ENV_RSFFV
ID ENV_RSFFV Reviewed; 408 AA.
AC P03389;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Glycoprotein 55;
DE Short=gp55;
DE Flags: Precursor;
GN Name=env;
OS Rauscher spleen focus-forming virus (RSFFV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=11821;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6088793; DOI=10.1128/jvi.51.3.695-705.1984;
RA Bestwick R.K., Boswell B.A., Kabat D.;
RT "Molecular cloning of biologically active Rauscher spleen focus-forming
RT virus and the sequences of its env gene and long terminal repeat.";
RL J. Virol. 51:695-705(1984).
CC -!- FUNCTION: Envelope-like membrane glycoprotein.
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 {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=The envelope-like membrane
CC glycoprotein gp55 is defective in its transport to the cell surface and
CC remains associated predominantly with the rough endoplasmic reticulum
CC (RER) membrane. It is almost not incorporated into virions. Host cell
CC surface expression appears to be a prerequisite for its leukemogenicity
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Compared to other gammaretroviruses which possess 2
CC envelope proteins (gp70 and p15E), RSFFV 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.
CC -!- MISCELLANEOUS: The Rauscher murine leukemia virus complex induces a
CC rapid 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 Rauscher
CC murine leukemia virus (R-MuLV) that serves as a helper virus for SFFV.
CC Spleens of infected mice also contain a third component, the Rauscher
CC mink cell focus-inducing (R-MCF) virus.
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DR EMBL; K02375; AAA46505.1; -; Genomic_RNA.
DR PIR; A03988; VCMVSR.
DR SMR; P03389; -.
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; 2.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 3: Inferred from homology;
KW Coiled coil; 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; 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..408
FT /note="Glycoprotein 55"
FT /id="PRO_0000040795"
FT TOPO_DOM 33..385
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..408
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 256..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..371
FT /evidence="ECO:0000255"
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 297
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 408 AA; 44940 MW; 66383F99BCE9514A CRC64;
MEGPAFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHQ VFNVTWRVTN LMTGQTANAT
SLLGTMTDAF PKLYFDLCDL IGDDWDETGL GCRTPGGRKR ARTFDFYVCP GHTVPTGCGG
PREGYCGKWG CETTGQAYWK PSSSWDLISL KRGNTPRNQG PCYDSSAVSS DIKGATPGGR
CNPLVLEFTD AGKKASWDGP KVWGLRLYRS TGTDPVTRFS LTRQVLNIGP RVPIGPNPVI
TDQLPPSRPV QIMLPRPPQP PPPGAASIVP ETAPPSQQPG TGDRLLNLVD GAYQALNLTN
PDKTQDCWLC LVSGPPYYEG VAVLGTYYNH TSALKEECCF YADHTGLVRD SMAKLRERLT
QRQKLFESSQ GWFEELFNRS TWFTTLIFTI IGPLIILLLI LLFWTLHS
