ENV_FRSF5
ID ENV_FRSF5 Reviewed; 409 AA.
AC P03393;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Glycoprotein 55;
DE Short=gp55;
DE Flags: Precursor;
GN Name=env;
OS Friend spleen focus-forming virus (isolate 502) (FSFFV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=355329;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6576374; DOI=10.1073/pnas.80.16.5037;
RA Clark S.P., Mak T.W.;
RT "Complete nucleotide sequence of an infectious clone of Friend spleen
RT focus-forming provirus: gp55 is an envelope fusion glycoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:5037-5041(1983).
RN [2]
RP CHARACTERIZATION.
RX PubMed=2159537; DOI=10.1128/jvi.64.6.2678-2686.1990;
RA Watanabe N., Nishi M., Ikawa Y., Amanuma H.;
RT "A deletion in the Friend spleen focus-forming virus env gene is necessary
RT for its product (gp55) to be leukemogenic.";
RL J. Virol. 64:2678-2686(1990).
RN [3]
RP ERRATUM OF PUBMED:2159537.
RA Watanabe N., Nishi M., Ikawa Y., Amanuma H.;
RL J. Virol. 64:5694-5694(1990).
RN [4]
RP REVIEW.
RX PubMed=11090047;
RA Ney P.A., D'Andrea A.D.;
RT "Friend erythroleukemia revisited.";
RL Blood 96:3675-3680(2000).
RN [5]
RP FUNCTION, AND INTERACTION WITH MOUSE MST1R ISOFORM SF-STK.
RX PubMed=11483734; DOI=10.1128/jvi.75.17.7893-7903.2001;
RA Nishigaki K., Thompson D., Hanson C., Yugawa T., Ruscetti S.;
RT "The envelope glycoprotein of friend spleen focus-forming virus covalently
RT interacts with and constitutively activates a truncated form of the
RT receptor tyrosine kinase Stk.";
RL J. Virol. 75:7893-7903(2001).
RN [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH MOUSE EPOR.
RX PubMed=12930840; DOI=10.1074/jbc.m302974200;
RA Constantinescu S.N., Keren T., Russ W.P., Ubarretxena-Belandia I.,
RA Malka Y., Kubatzky K.F., Engelman D.M., Lodish H.F., Henis Y.I.;
RT "The erythropoietin receptor transmembrane domain mediates complex
RT formation with viral anemic and polycythemic gp55 proteins.";
RL J. Biol. Chem. 278:43755-43763(2003).
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. {ECO:0000269|PubMed:11483734,
CC ECO:0000269|PubMed:12930840}.
CC -!- SUBUNIT: Homooligomer (Probable). Forms heterooligomers with mouse
CC EPOR, probably via their respective transmembrane domains. Forms
CC covalent heterodimers with mouse MST1R isoform sf-Stk, probably via
CC disulfide bonds. {ECO:0000269|PubMed:12930840, ECO:0000305}.
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
CC leukemogenicity.
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; K00021; AAA46487.1; -; Genomic_RNA.
DR PIR; A03993; VCVW5S.
DR RefSeq; NP_041218.1; NC_001500.1.
DR SMR; P03393; -.
DR GlyConnect; 128; 2 N-Linked glycans.
DR GlyConnect; 129; 7 N-Linked glycans, 1 O-Linked glycan.
DR GlyConnect; 130; 4 N-Linked glycans, 1 O-Linked glycan.
DR GlyConnect; 131; 4 N-Linked glycans, 1 O-Linked glycan.
DR GlyConnect; 132; 4 N-Linked glycans.
DR GlyConnect; 133; 4 N-Linked glycans.
DR GlyConnect; 134; 2 N-Linked glycans, 3 O-Linked glycans.
DR GlyConnect; 135; 1 N-Linked glycan, 2 O-Linked glycans.
DR GlyConnect; 136; 1 N-Linked glycan, 2 O-Linked glycans.
DR GeneID; 1491889; -.
DR KEGG; vg:1491889; -.
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 1: Evidence at protein level;
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_0000040718"
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 254..280
FT /note="Disordered"
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; 44777 MW; 407F56F769863D74 CRC64;
MKGPAFSKPL KDKINPWGPL IVLGILIRAG VSVQHDSPHQ VFNVTWRVTN LMTGQTANAT
SLLGTMTDAF PMLHFDLCDL IGDDWDETGL ECRTPGGRKR ARTFDFYVCP GHTVPTGCGG
PREGYCGKWG CETTGQAYWK PSSSWDLISL KRGNTPKDRG PCYDSSVSSG VQGATPGGRC
NPLVLKFTDA GKKASWDSPK VWGLRLYRPT GIDPVTRFSL TRQVLNIGPR IPIGPNPVII
GQLPPSRPVQ VRLPRPPQPP PTGAASMVPG TAPPSQQPGT GDRLLNLVQG AYQALNLTNP
DKTQECWLCL VSGPPYYEGV AVLGTNSNHT SALKEKCCFY ADHTGLVRDS MAKLRKRLTQ
RQKLFESSQG WFEGSFNRSP WFTTLISTIM GLLIILLLLL ILLLWTLHS
