ERVFRD-1

Syncytin-2

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.

59.594 kDa

MGLLLLLLILTPLLAAYCHPDFRLLEKAQQLLQSTGSPYSTNCWLCTSSSSKTPGRAYPASSREWTTIEAELHISYQWDPNLKGLIRLANSLLSKVKQDFPDIRKEPPIFGPIFTNVNLIGIAPICVTAKRKDGTNVGTLPSTVCNVTLTVDPNQQTYQKYAHNQFHHQPRFPKPPNITFPQGTLLDKSTRFCQGRPSSCSTRNFWFQPADYNQCLQIPNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLSTSAVSEFSGTSVTSLFSFHISTCLKTQGAFYICGQSIHQCLPTNWTGTCTIGYVSPDIFIAPGNLSLPIPIYGNFHFPRVKRAIHLIPLLVGLGIVGSAGTGIAGIAKASFTYSQLSKEIANNIEAMAKTLTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNRASTLQEQATQGWLNWEGTWKWFSWVLPFTGPLVSLLLLLLFGPCLLNLITQFVSSRLQATKLQMKLNKRVHPRNSQESPF

ERVFRD-1

Syncytin-2

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.

59.569 kDa

MGLLLLVLILTPSLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYRWDPNLKGLMRPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGIAPICVTAKRKNGTNVGTLPSTVCNVTFTVDSNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSSRFCQGRPSSCSTRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLGISAVSEFFGTSLTPLFHFHISTCLKTQGAFYICGQLIHQCLPSNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGNSQLPRVRRAIHFIPLLAGLGILAGTGTGIAGITKASLTYSQLSKEIANNIDTMAKALTTMQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPLTGPLVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNLSAGRRPRNIQESPF

ERVFRD-1

Syncytin-2

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.

59.523 kDa

MGLLLLVLILTPSLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYRWDPNLKGLMRPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGIAPICVMAKRKNGTNVGTLPSTVCNVTFTVDSNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSSRFCQGRPSSCSTRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLGISAVSEFFGTSLTPLFHFHISTCLKTQGAFYICGQSIHQCLPSNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGNSPLPRVRRAIHFIPLLAGLGILAGTGTGIAGITKASLTYSQLSKEIANNIDTMAKALTTMQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPLTGPLVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNLSAGRHPRNIQESPF

ERVFRD-1

Syncytin-2

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution and this one is unable to confer infectivity.

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.

59.657 kDa

MGLLLLVLILTPLLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYQWDPNLKGLMRPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGIAPICVTAKRKNGTNVGTLPSTVCNVTFTVDPNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSTRFCQGRPSSCSTRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLGISAVSEFFGNSLTPLFHFHISTCLKTQGAFYICGQSIHQCLPSNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGKSQLPRVRRAIHFIPLLAGLGILAGTGTGIAGITKASLTYSQLSKEIANNIDTMAKTLTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPFIGPFVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNLSAGRRPRTIQESPF

ERVFRD-1

Syncytin-2

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.

59.584 kDa

MGLLLLVLILTPSLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYRWDPNLKGLMRPANSLLSMVKQDFPDIRQKPPIFGPIFTNINLMGIAPICVMAKRKNGTNVGTLPSTVCNVTFTVDSNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSSRFCQGRPSSCSTRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLGISAVSEFFGTSLTPLFHFHISTCLKTQGAFYICGQSIHQCLPSNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGNSQLPRVRRAIHFIPLLAGLGILAGTGTGIAGITKASLTYSQLSKEIANNIDTMAKALTTMQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPLTGPLVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNLSAGRHPRNIQESPF

ERVFRD-1

Syncytin-2

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.

59.489 kDa

MGLLLLVLILTPLLAAHRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYHWDPNLKGLMRPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGIAPICVTAKRKNGTNVGTLPSTVCNVTFTVDPNQQTYQTYTHKQFLHQPRFPKPPNITFPQGTLLDKSTRFCQGRPSSCSTRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLGISAVSEFFGTSLTPLFHFHISTCLKTQGAFYICGQSIHQCLPSNWTGTCTIGYVTPDIFIAPGNISLPIPIYGNSQLPRVRRAIHFIPLLAGLGIIAGTGTGIAGITKASLTYSQLSKEIAKNIDTMAKALTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPFTGPLVSLLLLLLFGPCLLNLITQFVLSRLQAIKLQTNLSAGCRPHNIQESPF

ERVFRD-1

Syncytin-2

537 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.

59.494 kDa

MGLLLLVLILTPLLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYQWDPNLKGLMTPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGKAPICVTAKRKNGTNVGTLPSTVCNVTFTVDPNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSTQFCQGRPSSCRTRNFWFRPADYNQCLQIPNLSSPAEWVLLDQTRNSLFWENKTKGANQSQTPCIQVLAGMTIATSYLGISPVSEFFGTSLTPLFHFHISTCLKTQGAFYICGQSIHQCLPTNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGNSQLPRARRAIHFIPLLAGLGILAGTGTGIAGITKASFTYSQLSKEIAKNIDTMAKTLTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPFIGPLVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNGAGCRPRNIQESPF