ENV1_MOUSE
ID ENV1_MOUSE Reviewed; 641 AA.
AC P10404; Q78N71; Q78N73; Q78N94; Q80SW7; Q80SW8; Q80SY0; Q80SY1; Q811M9;
AC Q811N4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=MLV-related proviral Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE Flags: Precursor;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NFS;
RX PubMed=12970417; DOI=10.1128/jvi.77.19.10327-10338.2003;
RA Evans L.H., Lavignon M., Taylor M., Alamgir A.S.;
RT "Antigenic subclasses of polytropic murine leukemia virus (MLV) isolates
RT reflect three distinct groups of endogenous polytropic MLV-related
RT sequences in NFS/N mice.";
RL J. Virol. 77:10327-10338(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-313.
RC STRAIN=129;
RX PubMed=2415714; DOI=10.1128/jvi.56.3.691-700.1985;
RA Levy D.E., Lerner R.A., Wilson M.C.;
RT "Normal expression of polymorphic endogenous retroviral RNA containing
RT segments identical to mink cell focus-forming virus.";
RL J. Virol. 56:691-700(1985).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 a labile interchain disulfide bond.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-
CC pass type I membrane protein. Cell membrane; Single-pass type I
CC membrane protein. Note=The surface protein is not anchored to the viral
CC 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. R-
CC peptide: Cell membrane; peripheral membrane protein. The R-peptide is
CC membrane-associated through its palmitate (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Cell membrane; Peripheral membrane protein. Note=The
CC surface protein is not anchored to the viral envelope, but associates
CC with the extravirion surface through its binding to TM. Both proteins
CC are thought to be concentrated at the site of budding and incorporated
CC into the virions possibly by contacts between the cytoplasmic tail of
CC Env and the N-terminus of Gag. R-peptide: Cell membrane; peripheral
CC membrane protein. The R-peptide is membrane-associated through its
CC palmitate (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC viral release at the surface of infected mononuclear cells and promotes
CC endocytosis.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By 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. The R-peptide is released from the C-terminus of the
CC cytoplasmic tail of the TM protein upon particle formation as a result
CC of proteolytic cleavage by the viral protease. Cleavage of this peptide
CC is required for TM to become fusogenic (By similarity). {ECO:0000250}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion (By
CC similarity). {ECO:0000250}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
CC -!- CAUTION: This polyprotein is encoded by an endogenous retrovirus
CC expressed in some mouse strains. Multiple sequences are present in
CC different regions of the genome, probably reflecting the different
CC sites of integration of the exogenous retrovirus. {ECO:0000305}.
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DR EMBL; AY219544; AAO37244.2; -; Genomic_DNA.
DR EMBL; AY219545; AAO37246.2; -; Genomic_DNA.
DR EMBL; AY219546; AAO37248.2; -; Genomic_DNA.
DR EMBL; AY219547; AAO37250.2; -; Genomic_DNA.
DR EMBL; AY219548; AAO37252.2; -; Genomic_DNA.
DR EMBL; AY219550; AAO37255.2; -; Genomic_DNA.
DR EMBL; AY219551; AAO37257.2; -; Genomic_DNA.
DR EMBL; AY219554; AAO37261.2; -; Genomic_DNA.
DR EMBL; AY219557; AAO37265.2; -; Genomic_DNA.
DR EMBL; AY219558; AAO37267.2; -; Genomic_DNA.
DR EMBL; AY219564; AAO37279.2; -; Genomic_DNA.
DR EMBL; AY219566; AAO37283.2; -; Genomic_DNA.
DR EMBL; AY219567; AAO37285.2; -; Genomic_DNA.
DR EMBL; M11301; AAA37561.1; -; mRNA.
DR PDB; 4JGS; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I=469-564.
DR PDBsum; 4JGS; -.
DR AlphaFoldDB; P10404; -.
DR SMR; P10404; -.
DR IntAct; P10404; 1.
DR GlyGen; P10404; 5 sites.
DR SwissPalm; P10404; -.
DR CPTAC; non-CPTAC-3575; -.
DR EPD; P10404; -.
DR jPOST; P10404; -.
DR MaxQB; P10404; -.
DR PeptideAtlas; P10404; -.
DR PRIDE; P10404; -.
DR TopDownProteomics; P10404; -.
DR InParanoid; P10404; -.
DR PRO; PR:P10404; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P10404; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; 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; 1.
DR Pfam; PF00429; TLV_coat; 2.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cleavage on pair of basic residues;
KW Coiled coil; Disulfide bond; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion; Zinc.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..440
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000021186"
FT CHAIN 441..641
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000295257"
FT TOPO_DOM 33..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 256..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..463
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 509..525
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 471..520
FT /evidence="ECO:0000255"
FT COILED 530..566
FT /evidence="ECO:0000255"
FT MOTIF 307..310
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 526..534
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT MOTIF 626..629
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT SITE 440..441
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT LIPID 601
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..126
FT /evidence="ECO:0000250"
FT DISULFID 118..131
FT /evidence="ECO:0000250"
FT DISULFID 307..534
FT /note="Interchain (between SU and TM chains, or C-337 with
FT C-558); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 307..310
FT /evidence="ECO:0000250"
FT DISULFID 337..391
FT /evidence="ECO:0000250"
FT DISULFID 356..368
FT /evidence="ECO:0000250"
FT DISULFID 398..411
FT /evidence="ECO:0000250"
FT DISULFID 526..533
FT /evidence="ECO:0000250"
FT VARIANT 22
FT /note="V -> I"
FT VARIANT 24
FT /note="G -> R"
FT VARIANT 153
FT /note="R -> G"
FT VARIANT 157
FT /note="Q -> R"
FT VARIANT 268
FT /note="I -> T"
FT VARIANT 280
FT /note="G -> E"
FT VARIANT 339
FT /note="V -> A"
FT VARIANT 349
FT /note="E -> K"
FT VARIANT 358
FT /note="G -> R"
FT VARIANT 434
FT /note="R -> K"
FT VARIANT 458
FT /note="G -> D"
FT VARIANT 491
FT /note="E -> K"
FT VARIANT 514
FT /note="G -> R"
FT VARIANT 524
FT /note="G -> R"
FT VARIANT 531
FT /note="E -> K"
FT VARIANT 546
FT /note="S -> N"
FT VARIANT 548
FT /note="A -> T"
FT VARIANT 552
FT /note="E -> K"
FT VARIANT 636
FT /note="E -> K"
FT HELIX 477..518
FT /evidence="ECO:0007829|PDB:4JGS"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:4JGS"
FT HELIX 525..529
FT /evidence="ECO:0007829|PDB:4JGS"
FT HELIX 540..556
FT /evidence="ECO:0007829|PDB:4JGS"
SQ SEQUENCE 641 AA; 69613 MW; C39BF1C2F7B4063F CRC64;
MEGPAFSKPL KDKINPWGPL IVLGILIRAG VSVQHDSPHQ VFNVTWRVTN LMTGQTANAT
SLLGTMTDAF PKLYFDLCDL IGDDWDETGL GCRTPGGRKR ARTFDFYVCP GHTVPTGCGG
PREGYCGKWG CETTGQAYWK PSSSWDLISL KRRNTPQNQG PCYDSSAVSS DIKGATPGGR
CNPLVLEFTD AGKKASWDGP KVWGLRLYRS TGTDPVTRFS LTRQVLNIGP RVPIGPNPVI
TDQLPPSRPV QIMLPRPPQP PPPGAASIVP ETAPPSQQPG TGDRLLNLVD GAYQALNLTS
PDKTQECWLC LVAGPPYYEG VAVLGTYSNH TSAPANCSVA SQHKLTLSEV TGQGLCVGAV
PKTHQALCNT TQKTSDGSYY LAAPAGTIWA CNTGLTPCLS TTVLDLTTDY CVLVELWPKV
TYHSPGYVYG QFERKTKYKR EPVSLTLALL LGGLTMGGIA AGVGTGTTAL VATKQFEQLQ
AAIHTDLGAL EKSVSALEKS LTSLSEVVLQ NRRGLDLLFL KEGGLCAALK EECCFYADHT
GVVRDSMAKL RERLNQRQKL FESGQGWFEG LFNRSPWFTT LISTIMGPLI ILLLILLFGP
CILNRLVQFV KDRISVVQAL VLTQQYHQLK SIDPEEVESR E
