Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-11796-00732
Entry Name
UniProt Accession
Theoretical PI
8.59
Molecular Weight
74024.76
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
R-peptide
Protein Synonyms/Alias
Env polyprotein; SU; Glycoprotein 70; gp70; TM; Envelope protein p15E; p2E;
Gene Name
env
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
640
Canonical
LILLFGPCILNRLVQ
[1]
S-Palmitoylation
Organism
Friend murine leukemia virus (isolate 57) (FrMLV)
NCBI Taxa ID
11796
Reference
[1] Yang C, Compans RW. Palmitoylation of the murine leukemia virus envelopeglycoprotein transmembrane subunits. Virology. 1996 Jul 1;221(1):87-97. PubMedPMID: 8661417.[PMID:8661417]
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: 35 620 Extracellular.
Transmembrane: 621 641 Helical.
Topological domain: 642 675 Cytoplasmic.
Region: 35 270 Receptor-binding domain (RBD).
Region: 482 502 Fusion peptide.
Region: 548 564 Immunosuppression.
Motif: 346 349 CXXC.
Motif: 565 573 CX6CC.
Motif: 665 668 YXXL motif; contains endocytosis signal.
Metal binding site: 89 89 Zinc.
Metal binding site: 120 120 Zinc.
Functional site: 479 480 Cleavage; by host.
Functional site: 659 660 Cleavage; by viral protease p14.
Protein Length
675 AA.
Protein Sequence
(Canonical)
MACSTLPKSP KDKIDPRDLL IPLILFLSLK GARSAAPGSS PHQVYNITWE VTNGDRETVW  60
AISGNHPLWT WWPVLTPDLC MLALSGPPHW GLEYQAPYSS PPGPPCCSGS SGSSAGCSRD  120
CDEPLTSLTP RCNTAWNRLK LDQVTHKSSE GFYVCPGSHR PREAKSCGGP DSFYCASWGC  180
ETTGRVYWKP SSSWDYITVD NNLTTSQAVQ VCKDNKWCNP LAIQFTNAGK QVTSWTTGHY  240
WGLRLYVSGR DPGLTFGIRL RYQNLGPRVP IGPNPVLADQ LSLPRPNPLP KPAKSPPASN  300
STPTLISPSP TPTQPPPAGT GDRLLNLVQG AYQALNLTNP DKTQECWLCL VSGPPYYEGV  360
AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GRGLCIGTVP KTHQALCNTT LKIDKGSYYL  420
VAPTGTTWAC NTGLTPCLSA TVLNRTTDYC VLVELWPRVT YHPPSYVYSQ FEKSYRHKRE  480
PVSLTLALLL GGLTMGGIAA GVGTGTTALV ATQQFQQLHA AVQDDLKEVE KSITNLEKSL  540
TSLSEVVLQN RRGLDLLFLK EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLTQRQKLF  600
ESSQGWFEGL FNRSPWFTTL ISTIMGPLII LLLILLFGPC ILNRLVQFVK DRISVVQALV  660
LTQQYHQLKP LEYEP                                                   675
FASTA
(Canonical)
>LipidDB-11796-00732|P03390
MACSTLPKSPKDKIDPRDLLIPLILFLSLKGARSAAPGSSPHQVYNITWEVTNGDRETVW
AISGNHPLWTWWPVLTPDLCMLALSGPPHWGLEYQAPYSSPPGPPCCSGSSGSSAGCSRD
CDEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGC
ETTGRVYWKPSSSWDYITVDNNLTTSQAVQVCKDNKWCNPLAIQFTNAGKQVTSWTTGHY
WGLRLYVSGRDPGLTFGIRLRYQNLGPRVPIGPNPVLADQLSLPRPNPLPKPAKSPPASN
STPTLISPSPTPTQPPPAGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSGPPYYEGV
AVLGTYSNHTSAPANCSVASQHKLTLSEVTGRGLCIGTVPKTHQALCNTTLKIDKGSYYL
VAPTGTTWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSYRHKRE
PVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLHAAVQDDLKEVEKSITNLEKSL
TSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLTQRQKLF
ESSQGWFEGLFNRSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFVKDRISVVQALV
LTQQYHQLKPLEYEP
Gene Ontology
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0019028; C:viral capsid; IEA:InterPro
GO:0019031; C:viral envelope; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0005198; F:structural molecule activity; IEA:InterPro
GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW
GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW
GO:0039588; P:suppression by virus of host antigen processing and presentation; IEA:UniProtKB-KW
GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR008981; FMuLV_rcpt-bd
InterPro; IPR018154; TLV/ENV_coat_polyprotein
Pfam
Pfam; PF00429; TLV_coat;
SMART
PROSITE
PRINTS