion hairpin state. During fusion of
viral and target intracellular membranes, the coiled coil regions
(heptad repeats) assume a trimer-of-hairpins structure, positioning the
fusion peptide in close proximity to the C-terminal region of the
ectodomain. The formation of this structure appears to drive apposition
and subsequent fusion of viral and target cell membranes. Complete
fusion occurs in host cell endosomes and is dynamin-dependent, however
some lipid transfer might occur at the plasma membrane. The virus
undergoes clathrin-dependent internalization long before endosomal
fusion, thus minimizing the surface exposure of conserved viral
epitopes during fusion and reducing the efficacy of inhibitors
targeting these epitopes. Membranes fusion leads to delivery of the
nucleocapsid into the cytoplasm. {ECO:0000256|HAMAP-Rule:MF_04083}.
-!- SUBUNIT: The mature envelope protein (Env) consists of a homotrimer of
non-covalently associated gp120-gp41 heterodimers. The resulting
complex protrudes from the virus surface as a spike. There seems to be
as few as 10 spikes on the average virion. Surface protein gp120
interacts with host CD4, CCR5 and CXCR4. Gp120 also interacts with the
C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred
to as DC-SIGN(R)). Gp120 and gp41 interact with GalCer. Gp120 interacts
with host ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction
results in rapid activation of integrin ITGAL/LFA-1, which facilitates
efficient cell-to-cell spreading of HIV-1. Gp120 interacts with cell-
associated heparan sulfate; this interaction increases virus
infectivity on permissive cells and may be involved in infection of
CD4- cells. {ECO:0000256|HAMAP-Rule:MF_04083}.
-!- SUBCELLULAR LOCATION: Host cell membrane
{ECO:0000256|SAAS:SAAS01060237}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS01060237}. Host cell membrane
{ECO:0000256|SAAS:SAAS01060091}; Single-pass type I membrane protein
{ECO:0000256|SAAS:SAAS01060091}. Host endosome membrane
{ECO:0000256|SAAS:SAAS01060316}; Single-pass type I membrane protein
{ECO:0000256|SAAS:SAAS01060316}. Virion membrane
{ECO:0000256|SAAS:SAAS00796993}; Single-pass type I membrane protein
{ECO:0000256|SAAS:SAAS00796993}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-
Rule:MF_04083}; Peripheral membrane protein {ECO:0000256|HAMAP-
Rule:MF_04083}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04083};
Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_04083}. Host
endosome membrane {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I
membrane protein {ECO:0000256|HAMAP-Rule:MF_04083}. Note=The surface
protein is not anchored to the viral envelope, but associates with the
extravirion surface through its binding to TM. It is probably
concentrated at the site of budding and incorporated into the virions
possibly by contacts between the cytoplasmic tail of Env and the N-
terminus of Gag. {ECO:0000256|HAMAP-Rule:MF_04083}.
-!- SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane
{ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
{ECO:0000256|HAMAP-Rule:MF_04083}. Host cell membrane
{ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
{ECO:0000256|HAMAP-Rule:MF_04083}. Host endosome membrane
{ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
{ECO:0000256|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at
the site of budding and incorporated into the virions possibly by
contacts between the cytoplasmic tail of Env and the N-terminus of Gag.
{ECO:0000256|HAMAP-Rule:MF_04083}.
-!- DOMAIN: Some of the most genetically diverse regions of the viral
genome are present in Env. They are called variable regions 1 through 5
(V1 through V5). Coreceptor usage of gp120 is determined mainly by the
primary structure of the third variable region (V3) in the outer domain
of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or
CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and
macrophage tropism), is used to trigger the fusion potential of the Env
complex, and hence which cells the virus can infect. Binding to CCR5
involves a region adjacent in addition to V3. {ECO:0000256|HAMAP-
Rule:MF_04083}.
-!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
many retroviral envelope proteins. Synthetic peptides derived from this
relatively conserved sequence inhibit immune function in vitro and in
vivo. {ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095}.
-!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
{ECO:0000256|HAMAP-Rule:MF_04083}.
-!- DOMAIN: The YXXL motif is involved in determining the exact site of
viral release at the surface of infected mononuclear cells and promotes
endocytosis. YXXL and di-leucine endocytosis motifs interact directly
or indirectly with the clathrin adapter complexes, opperate
independently, and their activities are not additive.
{ECO:0000256|HAMAP-Rule:MF_04083}.
-!- DOMAIN: The membrane proximal external region (MPER) present in gp41 is
a tryptophan-rich region recognized by the antibodies 2F5, Z13, and
4E10. MPER seems to play a role in fusion. {ECO:0000256|HAMAP-
Rule:MF_04083}.
-!- PTM: Highly glycosylated by host. The high number of glycan on the
protein is reffered to as 'glycan shield' because it contributes to
hide protein sequence from adaptive immune system. {ECO:0000256|HAMAP-
Rule:MF_04083}.
-!- PTM: Palmitoylation of the transmembrane protein and of Env polyprotein
(prior to its proteolytic cleavage) is essential for their association
with host cell membrane lipid rafts. Palmitoylation is therefore
required for envelope trafficking to classical lipid rafts, but not for
viral replication. {ECO:0000256|HAMAP-Rule:MF_04083}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Envelope glycoproteins are synthesized as a inactive precursor that is
heavily N-glycosylated and processed likely by host cell furin in the
Golgi to yield the mature SU and TM proteins. The cleavage site between
SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9
disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to
CD4 receptor. {ECO:0000256|HAMAP-Rule:MF_04083}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
majority of strains found worldwide belong to the group M. Group O
seems to be endemic to and largely confined to Cameroon and neighboring
countries in West Central Africa, where these viruses represent a small
minority of HIV-1 strains. The group N is represented by a limited
number of isolates from Cameroonian persons. The group M is further
subdivided in 9 clades or subtypes (A to D, F to H, J and K).
{ECO:0000256|HAMAP-Rule:MF_04083}.
-!- MISCELLANEOUS: Inhibitors targeting HIV-1 viral envelope proteins are
used as antiretroviral drugs. Attachment of virions to the cell surface
via non-specific interactions and CD4 binding can be blocked by
inhibitors that include cyanovirin-N, cyclotriazadisulfonamide analogs,
PRO 2000, TNX 355 and PRO 542. In addition, BMS 806 can block CD4-
induced conformational changes. Env interactions with the coreceptor
molecules can be targeted by CCR5 antagonists including SCH-D,
maraviroc (UK 427857) and aplaviroc (GW 873140), and the CXCR4
antagonist AMD 070. Fusion of viral and cellular membranes can be
inhibited by peptides such as enfuvirtide and tifuvirtide (T 1249).
Resistance to inhibitors associated with mutations in Env are observed.
Most of the time, single mutations confer only a modest reduction in
drug susceptibility. Combination of several mutations is usually
required to develop a high-level drug resistance. {ECO:0000256|HAMAP-
Rule:MF_04083}.
-!- SIMILARITY: Belongs to the HIV-1 env protein family.
{ECO:0000256|HAMAP-Rule:MF_04083}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation of
feature annotation. {ECO:0000256|HAMAP-Rule:MF_04083}.
---------------------------------------------------------------------------
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EMBL; EF593261; ABS53229.1; -; Genomic_DNA.
EMBL; EU578570; ACD34556.1; -; Genomic_RNA.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
GO; GO:0090527; P:actin filament reorganization; IEA:UniProtKB-UniRule.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-UniRule.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IEA:UniProtKB-UniRule.
GO; GO:1903908; P:positive regulation of plasma membrane raft polarization; IEA:UniProtKB-UniRule.
GO; GO:1903911; P:positive regulation of receptor clustering; IEA:UniProtKB-UniRule.
GO; GO:0019082; P:viral protein processing; IEA:UniProtKB-UniRule.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
Gene3D; 2.170.40.20; -; 2.
HAMAP; MF_04083; HIV_ENV; 1.
InterPro; IPR036377; Gp120_core_sf.
InterPro; IPR037527; Gp160.
InterPro; IPR000328; GP41-like.
InterPro; IPR000777; HIV1_Gp120.
Pfam; PF00516; GP120; 1.
Pfam; PF00517; GP41; 1.
SUPFAM; SSF56502; SSF56502; 2.
3: Inferred from homology;
Apoptosis {ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS01060203};
Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP-
Rule:MF_04083};
Cleavage on pair of basic residues {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095};
Coiled coil {ECO:0000256|HAMAP-Rule:MF_04083};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|SAAS:SAAS01050261};
Fusion of virus membrane with host endosomal membrane {ECO:0000256|HAMAP-
Rule:MF_04083};
Fusion of virus membrane with host membrane {ECO:0000256|HAMAP-
Rule:MF_04083}; Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04083};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060118};
Host endosome {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060155};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060118};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797747};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04083};
Membrane {ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797734, ECO:0000256|SAAS:SAAS01060118};
Palmitate {ECO:0000256|HAMAP-Rule:MF_04083};
Signal {ECO:0000256|HAMAP-Rule:MF_04083};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797734};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797734};
Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797747};
Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797156,
ECO:0000313|EMBL:ABS53229.1};
Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04083};
Viral penetration into host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04083};
Virion {ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797156, ECO:0000256|SAAS:SAAS00797747,
ECO:0000313|EMBL:ABS53229.1};
Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04083};
Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797747}.
CHAIN 31..853
/note="Envelope glycoprotein gp160"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
/id="PRO_5023203342"
CHAIN 508..853
/note="Transmembrane protein gp41"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
/id="PRO_5023203346"
TRANSMEM 675..702
/note="Helical"
/evidence="ECO:0000256|RuleBase:RU363095"
TOPO_DOM 703..853
/note="Cytoplasmic"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DOMAIN 32..507
/note="GP120"
/evidence="ECO:0000259|Pfam:PF00516"
DOMAIN 527..716
/note="GP41"
/evidence="ECO:0000259|Pfam:PF00517"
REGION 129..154
/note="V1"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
REGION 358..368
/note="CD4-binding loop"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
REGION 379..412
/note="V4"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
REGION 450..470
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 571..589
/note="Immunosuppression"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
REGION 659..680
/note="MPER; binding to GalCer"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
COILED 630..664
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
MOTIF 709..712
/note="YXXL motif; contains endocytosis signal"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
MOTIF 852..853
/note="Di-leucine internalization motif"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
SITE 507..508
/note="Cleavage; by host furin"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
LIPID 761
/note="S-palmitoyl cysteine; by host"
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DISULFID 52..72
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DISULFID 129..155
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DISULFID 215..244
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DISULFID 225..236
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DISULFID 372..439
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DISULFID 379..412
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
DISULFID 595..601
/evidence="ECO:0000256|HAMAP-Rule:MF_04083"
SEQUENCE 853 AA; 96640 MW; 2BC9C207C3024B1B CRC64;
MRVKEIRRNW QPWKWGALLL GMLMICNAIE PLWVTVYYGV PVWKEATTTL FCASDAKAYD
TEVHNVWATH ACVPTDPSPQ EVVLKNVTEN FNMWKNNMVE QMHEDIISLW DESLKPCVKL
TPLCVTLNCT DREGTNSTNT TSGWEKVEKG EIKNCSFNIT TDMKDKVQKV YATFYKLDVI
SIDNSSNYRL INCNTSVITQ ACPKVSFEPI PIYYCTPAGF AILKCNDKTF NGKGPCKNVS
TVQCTHGIKP VVSTQLLLNG SLAEEEIVIR SENFTNNAKT IIVQLNESIA INCTRPNNNT
RRSIHLGPMG AFHTGEIIGD IRQAHCNLSG AQWNNTLRKI VIKLREQFEN KTIVFSQSSG
GDPEIVMHSF NCGGEFFYCN TTQLFNSTWN GSSTENGTTE QNGNDTTLTL PCRIKQIVNM
WQTVGKAMYA PPIKGQIRCS SKITGLLLTR DGGNRDGGNN TETFRPGGGD MRDNWRSELY
KYKVVKIEPL GVAPTRAKRR VVQREKRAVG TIGAMILGFL GTAGSTMGAA SITLTVQARQ
LLSGIVRQQN NLLRAVEAQQ HLLQLTVWGI KQLQARILAV ESYLRDQQLL GLWGCSGKLR
CTTSVPWNIS WSNKSLEEIW NNMTWMQWDR EIGNYTQLIY TLIQESQDQQ EKNEQELLEL
DKWASLWNWF DITQWLWYIK IFIMLIGGLI GLRIVFAVFS IVNRSRQGYS PLSLQTLLPV
PRGPDRPEGI EGEGGERDRD RSVRLVSGFS AIIWDDLRSL CLFSYHRLRD LLLVLVRIVE
ILGRRGWEAL KYWWSLLQYW SQELQNSAVS LLDATAIAVA EGTDRIIEAI RGGFRALLHI
PTRIRQGLER LLL


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Z5010240 Recombinant HIV_I Envelope (spanning C_terminus of gp120 and gp41) 500 µg
Z5010240 Recombinant HIV_I Envelope (spanning C_terminus of gp120 and gp41) 500 µg
ACLHIV101 HIV_I Envelope (spanning C_terminus of gp120 and gp41), recombinant 100 µg.
orb81728 HIV-1 Envelope conjugated to HIV-2 gp39 protein HIV-1,2 recombinant- E.coli derived recombinant 27 kDa protein contains the C- terminus of gp120 and most of gp41. The protein is conjugated to 23 amino 100
orb81719 HIV-1 gag p17-p24, gp41-gp120 protein Proteins 100
orb81708 HIV-1 gp41,gp120 protein Proteins 100
EIAAB06400 Cd8b,Cd8b1,Ly-3,Lymphocyte antigen 3,Lyt3,Lyt-3,Mouse,Mus musculus,T-cell membrane glycoprotein Ly-3,T-cell surface glycoprotein CD8 beta chain,T-cell surface glycoprotein Lyt-3
BRP1111 HIV-M2 (gp41+gp120+gp36+O) Recombinant Protein 100μg
BRP1112 HIV-M2 (gp41+gp120+gp36+O) Recombinant Protein 1mg
orb81714 HIV-1 gp120 CM protein HIV-1 gp120 CM Recombinant- is the external envelope protein, full-length 100-120 kDa, derived from the env. gene of HIV-1 and glycosylated with N-linked sugars and produced usi 2
orb81712 HIV-1 gp120 LAV protein HIV-1 gp120 LAV Recombinant- is the external envelope protein, full-length 100-120 kDa, derived from the env. gene of HIV-1 and glycosylated with N-linked sugars and produced u 2
orb81713 HIV-1 gp120 MN protein HIV-1 gp120 MN Recombinant- is the external envelope protein, full-length 100-120 kDa, derived from the env. gene of HIV-1 and glycosylated with N-linked sugars and produced usi 2
Pathways :
WP1665: Limonene and pinene degradation
WP1675: Nitrogen metabolism
WP1685: Peptidoglycan biosynthesis
WP1714: Tyrosine metabolism
WP1970: Glycoprotein VI platelet signaling
WP1616: ABC transporters
WP210: Cytoplasmic Ribosomal Proteins
WP1049: G Protein Signaling Pathways
WP1692: Protein export
WP931: G Protein Signaling Pathways
WP1650: Fluorobenzoate degradation
WP1700: Selenoamino acid metabolism
WP1659: Glycine, serine and threonine metabolism
WP2203: TSLP Signaling Pathway
WP1438: Influenza A virus infection
WP2292: Chemokine signaling pathway
WP1531: Vitamin D synthesis
WP2371: Parkinsons Disease Pathway
WP1892: Protein folding
WP1625: Base excision repair
WP525: Mitochondrial Unfolded-Protein Response
WP1690: Propanoate metabolism
WP813: G Protein Signaling Pathways
WP2032: TSH signaling pathway
WP1657: Glycerolipid metabolism

Related Genes :
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :