MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | 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; |
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| MyHits synonyms | ENV_FIVWO , Q05312 , 059AC0FBFF4724FF |
 Legends: 1, N-linked (GlcNAc...); by host. {ECO:0000255}; 2, CHAIN Transmembrane protein. {ECO:0000250}; 3, TRANSMEM Helical. {ECO:0000255}; 4, TOPO_DOM Cytoplasmic. {ECO:0000255}; 5, REGION Fusion peptide. {ECO:0000255}; 6, REGION Immunosuppression. {ECO:0000250}; 7, COILED {ECO:0000255}; 8, SITE Cleavage; by host. {ECO:0000250}.
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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 05-OCT-2016, entry version 89.
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; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
OC Lentivirus; Feline lentivirus group.
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.,
RA Maraillon A., 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
CC cell by binding to its receptor. This interaction triggers the
CC refolding of the transmembrane protein (TM) and is thought to
CC activate its fusogenic potential by unmasking its fusion peptide.
CC Fusion occurs at the host cell plasma membrane (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral
CC fusion protein. Under the current model, the protein has at least
CC 3 conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral
CC and target cell membrane fusion, the coiled coil regions (heptad
CC repeats) assume a trimer-of-hairpins structure, positioning the
CC fusion peptide in close proximity to the C-terminal region of the
CC ectodomain. The formation of this structure appears to drive
CC apposition and subsequent fusion of viral and target cell
CC membranes. Membranes fusion leads to delivery of the nucleocapsid
CC into the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of
CC SU-TM heterodimers attached by noncovalent interactions or by a
CC labile interchain disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Host cell membrane {ECO:0000250}; Single-pass type I membrane
CC protein {ECO:0000250}. Note=It is probably concentrated at the
CC site of budding and incorporated into the virions possibly by
CC contacts between the cytoplasmic tail of Env and the N-terminus of
CC Gag. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Surface protein: Virion membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the extravirion surface
CC through its binding to TM. It is probably concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as a inactive precursor
CC that is N-glycosylated and processed likely by host cell furin or
CC by a furin-like protease in the Golgi to yield the mature SU and
CC TM proteins. The cleavage site between SU and TM requires the
CC minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.
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;
KW Host-virus interaction; Membrane; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1 854 Envelope glycoprotein gp150.
FT /FTId=PRO_0000239538.
FT CHAIN 1 609 Surface protein. {ECO:0000250}.
FT /FTId=PRO_0000038729.
FT CHAIN 610 854 Transmembrane protein. {ECO:0000250}.
FT /FTId=PRO_0000038730.
FT TOPO_DOM 1 783 Extracellular. {ECO:0000255}.
FT TRANSMEM 784 804 Helical. {ECO:0000255}.
FT TOPO_DOM 805 854 Cytoplasmic. {ECO:0000255}.
FT REGION 614 634 Fusion peptide. {ECO:0000255}.
FT REGION 660 678 Immunosuppression. {ECO:0000250}.
FT COILED 641 691 {ECO:0000255}.
FT COILED 734 770 {ECO:0000255}.
FT SITE 609 610 Cleavage; by host. {ECO:0000250}.
FT CARBOHYD 218 218 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 256 256 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 267 267 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 272 272 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 296 296 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 328 328 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 334 334 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 340 340 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 416 416 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 420 420 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 479 479 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 497 497 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 529 529 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 546 546 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 549 549 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 715 715 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 719 719 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 727 727 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 735 735 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 5 593 ipfam:Env-gp36 [T]
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
//
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