ENV_JSRV
ID ENV_JSRV Reviewed; 615 AA.
AC P31621;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 52;
DE Short=gp52;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 36;
DE Short=gp36;
DE Flags: Precursor;
GN Name=env;
OS Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus) (JSRV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11746;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1629959; DOI=10.1128/jvi.66.8.4930-4939.1992;
RA York D.F., Vigne R., Verwoerd D.W., Querat G.;
RT "Nucleotide sequence of the jaagsiekte retrovirus, an exogenous and
RT endogenous type D and B retrovirus of sheep and goats.";
RL J. Virol. 66:4930-4939(1992).
RN [2]
RP INTERACTION WITH SHEEP HYAL2 RECEPTOR.
RX PubMed=11296287; DOI=10.1073/pnas.071572898;
RA Rai S.K., Duh F.-M., Vigdorovich V., Danilkovitch-Miagkova A., Lerman M.I.,
RA Miller A.D.;
RT "Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-
RT anchored cell-surface receptor for jaagsiekte sheep retrovirus, the
RT envelope protein of which mediates oncogenic transformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4443-4448(2001).
RN [3]
RP FUNCTION.
RX PubMed=11991967; DOI=10.1128/jvi.76.11.5387-5394.2002;
RA Alberti A., Murgia C., Liu S.-L., Mura M., Cousens C., Sharp M.,
RA Miller A.D., Palmarini M.;
RT "Envelope-induced cell transformation by ovine betaretroviruses.";
RL J. Virol. 76:5387-5394(2002).
RN [4]
RP FUNCTION.
RX PubMed=12676986; DOI=10.1073/pnas.0837136100;
RA Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D., Liu S.-L.,
RA Miller A.D., Lerman M.I.;
RT "Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and
RT mediates transformation of epithelial cells by jaagsiekte sheep
RT retrovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003).
RN [5]
RP DOMAIN, AND SIGNAL SEQUENCE.
RX PubMed=15367614; DOI=10.1128/jvi.78.19.10479-10489.2004;
RA Hofacre A., Fan H.;
RT "Multiple domains of the Jaagsiekte sheep retrovirus envelope protein are
RT required for transformation of rodent fibroblasts.";
RL J. Virol. 78:10479-10489(2004).
RN [6]
RP FUNCTION.
RX PubMed=15613321; DOI=10.1128/jvi.79.2.927-933.2005;
RA Liu S.-L., Miller A.D.;
RT "Transformation of madin-darby canine kidney epithelial cells by sheep
RT retrovirus envelope proteins.";
RL J. Virol. 79:927-933(2005).
CC -!- FUNCTION: The envelope proteins induce cell transformation leading to
CC ovine pulmonary adenocarcinoma (OPA), a contagious lung cancer of sheep
CC and goat. They bind to the HYAL2 receptor for cell entry. Env proteins
CC probably do not act as oncogenes by themselves, but may rather liberate
CC an oncogenic factor that would normally be negatively regulated. One
CC mechanism of transformation seems to involve activation of the
CC phosphoinositide-3-OH kinase (PI3K)/Akt pathway but does not involve
CC the virus receptor HYAL2, and the other seems to involve Env binding to
CC HYAL2, HYAL2 degradation, and activation of the MST1R receptor tyrosine
CC kinase, which is normally suppressed by HYAL2.
CC {ECO:0000269|PubMed:11991967, ECO:0000269|PubMed:12676986,
CC ECO:0000269|PubMed:15613321}.
CC -!- SUBUNIT: Interacts with sheep HYAL2 receptor.
CC {ECO:0000269|PubMed:11296287}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=The surface protein is
CC not anchored to the viral envelope, but associates with the extravirion
CC surface through its binding to TM. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- DOMAIN: Both SU and TM seem to be involved in efficient transformation.
CC The cytoplasmic tail of TM is necessary for the transformation.
CC {ECO:0000269|PubMed:15367614}.
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DR EMBL; M80216; AAA89184.1; -; Genomic_RNA.
DR PIR; E42740; VCMVJA.
DR RefSeq; NP_041188.1; NC_001494.1.
DR GeneID; 1490021; -.
DR KEGG; vg:1490021; -.
DR Proteomes; UP000007215; Genome.
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:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
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:0016032; P:viral process; IDA:CACAO.
DR CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR InterPro; IPR000328; GP41-like.
DR Pfam; PF00517; GP41; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Coiled coil;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host-virus interaction; Membrane; Oncogene; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..84
FT /evidence="ECO:0000255"
FT CHAIN 85..615
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239241"
FT CHAIN 85..378
FT /note="Surface protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040737"
FT CHAIN 379..615
FT /note="Transmembrane protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040738"
FT TOPO_DOM 85..378
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 590..593
FT /note="Required for cell transformation"
FT COILED 411..461
FT /evidence="ECO:0000255"
FT COILED 495..531
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 615 AA; 69343 MW; DC48EF0A002CD0AC CRC64;
MPKRRAGFRK GWYARQRNSL THQMQRMTLS EPTSELPTQR QIEALMPYAW NEAHVQPPVT
PTNILIMLLL LLQRVQNGAA AAFWAYIPDP PMIQSLGWDR EIVPVYVNDT SLLGGKSDIH
ISPQQANISF YGLTTQYPMC FSYQSQHPHC IQVSADISYP RVTISGIDEK TGKKSYGNGT
GPLDIPFCDK HLSIGIGIDT PWTLCRARVA SVYNINNANA TFLWDWAPGG TPDFPEYRGQ
HPPIFSVNTA PIYQTELWKL LAAFGHGNSL YLQPNISGTK YGDVGVTGFL YPRACVPYPF
MLIQGHMEIT LSLNIYHLNC SNCILTNCIR GVAKGEQVII VKQPAFVMLP VEIAEAWYDE
TALELLQRIN TALSRPKRGL SLIILGIVSL ITLIATAVTA CVSLAQSIQA AHTVDSLSYN
VTKVMGTQED IDKKIEDRLS ALYDVVRVLG EQVQSINFRM KIQCHANYKW ICVTKKPYNT
SDFPWDKVKK HLQGIWFNTN LSLDLLQLHN EILDIENSPK ATLNIADTVD NFLQNLFSNF
PSLHSLWKTL IGLGIFVIII AIVIFVFPCV VRGLVRDFLK MRVEMLHMKY RTMLQHRHLM
ELLKNKERGA AGDDP
