ENV_FIVT2
ID ENV_FIVT2 Reviewed; 855 AA.
AC Q02282;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 02-DEC-2020, entry version 97.
DE RecName: Full=Envelope glycoprotein gp150;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 100;
DE Short=gp100;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 36;
DE Short=gp36;
GN Name=env;
OS Feline immunodeficiency virus (isolate TM2) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=31676;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1649349; DOI=10.1128/jvi.65.8.4539-4542.1991;
RA Kiyomasu T., Miyazawa T., Furuya T., Shibata R., Sakai H., Sakuragi J.I.,
RA Fukasawa M., Maki N., Hasegawa A., Mikami T., Adachi A.;
RT "Identification of feline immunodeficiency virus rev gene activity.";
RL J. Virol. 65:4539-4542(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1312825; DOI=10.1007/bf01317136;
RA Maki N., Miyazawa T., Fukasawa M., Hasegawa A., Hayami M., Miki K.,
RA Mikami T.;
RT "Molecular characterization and heterogeneity of feline immunodeficiency
RT virus isolates.";
RL Arch. Virol. 123:29-45(1992).
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; M59418; AAA43074.1; -; Genomic_RNA.
DR PIR; F45557; F45557.
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; IPR018582; Envelope_glycop_lentivirus.
DR InterPro; IPR000328; GP41-like.
DR Pfam; PF09590; Env-gp36; 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 CHAIN 1..855
FT /note="Envelope glycoprotein gp150"
FT /id="PRO_0000239534"
FT CHAIN 1..610
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038721"
FT CHAIN 611..855
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038722"
FT TOPO_DOM 1..784
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 615..635
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 661..679
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 642..692
FT /evidence="ECO:0000255"
FT COILED 735..771
FT /evidence="ECO:0000255"
FT SITE 610..611
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
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 499
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
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 716
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 855 AA; 98239 MW; BC2DFABB6245D70D CRC64;
MAEGGFTHNQ QWIGPEEAEE LLDFDIAVQM NEEGPLNPGV NPFRVPGITS QEKDDYCKIL
QTKLQELKNE VKEVKIEEGN AGKFRRARYL RYSDENVLSI VYLLIGYLRY LIDHRSLGSL
RHDIDIETPQ EEHYNNSEKG TTLNIKYGRR CCISTFIMYL ILFAGVGIWL GARAQVVWRL
PPLVVPVDDT EIIFWDCWAP EEPACQDFLG TMIYLKANVN ISIQEGPTLG NWAREIWSTL
FKKATRQCRR GRIWRRWNET ITGPLGCANN TCYNISVVVP DYQCYVDRVD TWLQGKVNIS
LCLTGGKMLY NKETRQLSYC TDPLQIPLIN YTFGPNQTCM WNTSLIKDSE IPKCGWWNQV
AYYDTCKWEE ANVTFQCHRT QSQSGSWIRT ISSWKQRNRW EWRPDFESEK VKISLQCNST
KNLTFAMRSS SDYYDVQGAW IEFGCHRNKS KRHSEARFRI RCKWNEGNNI SLIDTCGTNP
NVTGANPVDC TMKANTMYNC SLQDSFTMKI EDLIVHFNMT KAVELYNIAG NWSCTSDLPK
GWGYMNCNCT NGTDNSETKM ACPKNQGILR NWYNPVAGLR QALIKYQVVK QPEYLIVPEE
VMQYKFKQKR AAIHIMLALA TVLSMAGAGT GATAIGMVTQ YHQVLATHQQ ALEKITEALK
INNLRLITLE HQVLVIGLRV EAIEKFLYTA FAMQELGCNQ NQFFCKIPPS LWSMYNMTLN
QTIWNHGNIS LGNWYNQTRD LQNKFYEIIM DIEQNNVQGK TGIQQLQKWE NWVGWIGKIP
QYLKGLLGSV LGIGLGILLL LICLPTLVDC IRNCTNKILG YTVIAMPEID DEEVHLSVEL
RRNGRQCGIS EKEEE
