ENV_FRSFL
ID ENV_FRSFL Reviewed; 409 AA.
AC P03394;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Glycoprotein 55;
DE Short=gp55;
DE Flags: Precursor;
GN Name=env;
OS Friend spleen focus-forming virus (strain Lilly-Steeves) (FSFFV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=355328;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6308646; DOI=10.1073/pnas.80.15.4718;
RA Wolff L., Scolnick E., Ruscetti S.;
RT "Envelope gene of the Friend spleen focus-forming virus: deletion and
RT insertions in 3' gp70/p15E-encoding region have resulted in unique features
RT in the primary structure of its protein product.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4718-4722(1983).
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 EPOR by gp55 causes uncontrolled, polyclonal proliferation of infected
CC erythroblasts, leading to polycythemia (massive increase in the number
CC of mature red cells). Host susceptibility to SSFV-induced
CC erythroblastosis depends on the expression of the truncated isoform of
CC MST1R receptor tyrosine kinase (MST1R isoform sf-Stk). Interaction with
CC SSFV gp 55 results in constitutive tyrosine phosphorylation and
CC activation of MST1R isoform sf-Stk (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Forms heterooligomers with mouse EPOR, probably
CC via their respective transmembrane domains. Forms covalent heterodimers
CC with mouse MST1R isoform sf-Stk, probably via disulfide bonds (By
CC similarity). {ECO:0000250}.
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), gp55 corresponds to a gp70-p15E
CC fusion protein with a deletion of a portion of p15E. It is encoded by
CC the defective env gene of the virus.
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; V01552; CAA24793.1; -; Genomic_DNA.
DR PIR; A03994; VCVW2S.
DR SMR; P03394; -.
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; 2.
DR Pfam; PF00429; TLV_coat; 3.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 3: Inferred from homology;
KW Disulfide bond; 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..409
FT /note="Glycoprotein 55"
FT /id="PRO_0000040720"
FT TOPO_DOM 33..384
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..409
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 232..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..276
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 409 AA; 44700 MW; 2D12505183293B3A CRC64;
MEGPASSKPL KDKTNPWGPL IILGILIRAG VSVQLDSPHQ VSNVTWRVTN LMTGQTANAT
SLLGTMTEAF PKLYFDLCDL MGDDWDETGL GCRTPGGRKR ARTFDFYVCP GHTVPTGCGG
PREGYCGKWG CETTGQAYWK PSSSWDLISL KRGNTPKDQG PCYDSSVSSG VLGATPGGRC
NPLVLEFTDA GRKASWDAPK VWGLRLYRST GTDPVTRFSL TRQVLDIGPR VPIGSNPVTT
DQLPLSRPVQ TMPPRPLQPP PPGAASIVPE TAPPPQQPGA GDRLLNLVDG AYQALNLTNP
DKIQECWLCL VSGPPYYEGV VVLGTYFNHT IALKEKCCFY ADHTGLVRDS MAKLRKRLTQ
RQKLFESSRG WFEGSSNRSP WFTTLISAIM GSLIILLLLL ILLIWTLYS
