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_FIVSD , P19030 , 9B9CCC4E9F9CCD58 |
 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_FIVSD Reviewed; 854 AA.
AC P19030;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 05-OCT-2016, entry version 96.
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; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
OC Lentivirus; Feline lentivirus group.
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;
RA Phillips T.R., Talbott R.L., Lamont C., Muir S., Lovelace K.M.,
RA 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
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 non-covalent 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; M36968; AAA43079.1; -; Genomic_RNA.
DR ProteinModelPortal; P19030; -.
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_0000239533.
FT CHAIN 1 609 Surface protein. {ECO:0000250}.
FT /FTId=PRO_0000038719.
FT CHAIN 610 854 Transmembrane protein. {ECO:0000250}.
FT /FTId=PRO_0000038720.
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 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 330 330 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 336 336 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 342 342 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 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; 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
//
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