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Envelope glycoprotein gp150 (Env polyprotein) [Cleaved into: Surface protein (SU) (Glycoprotein 100) (gp100); Transmembrane protein (TM) (Glycoprotein 36) (gp36)]

 ENV_FIVPE               Reviewed;         856 AA.
P16090;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
10-MAY-2017, entry version 100.
RecName: Full=Envelope glycoprotein gp150;
AltName: Full=Env polyprotein;
Contains:
RecName: Full=Surface protein;
Short=SU;
AltName: Full=Glycoprotein 100;
Short=gp100;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
AltName: Full=Glycoprotein 36;
Short=gp36;
Name=env;
Feline immunodeficiency virus (isolate Petaluma) (FIV).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Feline lentivirus group.
NCBI_TaxID=11674;
NCBI_TaxID=9681; Felidae (cat family).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Clone 34TF10;
PubMed=2762293; DOI=10.1073/pnas.86.15.5743;
Talbott R.L., Sparger E.E., Lovelace K.M., Fitch W.M., Pedersen N.C.,
Luciw P.A., Elder J.H.;
"Nucleotide sequence and genomic organization of feline
immunodeficiency virus.";
Proc. Natl. Acad. Sci. U.S.A. 86:5743-5747(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Clone FIV-14;
PubMed=2813380; DOI=10.1073/pnas.86.20.8088;
Olmsted R.A., Hirsch V.M., Purcell R.H., Johnson P.R.;
"Nucleotide sequence analysis of feline immunodeficiency virus: genome
organization and relationship to other lentiviruses.";
Proc. Natl. Acad. Sci. U.S.A. 86:8088-8092(1989).
-!- FUNCTION: The surface protein (SU) attaches the virus to the host
cell by binding to its receptor. This interaction triggers the
refolding of the transmembrane protein (TM) and is thought to
activate its fusogenic potential by unmasking its fusion peptide.
Fusion occurs at the host cell plasma membrane (By similarity).
{ECO:0000250}.
-!- FUNCTION: The transmembrane protein (TM) acts as a class I viral
fusion protein. Under the current model, the protein has at least
3 conformational states: pre-fusion native state, pre-hairpin
intermediate state, and post-fusion hairpin state. During viral
and target cell membrane fusion, the coiled coil regions (heptad
repeats) assume a trimer-of-hairpins structure, positioning the
fusion peptide in close proximity to the C-terminal region of the
ectodomain. The formation of this structure appears to drive
apposition and subsequent fusion of viral and target cell
membranes. Membranes fusion leads to delivery of the nucleocapsid
into the cytoplasm (By similarity). {ECO:0000250}.
-!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of
SU-TM heterodimers attached by noncovalent interactions or by a
labile interchain disulfide bond. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}. Note=It is probably concentrated at the
site of budding and incorporated into the virions possibly by
contacts between the cytoplasmic tail of Env and the N-terminus of
Gag. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Surface protein: Virion membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
cell membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Note=The surface protein is not anchored to the
viral envelope, but associates with the extravirion surface
through its binding to TM. It is probably concentrated at the site
of budding and incorporated into the virions possibly by contacts
between the cytoplasmic tail of Env and the N-terminus of Gag (By
similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Envelope glycoproteins are synthesized as a inactive precursor
that is N-glycosylated and processed likely by host cell furin or
by a furin-like protease in the Golgi to yield the mature SU and
TM proteins. The cleavage site between SU and TM requires the
minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M25381; AAB59940.1; ALT_SEQ; Genomic_RNA.
PIR; D33543; VCLJFP.
SMR; P16090; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
InterPro; IPR018582; Envelope_glycop_lentivirus.
InterPro; IPR000328; GP41-like.
Pfam; PF09590; Env-gp36; 1.
3: Inferred from homology;
Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
Glycoprotein; Host cell membrane; Host membrane;
Host-virus interaction; Membrane; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein; Virion;
Virus entry into host cell.
CHAIN 1 856 Envelope glycoprotein gp150.
/FTId=PRO_0000239532.
CHAIN 1 611 Surface protein. {ECO:0000250}.
/FTId=PRO_0000038717.
CHAIN 612 856 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000038718.
TOPO_DOM 1 785 Extracellular. {ECO:0000255}.
TRANSMEM 786 806 Helical. {ECO:0000255}.
TOPO_DOM 807 856 Cytoplasmic. {ECO:0000255}.
REGION 616 636 Fusion peptide. {ECO:0000255}.
REGION 662 680 Immunosuppression. {ECO:0000250}.
COILED 643 693 {ECO:0000255}.
COILED 736 772 {ECO:0000255}.
COMPBIAS 552 557 Poly-Ser.
SITE 611 612 Cleavage; by host. {ECO:0000250}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 274 274 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 298 298 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 422 422 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 717 717 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 721 721 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 729 729 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 737 737 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
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


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