ENV_SMRVH
ID ENV_SMRVH Reviewed; 575 AA.
AC P21412;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 106.
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 Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 20;
DE Short=gp20;
DE Flags: Precursor;
GN Name=env;
OS Squirrel monkey retrovirus (SMRV-H) (SMRV-HLB).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11856;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3201749; DOI=10.1016/s0042-6822(88)90109-2;
RA Oda T., Ikeda S., Watanabe S., Hatsushika M., Akiyama K., Mitsunobu F.;
RT "Molecular cloning, complete nucleotide sequence, and gene structure of the
RT provirus genome of a retrovirus produced in a human lymphoblastoid cell
RT line.";
RL Virology 167:468-476(1988).
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
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 -!- 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. {ECO:0000250}.
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 (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}.
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DR EMBL; M23385; AAA66454.1; -; Genomic_RNA.
DR EMBL; M23385; AAA66455.1; -; Genomic_RNA.
DR PIR; D31827; VCLJHD.
DR RefSeq; NP_041262.1; NC_001514.1.
DR SMR; P21412; -.
DR PRIDE; P21412; -.
DR GeneID; 1491965; -.
DR KEGG; vg:1491965; -.
DR Proteomes; UP000007223; Genome.
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.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 2.
DR Pfam; PF00429; TLV_coat; 1.
PE 3: Inferred from homology;
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..386
FT /note="Surface protein"
FT /id="PRO_0000040801"
FT CHAIN 387..575
FT /note="Transmembrane protein"
FT /id="PRO_0000040802"
FT TOPO_DOM 20..517
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 390..410
FT /note="Fusion peptide"
FT REGION 450..466
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 411..461
FT /evidence="ECO:0000255"
FT COILED 471..507
FT /evidence="ECO:0000255"
FT MOTIF 249..252
FT /note="CXXC"
FT MOTIF 467..475
FT /note="CX6CC"
FT MOTIF 562..565
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT SITE 386..387
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 560..561
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 249..475
FT /note="Interchain (between SU and TM chains, or C-252 with
FT C-475); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 249..252
FT /evidence="ECO:0000250"
FT DISULFID 467..474
FT /evidence="ECO:0000250"
SQ SEQUENCE 575 AA; 62245 MW; 7210DECC53896669 CRC64;
MLCILILLLH PRLCPVTKGG LGKPSGDIYT ALFGAPCDCK GGTQTNNYAT PTYTQVTDCG
DKNAYLTYDT NWNGVSSPKW LCVRKPPSIP VINGRPGPCP SECTNNIKSQ MHSSCYSSFS
QCTQGNNTYF TAILQRTKST SETNPVTSGL QPHGVLQAGC DGTVGKSVCW NQQAPIHVSD
GGGPQDAVRE LYVQKQIELV IQSQFPKLSY HPLARSKPRG PDIDAQMLDI LSATHQALNI
SNPSLAQNCW LCLNQGTSMP LAFPVNISSF NASQNNCTPS LPFRVQPMPS QVYPCFFKGA
QNNSFDIPVG VANFVNCSSS SNHSEALCPG PGQAFVCGNN LAFTALPANW TGSCVLAALL
PDIDIISGDD PVPIPTFDYI AGRQKRAVTL IPLLVGLGVS TAVATGTAGL GVAVQSYTKL
SHQLINDVQA LSSTINDLQD QLDSLAEVVL QNRRGLDLLT AEQGGICLAL QERCCFYANK
SGIVRDKIKN LQEDLEKRRK ALADNLFLTG LNGLLPYLLP FLGPLFAIIL FFSFAPWILR
RVTALIRDQL NSLLGKPIQI HYHQLATRDL EYGRL
