ENV_IPMAE
ID ENV_IPMAE Reviewed; 584 AA.
AC P31789;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=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;
GN Name=env;
OS Mouse intracisternal a-particle MIAE (IAP-MIAE).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Intracisternal A-particles.
OX NCBI_TaxID=11932;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1920613; DOI=10.1128/jvi.65.11.5702-5709.1991;
RA Reuss F.U., Schaller H.C.;
RT "cDNA sequence and genomic characterization of intracisternal A-particle-
RT related retroviral elements containing an envelope gene.";
RL J. Virol. 65:5702-5709(1991).
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}.
CC -!- MISCELLANEOUS: Readthrough of three terminators occurs: UGA between
CC codons for Thr-71 and Ala-72, UGA between codons for His-110 and Arg-
CC 111, and UAA between codons for Val-392 and Ser-393.
CC -!- MISCELLANEOUS: This particle is a defective retrovirus.
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DR EMBL; M73818; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A41305; VCMSIA.
DR PRIDE; P31789; -.
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.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Coiled coil; 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 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..584
FT /note="Envelope glycoprotein"
FT /id="PRO_0000040733"
FT CHAIN 29..362
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040734"
FT CHAIN 363..584
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040735"
FT TOPO_DOM 29..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 364..384
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 391..441
FT /evidence="ECO:0000255"
FT COILED 477..513
FT /evidence="ECO:0000255"
FT SITE 362..363
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
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"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 584 AA; 65025 MW; 180CCAF8F14A4CD6 CRC64;
MVQKMLTSRG LFLILTMLNL SQVPSIMGEQ RWAILSTFPK PMPVRHDAIV FPKFFTTNKT
VDLPYLLYDP TAPLGENRSL LEQGSLCFQI NGPGNCINLT ARALGKFNEH RGWVSTTQDT
SNVEITFTNR TFWQEVNWVN GTFLPPNFSD KEHLHQPKIA PHCSLEDEGL ILPWSDCQSS
IIRWVDQSKT FSFSPNMIDD PEKEFVMKKG LFIQDFRMHP FHKWVLCGVN GSCTELNPLI
FIQGGAVGKA SFTGISRFAQ YWGIHDASQD SYGYTNTSVE ITGFNKTLVN QINYPSTPVC
VYPPFLFILS NDSFEVCSND SCWISQCWDV TKNTRAMVAR IPRWIPVPVE TPSTLSMFRQ
KRDFGITAAM IIAISASAAA ATAAGYAMVS AVSGTKLNQL SADLADAITV QTSASTKLKG
GLMILNQCLD LAEEQIGVLH QMAQLGCERK LEALCITSVQ YENFTYAANL SRQLSLYLAG
NWSERFDETL EALIAAVLKI NSTRMDLSLT EGLSSWISSA FSYFKEWVGV GLFGVATCCG
LVVMLWLVCK LRTQQTRDKV VITQALAAIE QGASPEIWLS MLKN
