ENV_FIVWO
ID ENV_FIVWO Reviewed; 854 AA.
AC Q05312;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 02-DEC-2020, entry version 98.
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 Wo) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=45409;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8380668; DOI=10.1006/viro.1993.1083;
RA Pancino G., Fossati I., Chappey C., Castelot S., Hurtrel B., Maraillon A.,
RA Klatzmann D., Sonigo P.;
RT "Structure and variations of feline immunodeficiency virus envelope
RT glycoproteins.";
RL Virology 192:659-662(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; L06312; AAA43068.1; -; Genomic_DNA.
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..854
FT /note="Envelope glycoprotein gp150"
FT /id="PRO_0000239538"
FT CHAIN 1..609
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038729"
FT CHAIN 610..854
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038730"
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 218
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
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; 98144 MW; 059AC0FBFF4724FF CRC64;
MAEGFAANRQ WIGPEEAEEL LDFDIAIQMN EEGPLNPGVN PFRVPGITEA EKQEYCNILQ
PKLQDLKGKI QEVKLEEGNA GKFRRARFLR YSDETVLSLI HLFIGYCPHL CRRHELGSLR
HDIDIEALQE ERYNDREKGI TDNIKYGKRC LIGTAVLYLL LSLGIIIHTC KAQVVWRLPP
LVVPVEESEI IFWDCWAPEE PACQDFLGAM IHLKASTNIS IQEGPTLGNW AREIWGTLFK
KATRQCRRGR IWRRWNETIT GPLGCANNTC YNISVIVPDY QCYLDRVDTW LQGKVNISLC
LTGGKMLYNK ETKQLSYCTD PLQIPLINYT FGPNQTCMWN TSQIQDPEIP KCGWWNQNAY
YNSCRWEHTD VQFQCQRTQS QPGSWIRAIS SWKQRNRWEW RPDFESEKVK VSLQCNSTKN
LTFAMRSSGD YGEVTGAWIE FGCHRTKSKY HTEARFRIRC RWNVGDNTSL IDTCGETQNV
SRANPVDCTM YANRMYNCSL QNGFTMKVDD LIMHFNKTKA VEMYNIAGNW SCKSDLPPTW
GYMNCNCTNS TNSGTGIRMA CPRNQGILRN WYNPVAGLRQ SLEKYQVVKQ PDYLVVPGEV
MEYKPRRKRA AIHVMLALAT VLSMAGAGTG ATAIGMVTQY QQVLATHQEA IEKVTEALKI
NNLRLVTLEH QVLVIGLKVE AMEKFLYTAF AMQELGCNQN QFFCKVPSAL WERYNMTINQ
TIWNHGNITL GEWYNQTKDL QQRFYEIIMD IEQNNVQGKK GLQQLQEWED WVGWIGNIPQ
YLKGLLGGIL GIGLGMLLLI LCLPTLVDCI RNCIHKILGY TVIAMPEVEE EEIQPQMELR
RNGRQCGMSE KEEE
