ID ENV_FIVSD Reviewed; 854 AA.
AC P19030;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 08-NOV-2023, entry version 106.
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 San Diego) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC Feline immunodeficiency virus.
OX NCBI_TaxID=11675;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate PPR;
RX PubMed=1697907; DOI=10.1128/jvi.64.10.4605-4613.1990;
RA Phillips T.R., Talbott R.L., Lamont C., Muir S., Lovelace K.M., Elder J.H.;
RT "Comparison of two host cell range variants of feline immunodeficiency
RT virus.";
RL J. Virol. 64:4605-4613(1990).
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 non-covalent 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; M36968; AAA43079.1; -; Genomic_RNA.
DR GlyCosmos; P19030; 22 sites, No reported glycans.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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..854
FT /note="Envelope glycoprotein gp150"
FT /id="PRO_0000239533"
FT CHAIN 1..609
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038719"
FT CHAIN 610..854
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038720"
FT TOPO_DOM 1..783
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 784..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 805..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 614..634
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 660..678
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 641..691
FT /evidence="ECO:0000255"
FT COILED 734..770
FT /evidence="ECO:0000255"
FT SITE 609..610
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 715
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 854 AA; 98333 MW; 9B9CCC4E9F9CCD58 CRC64;
MAEGFAANRQ WIGPEEAEEL LDFDKATQMN EEGPLNPGVN PFRVPAVTEA DKQEYCKILQ
PRLQEIRNEI QEVKLEEGNA GKFRRARFLR YSDESILSLI HLFIGYCTYL VNRRRLGSLR
HDINIEAPQE EQYSSREQGT TENIKYGRRC LIGTASLYLL LFIGVAIYLG TTNAQIVWRL
PPLVVPVEES EIIFWDCWAP EEPACQDFLG AMIHLKASTN ISIQEGPTLG NWAREIWGTL
FKKATRHCRR NKIWKRWNET ITGPVGCANN TCYNISVIIP DYQCYLDRVD TWLQGKVNIS
LCLTGGKMLY NRDTKQLSYC TDPLQIPLIN YTFGPNQTCM WNTSQIQDPE IPKCGWWNQI
AYYNSCRWES TNVKFYCQRT QSQPGTWIRT ISSWRQKNRW EWRPDFESEK VKISLQCNST
HNLTFAMRSS GDYGEVMGAW IEFGCHRNKS RFHTEARFRI RCRWNVGDNT SLIDTCGKNL
NVSGANPVDC TMYANKMYNC SLQNGFTMKV DDLIMHFNMT KAVEMYNIAG NWSCKSDLPQ
NWGYMNCNCT NGTSNDNKMA CPEDKGILRN WYNPVAGLRQ ALEKYQVVKQ PEYIVVPTEV
MTYKYKQKRA AIHIMLALAT VLSIAGAGTG ATAIGMVTQY QQVLATHQEA LDKITEALKI
NNLRLVTLEH QMLVIGLKVE AIEKFLYTAF AMQELGCNQN QFFCEIPKEL WLRYNMTLNQ
TIWNHGNITL GEWYNQTKYL QQKFYEIIMD IEQNNVQGKQ GLQKLQNWQD WMGWIGKIPQ
YLKGLLGGIL GIGLGILLLI LCLPTLVDCI RNCISKVLGY TVIAMPEIDD EEETVQMELR
KNGRQCGMSE KEEE
//
