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HERV-H_2q24.3 provirus ancestral Env polyprotein (Env protein HERV-H/p62) (Env protein HERV-H19) (Env protein HERV-Hcl.3) (Envelope polyprotein) (HERV-H/env62) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]

 ENH1_HUMAN              Reviewed;         584 AA.
Q9N2K0; O00354; Q96L63; Q9UNM3;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
13-FEB-2019, entry version 88.
RecName: Full=HERV-H_2q24.3 provirus ancestral Env polyprotein;
AltName: Full=Env protein HERV-H/p62;
AltName: Full=Env protein HERV-H19;
AltName: Full=Env protein HERV-Hcl.3;
AltName: Full=Envelope polyprotein;
AltName: Full=HERV-H/env62;
Contains:
RecName: Full=Surface protein;
Short=SU;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
Flags: Precursor;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-81 AND LEU-150.
PubMed=10366582; DOI=10.1006/viro.1999.9750;
Lindeskog M., Mager D.L., Blomberg J.;
"Isolation of a human endogenous retroviral HERV-H element with an
open env reading frame.";
Virology 258:441-450(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-81 AND LEU-150.
PubMed=11162811; DOI=10.1006/viro.2000.0737;
de Parseval N., Casella J.-F., Gressin L., Heidmann T.;
"Characterization of the three HERV-H proviruses with an open envelope
reading frame encompassing the immunosuppressive domain and
evolutionary history in primates.";
Virology 279:558-569(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-402, AND VARIANT LEU-81.
PubMed=12079564; DOI=10.1089/088922202760019383;
Jern P., Lindeskog M., Karlsson D., Blomberg J.;
"Full-length HERV-H elements with env SU open reading frames in the
human genome.";
AIDS Res. Hum. Retroviruses 18:671-676(2002).
[4]
FUNCTION.
PubMed=11562544;
Mangeney M., de Parseval N., Thomas G., Heidmann T.;
"The full-length envelope of an HERV-H human endogenous retrovirus has
immunosuppressive properties.";
J. Gen. Virol. 82:2515-2518(2001).
[5]
FUNCTION.
PubMed=14557543; DOI=10.1073/pnas.2132646100;
Blaise S., de Parseval N., Benit L., Heidmann T.;
"Genomewide screening for fusogenic human endogenous retrovirus
envelopes identifies syncytin 2, a gene conserved on primate
evolution.";
Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
[6]
TISSUE SPECIFICITY.
PubMed=12970426; DOI=10.1128/JVI.77.19.10414-10422.2003;
de Parseval N., Lazar V., Casella J.-F., Benit L., Heidmann T.;
"Survey of human genes of retroviral origin: identification and
transcriptome of the genes with coding capacity for complete envelope
proteins.";
J. Virol. 77:10414-10422(2003).
-!- FUNCTION: Retroviral envelope proteins mediate receptor
recognition and membrane fusion during early infection. Endogenous
envelope proteins may have kept, lost or modified their original
function during evolution. This endogenous envelope protein has
lost its original fusogenic properties but has immunosuppressive
properties in vivo. {ECO:0000269|PubMed:11562544,
ECO:0000269|PubMed:14557543}.
-!- FUNCTION: SU mediates receptor recognition. {ECO:0000250}.
-!- FUNCTION: TM anchors the envelope heterodimer to the viral
membrane through one transmembrane domain. The other hydrophobic
domain, called fusion peptide, mediates fusion of the viral
membrane with the target cell membrane (By similarity).
{ECO:0000250}.
-!- SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a
heterodimer. SU and TM are attached by noncovalent interactions or
by a labile interchain disulfide bond (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion.
-!- SUBCELLULAR LOCATION: Transmembrane protein: Cell membrane
{ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Low expression in skin and testis. No
expression in several cell lines. {ECO:0000269|PubMed:12970426}.
-!- DOMAIN: Contains the CKS-17 immunosuppressive domain present in
many retroviral envelope proteins. As a synthetic peptide, it
inhibits immune function in vitro and in vivo (By similarity).
{ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and
TM proteins. {ECO:0000250}.
-!- PTM: The CXXC motif is highly conserved across a broad range of
retroviral envelope proteins. It is thought to participate in the
formation of a labile disulfide bond possibly with the CX6CC motif
present in the transmembrane protein. Isomerization of the
intersubunit disulfide bond to an SU intrachain disulfide bond is
thought to occur upon receptor recognition in order to allow
membrane fusion (By similarity). {ECO:0000250}.
-!- POLYMORPHISM: Envelope protein HERV-H19 and HERV-H/p62 are allelic
variants of the same provirus.
-!- MISCELLANEOUS: Ortholog in Pan troglodytes.
-!- MISCELLANEOUS: HERV-H family subgenomic RNAs have been observed.
-!- MISCELLANEOUS: This provirus is intergenic, the closest flanking
genes being TAIP2 and GALNT3.
-!- SIMILARITY: Belongs to the gamma type-C retroviral envelope
protein family. HERV class-I H env subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF108843; AAD34324.1; -; Genomic_DNA.
EMBL; U88902; AAC79121.1; -; Genomic_DNA.
EMBL; AJ289709; CAB94192.1; -; Genomic_DNA.
EMBL; AY050297; AAL11491.1; -; Genomic_DNA.
PIR; B44282; B44282.
ProteinModelPortal; Q9N2K0; -.
SMR; Q9N2K0; -.
BioMuta; -; -.
PeptideAtlas; Q9N2K0; -.
PRIDE; Q9N2K0; -.
ProteomicsDB; 81855; -.
neXtProt; NX_Q9N2K0; -.
HOVERGEN; HBG017290; -.
PhylomeDB; Q9N2K0; -.
Proteomes; UP000005640; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
InterPro; IPR018154; TLV/ENV_coat_polyprotein.
PANTHER; PTHR10424; PTHR10424; 1.
Pfam; PF00429; TLV_coat; 2.
2: Evidence at transcript level;
Cell membrane; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; ERV; Glycoprotein; Membrane; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transposable element; Viral envelope protein; Virion.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 584 HERV-H_2q24.3 provirus ancestral Env
polyprotein.
/FTId=PRO_0000008460.
CHAIN 36 387 Surface protein. {ECO:0000250}.
/FTId=PRO_0000008461.
CHAIN 388 584 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000008462.
TOPO_DOM 36 523 Extracellular. {ECO:0000255}.
TRANSMEM 524 544 Helical. {ECO:0000255}.
TOPO_DOM 545 584 Cytoplasmic. {ECO:0000255}.
REGION 388 408 Fusion peptide. {ECO:0000250}.
MOTIF 64 67 CXXC. {ECO:0000250}.
MOTIF 454 470 CKS-17. {ECO:0000250}.
MOTIF 471 479 CX6CC. {ECO:0000250}.
SITE 387 388 Cleavage. {ECO:0000250}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 483 483 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 471 478 {ECO:0000250}.
VARIANT 81 81 V -> L (in allele HERV-H19).
{ECO:0000269|PubMed:10366582,
ECO:0000269|PubMed:11162811,
ECO:0000269|PubMed:12079564}.
/FTId=VAR_017799.
VARIANT 150 150 F -> L (in allele HERV-H19).
{ECO:0000269|PubMed:10366582,
ECO:0000269|PubMed:11162811}.
/FTId=VAR_017800.
CONFLICT 80 80 A -> T (in Ref. 3; AAL11491).
{ECO:0000305}.
CONFLICT 98 98 F -> C (in Ref. 3; AAL11491).
{ECO:0000305}.
CONFLICT 316 316 T -> A (in Ref. 3; AAL11491).
{ECO:0000305}.
CONFLICT 319 319 S -> G (in Ref. 1; AAC79121).
{ECO:0000305}.
SEQUENCE 584 AA; 64318 MW; C03D260B5A60BDAB CRC64;
MIFAGKAPSN TSTLMKFYSL LLYSLLFSFP FLCHPLPLPS YLHHTINLTH SLLAASNPSL
VNNCWLCISL SSSAYTAVPA VQTDWATSPI SLHLRTSFNS PHLYPPEELI YFLDRSSKTS
PDISHQQAAA LLRTYLKNLS PYINSTPPIF GPLTTQTTIP VAAPLCISWQ RPTGIPLGNL
SPSRCSFTLH LRSPTTNINE TIGAFQLHIT DKPSINTDKL KNISSNYCLG RHLPCISLHP
WLSSPCSSDS PPRPSSCLLI PSPENNSERL LVDTRRFLIH HENRTFPSTQ LPHQSPLQPL
TAAALAGSLG VWVQDTPFST PSHLFTLHLQ FCLAQGLFFL CGSSTYMCLP ANWTGTCTLV
FLTPKIQFAN GTEELPVPLM TPTQQKRVIP LIPLMVGLGL SASTVALGTG IAGISTSVMT
FRSLSNDFSA SITDISQTLS VLQAQVDSLA AVVLQNRRGL DLLTAEKGGL CIFLNEECCF
YLNQSGLVYD NIKKLKDRAQ KLANQASNYA EPPWALSNWM SWVLPIVSPL IPIFLLLLFG
PCIFRLVSQF IQNRIQAITN HSIRQMFLLT SPQYHPLPQD LPSA


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Pathways :
WP1616: ABC transporters
WP1665: Limonene and pinene degradation
WP1675: Nitrogen metabolism
WP1685: Peptidoglycan biosynthesis
WP1714: Tyrosine metabolism
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[] HERV-H_2q24.3 provirus ancestral Env polyprotein (Env protein HERV-H/p62) (Env protein HERV-H19) (Env protein HERV-Hcl.3) (Envelope polyprotein) (HERV-H/env62) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-18] Endogenous retrovirus group K member 18 Env polyprotein (Envelope polyprotein) (HERV-K(C1a) envelope protein) (HERV-K110 envelope protein) (HERV-K18 envelope protein) (HERV-K18 superantigen) (HERV-K_1q23.3 provirus ancestral Env polyprotein) (IDDMK1,2 22 envelope protein) (IDDMK1,2 22 superantigen) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVW-1 ERVWE1] Syncytin-1 (Endogenous retrovirus group W member 1) (Env-W) (Envelope polyprotein gPr73) (Enverin) (HERV-7q Envelope protein) (HERV-W envelope protein) (HERV-W_7q21.2 provirus ancestral Env polyprotein) (Syncytin) [Cleaved into: Surface protein (SU) (gp50); Transmembrane protein (TM) (gp24)]
[] HERV-H_2q24.1 provirus ancestral Env polyprotein (Env protein HERV-H/p59) (Envelope polyprotein) (HERV-H/env59) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERV3-1 ERV3] Endogenous retrovirus group 3 member 1 Env polyprotein (ERV-3 envelope protein) (ERV3 envelope protein) (ERV3-1 envelope protein) (Envelope polyprotein) (HERV-R envelope protein) (ERV-R envelope protein) (HERV-R_7q21.2 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-6 ERVK6] Endogenous retrovirus group K member 6 Env polyprotein (EnvK2 protein) (Envelope polyprotein) (HERV-K(C7) envelope protein) (HERV-K(HML-2.HOM) envelope protein) (HERV-K108 envelope protein) (HERV-K_7p22.1 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVFRD-1 ERVFRDE1 UNQ6191/PRO20218] Syncytin-2 (Endogenous retrovirus group FRD member 1) (Envelope polyprotein) (HERV-FRD) (HERV-FRD_6p24.1 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVFC1] Endogenous retrovirus group FC1 Env polyprotein (Envelope polyprotein) (Fc1env) (HERV-F(c)1_Xq21.33 provirus ancestral Env polyprotein) (HERV-Fc1env) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-9] Endogenous retrovirus group K member 9 Env polyprotein (EnvK4 protein) (Envelope polyprotein) (HERV-K(C6) envelope protein) (HERV-K109 envelope protein) (HERV-K_6q14.1 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-19] Endogenous retrovirus group K member 19 Env polyprotein (EnvK3 protein) (Envelope polyprotein) (HERV-K(C19) envelope protein) (HERV-K_19q11 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-7] Endogenous retrovirus group K member 7 Env polyprotein (Envelope polyprotein) (HERV-K(III) envelope protein) (HERV-K102 envelope protein) (HERV-K_1q22 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-8] Endogenous retrovirus group K member 8 Env polyprotein (EnvK6 protein) (Envelope polyprotein) (HERV-K115 envelope protein) (HERV-K_8p23.1 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[HERVK_113] Endogenous retrovirus group K member 113 Env polyprotein (EnvK5 protein) (Envelope polyprotein) (HERV-K113 envelope protein) (HERV-K_19p13.11 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-9] Endogenous retrovirus group K member 9 Pol protein (HERV-K(C6) Gag-Pol protein) (HERV-K109 Gag-Pol protein) (HERV-K_6q14.1 provirus ancestral Gag-Pol polyprotein) [Includes: Protease (EC 3.4.23.50) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (p66 RT)]
[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)]
[ERVK-24] Endogenous retrovirus group K member 24 Env polyprotein (Envelope polyprotein) (HERV-K101 envelope protein) (HERV-K_22q11.21 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[ERVK-6 ERVK6] Endogenous retrovirus group K member 6 Rec protein (Central open reading frame) (c-orf) (cORF) (Endogenous retrovirus K protein 6) (HERV-K(C7) Rec protein) (HERV-K(HML-2.HOM) Rec protein) (HERV-K108 Rec protein) (HERV-K_7p22.1 provirus Rec protein) (K-Rev) (Rev-like protein) (Rev/Rex homolog)
[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)]
[ERVK-21] Endogenous retrovirus group K member 21 Env polyprotein (EnvK1 protein) (Envelope polyprotein) (HERV-K_12q14.1 provirus ancestral Env polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[] ERV-H1 provirus ancestral Env polyprotein (ERV-H/env62) (Envelope polyprotein) (Env protein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)]
[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 :