ENV_HTLV2
ID ENV_HTLV2 Reviewed; 486 AA.
AC P03383; P03382;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Envelope glycoprotein gp63;
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 2 (HTLV-2).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11909;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2582407; DOI=10.1073/pnas.82.10.3101;
RA Shimotohno K., Takahashi Y., Shimizu N., Gojobori T., Golde D.W.,
RA Chen I.S.Y., Miwa M., Sugimura T.;
RT "Complete nucleotide sequence of an infectious clone of human T-cell
RT leukemia virus type II: an open reading frame for the protease gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3101-3105(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6204380; DOI=10.1126/science.6204380;
RA Sodroski J., Patarca R., Perkins D., Briggs D., Lee T.-H., Essex M.,
RA Coligan J., Wong-Staal F., Gallo R.C., Haseltine W.A.;
RT "Sequence of the envelope glycoprotein gene of type II human T lymphotropic
RT virus.";
RL Science 225:421-424(1984).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN BY FURIN.
RX PubMed=12487813; DOI=10.1089/088922202320886299;
RA Hasegawa H., Tatsumi M., Ogawa-Goto K., Takahashi H., Kojima A.,
RA Iwasaki T., Kurata T., Sata T., Takeuchi T., Sheehy N., Sawa H.,
RA Nagashima K., Hall W.W.;
RT "Processing of the HTLV-II envelope precursor glycoprotein gp62 by furin is
RT essential for cell fusion activity.";
RL AIDS Res. Hum. Retroviruses 18:1253-1260(2002).
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 -!- INTERACTION:
CC P03383; O43513: MED7; Xeno; NbExp=3; IntAct=EBI-9676086, EBI-394632;
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 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}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
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DR EMBL; M10060; AAB59887.1; -; Genomic_DNA.
DR EMBL; K02024; AAA45410.1; -; Genomic_RNA.
DR PIR; A03980; VCLJT2.
DR PIR; A03981; VCLJH2.
DR RefSeq; NP_041006.1; NC_001488.1.
DR SMR; P03383; -.
DR ELM; P03383; -.
DR IntAct; P03383; 1.
DR MINT; P03383; -.
DR PRIDE; P03383; -.
DR GeneID; 1491942; -.
DR KEGG; vg:1491942; -.
DR Proteomes; UP000009254; 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; 1.
DR Pfam; PF00429; TLV_coat; 2.
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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..486
FT /note="Envelope glycoprotein gp63"
FT /id="PRO_0000239544"
FT CHAIN 19..308
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038761"
FT CHAIN 309..486
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038762"
FT TOPO_DOM 19..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 309..329
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 372..388
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 337..383
FT /evidence="ECO:0000255"
FT COILED 393..425
FT /evidence="ECO:0000255"
FT MOTIF 221..224
FT /note="CXXC"
FT MOTIF 389..397
FT /note="CX6CC"
FT SITE 308..309
FT /note="Cleavage; by host furin"
FT LIPID 458
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 221..397
FT /note="Interchain (between SU and TM chains, or C-224 with
FT C-397); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 221..224
FT /evidence="ECO:0000250"
FT DISULFID 389..396
FT /evidence="ECO:0000250"
FT CONFLICT 27
FT /note="I -> V (in Ref. 2; AAA45410)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="D -> H (in Ref. 2; AAA45410)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> S (in Ref. 2; AAA45410)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..119
FT /note="SA -> CP (in Ref. 2; AAA45410)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="F -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="P -> L (in Ref. 2; AAA45410)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="S -> P (in Ref. 2; AAA45410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 54158 MW; 60D70B9CE8986CE5 CRC64;
MGNVFFLLLF SLTHFPLAQQ SRCTLTIGIS SYHSSPCSPT QPVCTWNLDL NSLTTDQRLH
PPCPNLITYS GFHKTYSLYL FPHWIKKPNR QGLGYYSPSY NDPCSLQCPY LGCQAWTSAY
TGPVSSPSWK FHSDVNFTQE VSQVSLRLHF SKCGSSMTLL VDAPGYDPLW FITSEPTQPP
PTSPPLVHDS DLEHVLTPST SWTTKILKFI QLTLQSTNYS CMVCVDRSSL SSWHVLYTPN
ISIPQQTSSR TILFPSLALP APPSQPFPWT HCYQPRLQAI TTDNCNNSII LPPFSLAPVP
PPATRRRRAV PIAVWLVSAL AAGTGIAGGV TGSLSLASSK SLLLEVDKDI SHLTQAIVKN
HQNILRVAQY AAQNRRGLDL LFWEQGGLCK AIQEQCCFLN ISNTHVSVLQ ERPPLEKRVI
TGWGLNWDLG LSQWAREALQ TGITILALLL LVILFGPCIL RQIQALPQRL QNRHNQYSLI
NPETML
