ENV_EIAV5
ID ENV_EIAV5 Reviewed; 860 AA.
AC P22430;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 23-FEB-2022, entry version 93.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 90;
DE Short=gp90;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 45;
DE Short=gp45;
DE Flags: Precursor;
GN Name=env;
OS Equine infectious anemia virus (isolate P3.2-5) (EIAV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11669;
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2825406; DOI=10.1016/0042-6822(87)90124-3;
RA Payne S.L., Fang F.D., Liu C.P., Dhruva B.R., Rwambo P., Issel C.J.,
RA Montelaro R.C.;
RT "Antigenic variation and lentivirus persistence: variations in envelope
RT gene sequences during EIAV infection resemble changes reported for
RT sequential isolates of HIV.";
RL Virology 161:321-331(1987).
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}. 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 -!- 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 EMBL; M18388; AAA66410.1; -; Genomic_RNA.
DR PIR; D34027; VCLJE4.
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:0005198; F:structural molecule activity; IEA:InterPro.
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 CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR InterPro; IPR000328; GP41-like.
DR InterPro; IPR001361; Gp90_EIAV.
DR Pfam; PF00971; EIAV_GP90; 1.
DR Pfam; PF00517; GP41; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Glycoprotein; Host cell membrane; Host membrane; Host-virus interaction;
KW Membrane; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT PROPEP 1..6
FT /evidence="ECO:0000250"
FT /id="PRO_0000239530"
FT CHAIN 7..860
FT /note="Envelope glycoprotein"
FT /id="PRO_0000038711"
FT CHAIN 7..445
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038712"
FT CHAIN 446..860
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038713"
FT TOPO_DOM 7..614
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..860
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 447..467
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 499..514
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT REGION 746..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 577..625
FT /evidence="ECO:0000255"
FT COILED 664..700
FT /evidence="ECO:0000255"
FT COMPBIAS 748..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 445..446
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 685..686
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
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 308
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
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 CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 860 AA; 97021 MW; 0037EB61528EF0DD CRC64;
MVSIAFYGGI PGGISTPITQ QSEKSKCEEN TIFQPYCYNN NSKNSMAESK EARDQEMNLK
EESKEEKRRN DWWKIGMFLL CLAGTTGGIL WWYEGLPQQH YIGLVAIGGR LNGSGQSNAI
ECWGSFPGCR PFQNYFSYET NRSMHMDNDT ATLLEAYHRE ITFIYKSSCT DSDHCQEYQC
KQVNLNSSDP SNSVRVEDVT NTTEYWGFKW LECNQTENFK TILVPENEMV KINDNDTWIP
KGCNETWARV KRCPIDILYG IHPIRLSVQP PFFLVQEKGT ADTSRIGNCG PTIFLGVLED
NKGVVRGNGT ACKVSDLNIN RKDYTGIYQV PIFYTCNFTN ITSCNNESII SVIMYETNQV
QYLLCNNNNN SNNYNCVVQS FGVIGQAHLE LPRPNKRIRN QSFNQYNCSI NNKTELETWK
LVNTSGITPL PISSEANTGL IRHKRDFGIS AIVAAIVAAT AIAASATMSY VALTEVNKIM
EVQNHTFEVE NSTLNGMDLI EQQIKILYAM ILQTHADVQL LKEKQQVEET FNLIGCIERT
HVFCHTGHPW NMSWGHLNES TQWDDWVSKM EDLNQEILTT LHGARNNLAQ SMITFNTPDS
IAQFGKDLWS HIGNWIPGLG ASIIKYIVMF LLIYLLLTSS PKILRALWKV TSGAGSSGSR
YLKKKFYHKH ASREDTWDQA QHNIHLAGVT GGSGNKYCKQ KYSRNDWNGE SEEYNRRPKS
WVKSIETFGE SYISEKTKGE ISQPGAAINE HKNGSGGNNP HQGSLDLEIR SEGGNIYDCC
IKAQEGTLAI PCCGFPLWLF WGLVIIVGRI AGYGLRGFAV IIRICIRGLN LIFEIIRKML
DYIGRALNPG TSHVSMPQYV
