ENV_FIVPE
ID ENV_FIVPE Reviewed; 856 AA.
AC P16090;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 02-JUN-2021, entry version 110.
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 Petaluma) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11674;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone 34TF10;
RX PubMed=2762293; DOI=10.1073/pnas.86.15.5743;
RA Talbott R.L., Sparger E.E., Lovelace K.M., Fitch W.M., Pedersen N.C.,
RA Luciw P.A., Elder J.H.;
RT "Nucleotide sequence and genomic organization of feline immunodeficiency
RT virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5743-5747(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone FIV-14;
RX PubMed=2813380; DOI=10.1073/pnas.86.20.8088;
RA Olmsted R.A., Hirsch V.M., Purcell R.H., Johnson P.R.;
RT "Nucleotide sequence analysis of feline immunodeficiency virus: genome
RT organization and relationship to other lentiviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8088-8092(1989).
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; M25381; AAB59940.1; ALT_SEQ; Genomic_RNA.
DR PIR; D33543; VCLJFP.
DR RefSeq; NP_040976.1; NC_001482.1.
DR GeneID; 1489987; -.
DR KEGG; vg:1489987; -.
DR Proteomes; UP000242267; 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: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; Reference proteome; 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_0000239532"
FT CHAIN 1..611
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038717"
FT CHAIN 612..856
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038718"
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 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 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; 97941 MW; 107A113D3880DAB3 CRC64;
MAEGFAANRQ WIGPEEAEEL LDFDIATQMS EEGPLNPGVN PFRVPGITEK EKQNYCNILQ
PKLQDLRNEI QEVKLEEGNA GKFRRARFLR YSDERVLSLV HAFIGYCIYL GNRNKLGSLR
HDIDIEAPQE ECYNNREKGT TDNIKYGRRC CLGTVTLYLI LFTGVIVYSQ TAGAQVVWRL
PPLVVPVEES EIIFWDCWAP EEPACQDFLG AMIHLKAKTN ISIREGPTLG NWAREIWATL
FKKATRQCRR GRIWKRWNET ITGPSGCANN TCYNVSVIVP DYQCYLDRVD TWLQGKINIS
LCLTGGKMLY NKVTKQLSYC TDPLQIPLIN YTFGPNQTCM WNTSQIQDPE IPKCGWWNQM
AYYNSCKWEE AKVKFHCQRT QSQPGSWFRA ISSWKQRNRW EWRPDFKSKK VKISLPCNST
KNLTFAMRSS GDYGEVTGAW IEFGCHRNKS NLHTEARFRI RCRWNVGSDT SLIDTCGNTP
NVSGANPVDC TMYSNKMYNC SLQNGFTMKV DDLIVHFNMT KAVEMYNIAG NWSCTSDLPS
SWGYMNCNCT NSSSSYSGTK MACPSNRGIL RNWYNPVAGL RQSLEQYQVV KQPDYLLVPE
EVMEYKPRRK RAAIHVMLAL ATVLSIAGAG TGATAIGMVT QYHQVLATHQ EAIEKVTGAL
KINNLRLVTL EHQVLVIGLK VEAMEKFLYT AFAMQELGCN QNQFFCKIPL ELWTRYNMTI
NQTIWNHGNI TLGEWYNQTK DLQQKFYEII MDIEQNNVQG KTGIQQLQKW EDWVRWIGNI
PQYLKGLLGG ILGIGLGVLL LILCLPTLVD CIRNCIHKIL GYTVIAMPEV EGEEIQPQME
LRRNGRQCGM SEKEEE
