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 28-JAN-2026, entry version 115. 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 Spleen focus-forming virus. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K02375; AAA46505.1; -; Genomic_RNA. DR PIR; A03988; VCMVSR. DR SMR; P03389; -. DR GlyCosmos; P03389; 5 sites, No reported glycans. 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: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:symbiont entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.210; -; 1. DR Gene3D; 3.90.310.10; ENV polyprotein, receptor-binding domain; 1. DR InterPro; IPR008981; FMuLV_rcpt-bd. DR InterPro; IPR018154; TLV/ENV_coat_polyprotein. DR PANTHER; PTHR10424:SF72; BC035947 PROTEIN-RELATED; 1. DR PANTHER; PTHR10424; VIRAL ENVELOPE PROTEIN; 1. DR Pfam; PF00429; TLV_coat; 2. DR SUPFAM; SSF49830; ENV polyprotein, receptor-binding domain; 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 //