ENV_FIVU1
ID ENV_FIVU1 Reviewed; 856 AA.
AC Q03804;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 94.
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 (strain UT-113) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=36373;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8382405; DOI=10.1006/viro.1993.1140;
RA Verschoor E.J., Hulskotte E.G.J., Ederveen J., Koolen M.J.M.,
RA Horzinek M.C., Rottier P.J.M.;
RT "Post-translational processing of the feline immunodeficiency virus
RT envelope precursor protein.";
RL Virology 193:433-438(1993).
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; X60725; CAA43131.1; -; Genomic_DNA.
DR PIR; A45394; A45394.
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..856
FT /note="Envelope glycoprotein gp150"
FT /id="PRO_0000239535"
FT CHAIN 1..611
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038723"
FT CHAIN 612..856
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038724"
FT TOPO_DOM 1..785
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 807..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 616..636
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 662..680
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 643..693
FT /evidence="ECO:0000255"
FT COILED 736..772
FT /evidence="ECO:0000255"
FT SITE 611..612
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
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 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 556
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 856 AA; 98476 MW; A39DA449DE0BF60C CRC64;
MAEGFVANGQ WIGPEEAEEL VDFEIATQMN EEGPLNPGIN PFRVPGITKQ EKQEYCSTMQ
PKLQALRNEI QEVKLEEGNA GKFRRARFLR YSDETILSLI YLFIGYFRYL VDRKRFGSLR
HDIDIEAPQE ECYNNKEKGM TENIKYGKRC LVGTAALYLI LAIGIIIIIR TTDAQVVWRL
PPLVVPVEES EIIFWDCWAP EEPACQDFLG AMIHLKASTN ISNTEGPTLG NWAREIWATL
FKKATRQCRR GRIWKRWNET ITGPIGCANN TCYNISVIVP DYQCYIDRVD TWLQGKVNIS
LCLTGGKMLY NKETKQLSYC TDPLQIPLIN YTFGPNQTCM WNISQIQDPE IPKCGWWNQQ
AYYNNCKWER TDVKFQCQRT QSQPGSWIRA ISSWKQGNRW EWRPDFESER VKVSLQCNST
RNLTFAMRSS GDYGEITGAW IEFGCHRNKS IRHNAARFRI RCRWNEGDNN SLIDTCGETQ
NVSGANPVDC TMYANKMYNC SLQDGFTMKV DDLIMHFNMT KAVEMYNIAG NWSCMSDLPT
EWGYMNCNCT NDTSNNNTRK MKCPKENGIL RNWYNPVAGL RQSLEKYQVV KQPDYLLVPE
EVMEYKPRRK RAAIHVMLAL ATVLSMAGAG TGATAIGMVT QYHQVLATQQ EAIEKVTEAL
KITNLRLVTL EHQVLVIGLK VEAMEKFLYT AFAMQELGCN QNQFFCKVPP ELWRRYNMTI
NQTIWNHGNI TLGEWYNQTK DLQKKFYGII MDIEQNNVQG KKGLQQLQKW EDWVGWIGNI
PQYLKGLLGS IVGIGLGILL LILCLPTLVD CIRNCIHKIL GYTVIAMPEV DGEEIQPQME
LRRNGRQCGM SEKEEE
