ENV_HTL1M
ID ENV_HTL1M Reviewed; 488 AA.
AC P23064;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Envelope glycoprotein gp62;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 46;
DE Short=gp46;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 21;
DE Short=gp21;
DE Flags: Precursor;
GN Name=env;
OS Human T-cell leukemia virus 1 (strain Japan MT-2 subtype A) (HTLV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11928;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2353464; DOI=10.1016/0042-6822(90)90498-g;
RA Gray G.S., White M., Bartman T., Mann D.;
RT "Envelope gene sequence of HTLV-1 isolate MT-2 and its comparison with
RT other HTLV-1 isolates.";
RL Virology 177:391-395(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Astier-Gin T., Guillemain B.;
RL Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERCHAIN DISULFIDE BOND.
RX PubMed=14685283; DOI=10.1038/sj.emboj.7600012;
RA Wallin M., Ekstroem M., Garoff H.;
RT "Isomerization of the intersubunit disulphide-bond in Env controls
RT retrovirus fusion.";
RL EMBO J. 23:54-65(2004).
RN [4]
RP FUNCTION OF THE GLYCINE-RICH REGION, AND MUTAGENESIS OF GLY-327; GLY-329;
RP VAL-330; GLY-332; GLY-333; ILE-334 AND GLY-336.
RX PubMed=15767455; DOI=10.1128/jvi.79.7.4533-4539.2005;
RA Wilson K.A., Baer S., Maerz A.L., Alizon M., Poumbourios P.;
RT "The conserved glycine-rich segment linking the N-terminal fusion peptide
RT to the coiled coil of human T-cell leukemia virus type 1 transmembrane
RT glycoprotein gp21 is a determinant of membrane fusion function.";
RL J. Virol. 79:4533-4539(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 338-425, AND DISULFIDE BOND.
RX PubMed=10200260; DOI=10.1073/pnas.96.8.4319;
RA Kobe B., Center R.J., Kemp B.E., Poumbourios P.;
RT "Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain
RT crystallized as a maltose-binding protein chimera reveals structural
RT evolution of retroviral transmembrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4319-4324(1999).
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}. Note=It is probably concentrated at the site of budding
CC and incorporated into the virions possibly by contacts between the
CC cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Host cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The
CC surface protein is not anchored to the viral envelope, but associates
CC with the extravirion surface through its binding to TM. It is probably
CC concentrated at the site of budding and incorporated into the virions
CC possibly by contacts between the cytoplasmic tail of Env and the N-
CC terminus of Gag (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The glycine-rich region of transmembrane protein is involved in
CC membrane fusion.
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.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: HTLV-1 lineages are divided in four clades, A
CC (Cosmopolitan), B (Central African group), C (Melanesian group) and D
CC (New Central African group).
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DR EMBL; M37747; AAA46185.1; -; Genomic_RNA.
DR EMBL; X56949; CAA40263.2; -; Genomic_DNA.
DR PIR; A35323; VCLJMT.
DR PIR; S14605; S14605.
DR SMR; P23064; -.
DR TCDB; 1.G.17.1.4; the bovine leukemia virus envelop glycoprotein (blv-env) family.
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; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 1: Evidence at protein 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; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..488
FT /note="Envelope glycoprotein gp62"
FT /id="PRO_0000038755"
FT CHAIN 21..312
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038756"
FT CHAIN 313..488
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038757"
FT TOPO_DOM 21..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 313..333
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 327..339
FT /note="Gly-rich"
FT REGION 376..392
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 340..385
FT COILED 397..429
FT /evidence="ECO:0000255"
FT MOTIF 225..228
FT /note="CXXC"
FT MOTIF 393..401
FT /note="CX6CC"
FT SITE 312..313
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT LIPID 462
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 225..401
FT /note="Interchain (between SU and TM chains, or C-228 with
FT C-401); in linked form"
FT /evidence="ECO:0000269|PubMed:10200260"
FT DISULFID 225..228
FT /evidence="ECO:0000269|PubMed:10200260"
FT DISULFID 393..400
FT /evidence="ECO:0000250"
FT MUTAGEN 327
FT /note="G->A: 10% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 327
FT /note="G->P: 85% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 329
FT /note="G->A: 25% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 329
FT /note="G->P: 80% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 330
FT /note="V->A: 30% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 332
FT /note="G->A: 40% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 332
FT /note="G->P: 85% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 333
FT /note="G->P: 85% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 334
FT /note="I->A: 90% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT MUTAGEN 336
FT /note="G->P: 85% loss of transmembrane protein cell-cell
FT fusion activity."
FT /evidence="ECO:0000269|PubMed:15767455"
FT CONFLICT 341
FT /note="A -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 53856 MW; F89B6FEE8A8B06AF CRC64;
MGKFLATLIL FFQFCPLILG DYSPSCCTLT IGVSSYHSKP CNPAQPVCSW TLDLLALSAD
QALQPPCPNL VSYSSYHATY SLYLFPHWIK KPNRNGGGYY SASYSDPCSL KCPYLGCQSW
TCPYTGAVSS PYWKFQQDVN FTQEVSRLNI NLHFSKCGFP FSLLVDAPGY DPIWFLNTEP
SQLPPTAPPL LPHSNLDHIL EPSIPWKSKL LTLVQLTLQS TNYTCIVCID RASLSTWHVL
YSPNVSVPSS SSTPLLYPSL ALPAPHLTLP FNWTHCFDPQ IQAIVSSPCH NSLILPPFSL
SPVPTLGSRS RRAVPVAVWL VSALAMGAGV AGGITGSMSL ASGKSLLHEV DKDISQLTQA
IVKNHKNLLK IAQYAAQNRR GLDLLFWEQG GLCKALQEQC CFLNITNSHV SILQERPPLE
NRVLTGWGLN WDLGLSQWAR EALQTGITLV ALLLLVILAG PCILRQLRHL PSRVRYPHYS
LINPESSL
