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_FIVU8 , Q04995 , 78CC9DD035543D7D |
 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_FIVU8 Reviewed; 855 AA.
AC Q04995;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 05-OCT-2016, entry version 87.
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 UK8) (FIV).
OC Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
OC Lentivirus; Feline lentivirus group.
OX NCBI_TaxID=36372;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383177; DOI=10.1099/0022-1317-74-3-425;
RA Rigby M.A., Holmes E.C., Pistello M., Mackay A., Brown A.J.L.,
RA Neil J.C.;
RT "Evolution of structural proteins of feline immunodeficiency virus:
RT molecular epidemiology and evidence of selection for change.";
RL J. Gen. Virol. 74:425-436(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR EMBL; X69496; CAA49250.1; ALT_INIT; Genomic_DNA.
DR PIR; JQ2004; JQ2004.
DR PIR; S29955; S29955.
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 1 855 Envelope glycoprotein gp150.
FT /FTId=PRO_0000239537.
FT CHAIN 1 610 Surface protein. {ECO:0000250}.
FT /FTId=PRO_0000038727.
FT CHAIN 611 855 Transmembrane protein. {ECO:0000250}.
FT /FTId=PRO_0000038728.
FT TOPO_DOM 1 784 Extracellular. {ECO:0000255}.
FT TRANSMEM 785 805 Helical. {ECO:0000255}.
FT TOPO_DOM 806 855 Cytoplasmic. {ECO:0000255}.
FT REGION 615 635 Fusion peptide. {ECO:0000255}.
FT REGION 661 679 Immunosuppression. {ECO:0000250}.
FT COILED 642 692 {ECO:0000255}.
FT COILED 735 771 {ECO:0000255}.
FT SITE 610 611 Cleavage; by host. {ECO:0000250}.
FT CARBOHYD 220 220 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 258 258 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 269 269 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 274 274 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 298 298 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 336 336 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 418 418 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 422 422 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 448 448 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 469 469 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 481 481 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 499 499 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 518 518 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 531 531 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 548 548 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 551 551 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 716 716 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 720 720 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 728 728 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 736 736 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 5 594 ipfam:Env-gp36 [T]
SQ SEQUENCE 855 AA; 97810 MW; 78CC9DD035543D7D CRC64;
MAEGFAANRQ WIGPEEAEEL LDFDIATQMN EEGPLNPGIN PFRVPGITET EKQDYCNMLQ
PKLQALRNEI QEVKLEEGNA GKFRRARFLR YSDETILSLI HLFIGYCTYL LNRKELGSLR
HDIDIEAPQE ECYSSREQSI TDNIKYGKRC FIGTAGLYLL LFIGVGIYLG TAKAQVVWRL
PPLVVPVEES EIIFWDCWAP EEPACQDFLG AMIHLKASTN ISIQEGPTLG NWAKEIWGTL
FKKATRQCRR GRIWKRWNET ITGPLGCANN TCYNISVIVP DYQCYLDRVD TWLQGKVNVS
LCLTGGKILY NKYTKQLSYC TDPLQIPLIS YTFGPNQTCM WDTSQIQDPE IPKCGWWNQI
AYYNSCRWES TDVKFHCQRT QSQPGLWLRA ISSWKQRNRW EWRPDFESEK AKVSLQCNST
KNLTFAMRSS GDYGEVTGAW IEFGCHRNKS KLHTEARFRI RCRWNVGDNT SLIDTCGETQ
NVSGANPVDC TMYANRMYNC SLQNGFTMKV DDLIMHFNMT KAVEMYDIAG NWSCTSDLPP
TWGYMNCNCT NSSSTNSVKM ACPKNQGILR NWYNPVAGLR QSLEKYQVVK QPDYLVVPGE
VMEYKPRRKR AAIHVMLALA TVLSMAGAGT GATAIGMVTQ YHQVLATHQE TIEKVTEALK
INNLRLVTLE HQVLVIGLKV EAMEKFLYTA FAMQELGCNQ NQFFCKVPPE LWKRYNMTIN
QTIWNHGNIT LGEWYNQTKE LQQKFYEIIM NIEQNNVQVK KGLQQLQEWE DWVGWIGNIP
QYLKGLLGGI LGIGIGVLLL ILCLPTLVDC IRNCISKVLG YTVIAMPEIG DEEETVQMEL
RKNGRQCGMS EKEEE
//
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