ENV_FRSFB
ID ENV_FRSFB Reviewed; 356 AA.
AC P31793;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Glycoprotein 42;
DE Short=gp42;
DE Flags: Precursor;
GN Name=env;
OS Friend spleen focus-forming virus (strain BB6) (FSFFV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=31692;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1583724; DOI=10.1128/jvi.66.6.3652-3660.1992;
RA Majumdar M.K., Cho C.L., Fox M.T., Eckner K.L., Kozak S., Kabat D.,
RA Geib R.W.;
RT "Mutations in the env gene of friend spleen focus-forming virus overcome
RT Fv-2r-mediated resistance to Friend virus-induced erythroleukemia.";
RL J. Virol. 66:3652-3660(1992).
CC -!- FUNCTION: This envelope-like membrane glycoprotein is responsible for
CC ligand-independent activation of the erythropoietin receptor EPOR
CC leading to the abnormally rapid proliferation of erythroid precursor
CC cells. In the first stage of Friend disease, constitutive activation of
CC the EPOR by gp42 causes uncontrolled, polyclonal proliferation of
CC infected erythroblasts, leading to polycythemia (massive increase in
CC the number of mature red cells). Host susceptibility to SSFV-induced
CC erythroblastosis usually depends on the expression of the truncated
CC isoform of MST1R receptor tyrosine kinase (MST1R isoform sf-Stk), but
CC the deletion mutant BB6 apparently can overcome its absence.
CC -!- SUBUNIT: Homooligomer. Forms heterooligomers with mouse EPOR, probably
CC via their respective transmembrane domains. BB6 deletion mutant does
CC not interact with mouse MST1R isoform sf-Stk.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Host cell membrane; Single-pass type I
CC membrane protein. Virion membrane; Single-pass type I membrane protein.
CC Note=The envelope-like membrane glycoprotein gp55 is defective in its
CC transport to the cell surface and remains associated predominantly with
CC the rough endoplasmic reticulum (RER) membrane. It is almost not
CC incorporated into virions. Host cell surface expression appears to be a
CC prerequisite for its leukemogenicity (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Compared to other gammaretroviruses which possess 2
CC envelope proteins (gp70 and p15E), FSFFV gp55 corresponds to a gp70-
CC p15E fusion protein with a deletion of a portion of p15E. It is encoded
CC by the defective env gene of the virus. Strain BB6 gp42 is a truncated
CC form of gp55.
CC -!- MISCELLANEOUS: The Friend murine leukemia virus complex induces a rapid
CC and fatal erythroleukemia in adult mice. It is the replication-
CC defective spleen focus-forming virus (SFFV) contained in this complex
CC that causes foci of proliferating erythroid cells in spleens of
CC infected mice. The second component is a replication competent Friend
CC murine leukemia virus (F-MuLV) that serves as a helper virus for SFFV.
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DR EMBL; M90673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A41995; VCVWB6.
DR SMR; P31793; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.90.310.10; -; 1.
DR InterPro; IPR008981; FMuLV_rcpt-bd.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 2.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 3: Inferred from homology;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endoplasmic reticulum; Host membrane;
KW Host-virus interaction; Membrane; Oncogene; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..356
FT /note="Glycoprotein 42"
FT /id="PRO_0000040722"
FT TOPO_DOM 33..331
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..356
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 247..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 306..309
FT /note="CXXC"
FT COMPBIAS 249..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 38778 MW; 0C7893BE2794F980 CRC64;
MEGPAFSKPL KDKINPWGPL IVLGILIRAG VSVQRDSPHQ VFNVTWRVTN LMTGQTANAT
SLLGTMTDAF PKLYFDLCDL IGNDWDETRL GCRTPGEGKR ARTFDLYVCP GHTVPTGCGG
PREGYCGKWG CETTGQAYWK PSSSWDLISL KRGNTPKDRG PCYDSSVSSG VQGATPGGRC
NPLVLKFTDA GKKASWDAPK VWGLRLYRST GTDPVTRFSL TRQVLNIGPR VPIGPNPVIS
DQLPPSRPAQ IMLPRPPQPP PPGTASIVPE TAPPSQQPGT RDRLLNLVNK AYQALNLTSP
DKTQECWLCL VSRPPYYEGV AVLGTNSNHT TLISTIMGLL IILLLLLILL LWTLHS
