ENV_MMTVG
ID ENV_MMTVG Reviewed; 688 AA.
AC P03374;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Envelope glycoprotein gp70;
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 Mouse mammary tumor virus (strain GR) (MMTV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11760;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11894899; DOI=10.1002/j.1460-2075.1983.tb01393.x;
RA Redmond S.M.S., Dickson C.;
RT "Sequence and expression of the mouse mammary tumour virus env gene.";
RL EMBO J. 2:125-131(1983).
RN [2]
RP PROTEIN SEQUENCE OF 684-688, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=6310154; DOI=10.1128/jvi.48.1.314-319.1983;
RA Henderson L.E., Sowder R., Smythers G., Oroszlan S.;
RT "Terminal amino acid sequences and proteolytic cleavage sites of mouse
RT mammary tumor virus env gene products.";
RL J. Virol. 48:314-319(1983).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to its receptor. This interaction triggers the refolding of
CC the transmembrane protein (TM) and is thought to activate its fusogenic
CC potential by unmasking its fusion peptide. Fusion occurs at the host
CC cell plasma membrane (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Membranes fusion leads to
CC delivery of the nucleocapsid into the cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached by noncovalent interactions or by a labile
CC interchain disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the extravirion surface through its
CC binding to TM. Both proteins are thought to be concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC N-glycosylated and processed likely by host cell furin or by a furin-
CC like protease in the Golgi to yield the mature SU and TM proteins. The
CC cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC [KR]-R (By similarity). {ECO:0000250}.
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DR EMBL; X01811; CAA25955.1; -; Genomic_RNA.
DR PIR; A03972; VCMVM.
DR BindingDB; P03374; -.
DR ChEMBL; CHEMBL5825; -.
DR ABCD; P03374; 3 sequenced antibodies.
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:0005198; F:structural molecule activity; IEA:InterPro.
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 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; Direct protein sequencing;
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 membrane; Host-virus interaction; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..98
FT /evidence="ECO:0000250"
FT CHAIN 99..688
FT /note="Envelope glycoprotein gp70"
FT /id="PRO_0000239593"
FT CHAIN 99..454
FT /note="Surface protein"
FT /id="PRO_0000040783"
FT PROPEP 455..456
FT /evidence="ECO:0000250"
FT /id="PRO_0000040784"
FT CHAIN 457..688
FT /note="Transmembrane protein"
FT /id="PRO_0000040785"
FT TOPO_DOM 99..624
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..477
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 463..481
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 426..474
FT /evidence="ECO:0000255"
FT COILED 511..541
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 138
FT /note="Involved in binding to the cell receptor"
FT /evidence="ECO:0000250"
FT SITE 454..455
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 688 AA; 77221 MW; C6F76748B440316D CRC64;
MPNHQSGSPT GSSDLLLSGK KQRPHLALRR KRRREMRKIN RKVRRMNLAP IKEKTAWQHL
QALISEAEEV LKTSQTPQNS LTLFLALLSV LGPPPVTGES YWAYLPKPPI LHPVGWGSTD
PIRVLTNQTM YLGGSPDFHG FRNMSGNVHF EGKSDTLPIC FSFSFSTPTG CFQVDKQVFL
SDTPTVDNNK PGGKGDKRRM WELWLHTLGN SGANTKLVPI KKKLPPKYPH CQIAFKKDAF
WEGDESAPPR WLPCAFPDKG VSFSPKGALG LLWDFSLPSP SVDQSDQIKS KKDLFGNYTP
PVNKEVHRWY EAGWVEPTWF WENSPKDPND RDFTALVPHT ELFRLVAASR HLILKRPGFQ
EHEMIPTSAC VTYPYAILLG LPQLIDIEKR GSTFHISCSS CRLTNCLDSS AYDYAAIIVK
RPPYVLLPVD IGDEPWFDDS AIQTFRYATD LIRAKRFVAA IILGISALIA IITSFAVATT
ALVKEMQTAT FVNNLHRNVT LALSEQRIID LKLEARLNAL EEVVLELGQD VANLKTRMST
RCHANYDFIC VTPLPYNATE DWERTRAHLL GIWNDNEISY NIQELTNLIS DMSKQHIDAV
DLSGLAQSFA NGVKALNPLD WTQYFIFIGV GALLLVIVLM IFPIVFQCLA KSLDQVQSDL
NVLLLKKKKG GNAAPAAEMV ELPRVSYT
