ENV_MLVFR
ID ENV_MLVFR Reviewed; 445 AA.
AC P03395;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 70;
DE Short=gp70;
DE Flags: Fragment;
GN Name=env;
OS Friend murine leukemia virus (FrMLV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11795;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=6310544; DOI=10.1073/pnas.79.19.5788;
RA Chen R.;
RT "Complete amino acid sequence and glycosylation sites of glycoprotein gp71A
RT of Friend murine leukemia virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:5788-5792(1982).
RN [2]
RP GLYCOSYLATION AT ASN-12; ASN-168; ASN-266; THR-268; SER-273; SER-275;
RP THR-277; THR-279; ASN-302; THR-304; THR-309; ASN-334; ASN-341; ASN-374 AND
RP ASN-410.
RX PubMed=2298213; DOI=10.1111/j.1432-1033.1990.tb15281.x;
RA Geyer R., Dabrowski J., Dabrowski U., Linder D., Schlueter M.,
RA Schott H.-H., Stirm S.;
RT "Oligosaccharides at individual glycosylation sites in glycoprotein 71 of
RT Friend murine leukemia virus.";
RL Eur. J. Biochem. 187:95-110(1990).
RN [3]
RP DISULFIDE BONDS, AND SEQUENCE REVISION TO 184.
RX PubMed=1730242; DOI=10.1111/j.1432-1033.1992.tb19828.x;
RA Linder M., Linder D., Hahnen J., Schott H.-H., Stirm S.;
RT "Localization of the intrachain disulfide bonds of the envelope
RT glycoprotein 71 from Friend murine leukemia virus.";
RL Eur. J. Biochem. 203:65-73(1992).
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 -!- 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: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane; Peripheral membrane protein.
CC Note=The surface protein is not anchored to the viral envelope, but
CC associates with the virion surface through its binding to TM.
CC {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 PIR; S20285; VCFMLV.
DR SMR; P03395; -.
DR GlyConnect; 315; 50 N-Linked glycans (8 sites), 2 O-Linked glycans (7 sites).
DR iPTMnet; P03395; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:0046872; F:metal ion binding; 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: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; 1.
DR Pfam; PF00429; TLV_coat; 1.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond;
KW 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 Metal-binding; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell;
KW Zinc.
FT CHAIN <1..>445
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239584"
FT CHAIN 1..445
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000125471"
FT TOPO_DOM 1..>445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 253..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 312..315
FT /note="CXXC"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000083"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000084"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000085"
FT CARBOHYD 268
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000086"
FT CARBOHYD 273
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000087"
FT CARBOHYD 275
FT /note="O-linked (GalNAc...) serine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000088"
FT CARBOHYD 277
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000089"
FT CARBOHYD 279
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000090"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000091"
FT CARBOHYD 304
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000092"
FT CARBOHYD 309
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000093"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host; alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host;
FT alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine; by host; alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host; alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host;
FT alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine; by host; alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine; by host"
FT /evidence="ECO:0000269|PubMed:2298213"
FT /id="CAR_000096"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host; alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) (polylactosaminoglycan)
FT asparagine; by host; alternate"
FT /evidence="ECO:0000269|PubMed:2298213"
FT DISULFID 46..98
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 72..87
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 73..83
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 121..141
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 133..146
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 178..184
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 312..315
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 342..396
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 361..373
FT /evidence="ECO:0000269|PubMed:1730242"
FT DISULFID 403..416
FT /evidence="ECO:0000269|PubMed:1730242"
FT NON_TER 1
FT NON_TER 445
SQ SEQUENCE 445 AA; 48615 MW; FB30083E491E8975 CRC64;
AAPGSSPHQV YNITWEVTNG DRETVWAISG NHPLWTWWPV LTPDLCMLAL HGPPHWGLEY
QAPYSSPPGP PCCSGSGGSS PGCSRDCNEP LTSLTPRCNT AWNRLKLDQV THKSSEGFYV
CPGSHRPREA KSCGGPDSFY CASWGCETTG RAYWKPSSSW DYITVDNNLT TNQAVQVCKD
NKWCNPLAIQ FTNAGRQVTS WITGHYWGLR LYVSGQDPGL TFGIRLKYQN LGPRVPIGPN
PVLADQLSFP LPNPLPKPAK SPPVSNSTPT MISPSPTPTQ PPPAGTGDRL LNLVQGAYQA
LNLTNPDKTQ ECWLCLVSGP PYYEGVAVLG TYSNHTSAPT NCSVASQHKL TLSEVTGRGL
CIGTVPKTHQ ALCNTTLKTN KGSYYLVAPA GTTWACNTGL TPCLSATVLN RTTDYCVLVE
LWPRVTYHPP SYVYSQFEKS YRHKR
