Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-11888-00737
Entry Name
UniProt Accession
Theoretical PI
8.68
Molecular Weight
65660.64
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Transmembrane protein
Protein Synonyms/Alias
Env polyprotein; SU; Glycoprotein 85; gp85; TM; Glycoprotein 37; gp37;
Gene Name
env
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
569
Canonical
VILLLLVCLPCLLQF
[1]
S-Palmitoylation
572
Canonical
LLLVCLPCLLQFVSS
[1]
S-Palmitoylation
Organism
Rous sarcoma virus (strain Prague C) (RSV-PrC)
NCBI Taxa ID
11888
Reference
[1] Ochsenbauer-Jambor C, Miller DC, Roberts CR, Rhee SS, Hunter E. Palmitoylationof the Rous sarcoma virus transmembrane glycoprotein is required for proteinstability and virus infectivity. J Virol. 2001 Dec;75(23):11544-54.[PMID:11689636]
Functional Description
The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).
Sequence Annotation
Topological domain: 65 556 Extracellular.
Transmembrane: 557 577 Helical.
Topological domain: 578 603 Cytoplasmic.
Region: 422 442 Fusion peptide.
Region: 478 494 Immunosuppression.
Functional site: 405 406 Cleavage; by host.
Protein Length
603 AA.
Protein Sequence
(Canonical)
MRRALFLQAF LTGYPGKTSK KDSKEKPLAT SKKDPEKTPL LPTRVNYILI IGVLVLCEVT  60
GVRADVHLLE QPGNLWITWA NRTGQTDFCL STQSATSPFQ TCLIGIPSPI SEGDFKGYVS  120
DTNCSTVGTD RLVLSASITG GPDNSTTLTY RKVSCLLLKL NVSMWDEPPE LQLLGSQSLP  180
NVTNITQVSG VAGGCVYFAP RATGLFLGWS KQGLSRFLLR HPFTSTSNST EPFTVVTADR  240
HNLFMGSEYC GAYGYRFWEI YNCSQTRNTY RCGDVGGTGL PETWCRGKGG IWVNQSKEIN  300
ETEPFSFTAN CTGSNLGNVS GCCGEPITIL PLGAWIDSTQ GSFTKPKALP PAIFLICGDR  360
AWQGIPSRPV GGPCYLGKLT MLAPNHTDIL KILANSSRTG IRRKRSVSHL DDTCSDEVQL  420
WGPTARIFAS ILAPGVAAAQ ALREIERLAC WSVKQANLTT SLLGDLLDDV TSIRHAVLQN  480
RAAIDFLLLA HGHGCEDVAG MCCFNLSDHS ESIQKKFQLM KKHVNKIGVD SDPIGSWLRG  540
IFGGIGEWAV HLLKGLLLGL VVILLLLVCL PCLLQFVSSS IRKMINSSIN YHTEYRKMQG  600
GAV                                                                603
FASTA
(Canonical)
>LipidDB-11888-00737|P03396
MRRALFLQAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVT
GVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVS
DTNCSTVGTDRLVLSASITGGPDNSTTLTYRKVSCLLLKLNVSMWDEPPELQLLGSQSLP
NVTNITQVSGVAGGCVYFAPRATGLFLGWSKQGLSRFLLRHPFTSTSNSTEPFTVVTADR
HNLFMGSEYCGAYGYRFWEIYNCSQTRNTYRCGDVGGTGLPETWCRGKGGIWVNQSKEIN
ETEPFSFTANCTGSNLGNVSGCCGEPITILPLGAWIDSTQGSFTKPKALPPAIFLICGDR
AWQGIPSRPVGGPCYLGKLTMLAPNHTDILKILANSSRTGIRRKRSVSHLDDTCSDEVQL
WGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQN
RAAIDFLLLAHGHGCEDVAGMCCFNLSDHSESIQKKFQLMKKHVNKIGVDSDPIGSWLRG
IFGGIGEWAVHLLKGLLLGLVVILLLLVCLPCLLQFVSSSIRKMINSSINYHTEYRKMQG
GAV
Gene Ontology
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0019031; C:viral envelope; IEA:UniProtKB-KW
GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW
GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR005166; RSV_p95_env
InterPro; IPR018154; TLV/ENV_coat_polyprotein
Pfam
Pfam; PF03708; Avian_gp85;
Pfam; PF00429; TLV_coat;
SMART
PROSITE
PRINTS