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Signal Peptide Database - Viruses
Entry Details
ID
3285
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P03375 (Created: 1986-07-21 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1B1
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate BH10 group M subtype B)
Organism Common
HIV-1
Lineage
Viruses
Retro-transcribing viruses
Retroviridae
Orthoretrovirinae
Lentivirus
Primate lentivirus group
Protein Length [aa]
856
Protein Mass [Da]
97225
Features
Type
Description
Status
Start
End
signal peptide
by similarity
1
32
chain
Envelope glycoprotein gp160
33
856
chain
Surface protein
by similarity
33
511
chain
Transmembrane protein
by similarity
512
856
disulfide bond
54
74
disulfide bond
119
205
disulfide bond
126
196
disulfide bond
131
157
disulfide bond
218
247
disulfide bond
228
239
disulfide bond
296
331
disulfide bond
378
445
disulfide bond
385
418
transmembrane region
potential
685
705
topological domain
Extracellular
potential
33
684
topological domain
Cytoplasmic
potential
706
856
region of interest
V1
131
156
region of interest
V2
157
196
region of interest
V3
296
330
region of interest
V4
385
418
region of interest
V5
461
471
region of interest
Fusion peptide
potential
512
532
region of interest
Immunosuppression
by similarity
576
592
region of interest
Involved in GalCer binding
662
667
glycosylation site
N-linked (GlcNAc...)
88
88
glycosylation site
N-linked (GlcNAc...)
136
136
glycosylation site
N-linked (GlcNAc...)
141
141
glycosylation site
N-linked (GlcNAc...)
156
156
glycosylation site
N-linked (GlcNAc...)
160
160
glycosylation site
N-linked (GlcNAc...)
186
186
glycosylation site
N-linked (GlcNAc...)
197
197
glycosylation site
N-linked (GlcNAc...)
230
230
glycosylation site
N-linked (GlcNAc...)
234
234
glycosylation site
N-linked (GlcNAc...)
241
241
glycosylation site
N-linked (GlcNAc...)
262
262
glycosylation site
N-linked (GlcNAc...)
276
276
glycosylation site
N-linked (GlcNAc...)
289
289
glycosylation site
N-linked (GlcNAc...)
295
295
glycosylation site
N-linked (GlcNAc...)
301
301
glycosylation site
N-linked (GlcNAc...)
332
332
glycosylation site
N-linked (GlcNAc...)
339
339
glycosylation site
N-linked (GlcNAc...)
356
356
glycosylation site
N-linked (GlcNAc...)
386
386
glycosylation site
N-linked (GlcNAc...)
392
392
glycosylation site
N-linked (GlcNAc...)
397
397
glycosylation site
N-linked (GlcNAc...)
406
406
glycosylation site
N-linked (GlcNAc...)
448
448
glycosylation site
N-linked (GlcNAc...)
463
463
glycosylation site
N-linked (GlcNAc...)
potential
611
611
glycosylation site
N-linked (GlcNAc...)
potential
616
616
glycosylation site
N-linked (GlcNAc...)
potential
625
625
glycosylation site
N-linked (GlcNAc...)
potential
637
637
glycosylation site
N-linked (GlcNAc...)
potential
674
674
sequence variant
(in strain: Isolate PV22)
0
0
sequence variant
(in strain: Isolate PV22)
0
0
sequence variant
(in strain: Isolate PV22)
0
0
sequence variant
(in strain: Isolate PV22)
0
0
sequence variant
(in strain: Isolate PV22)
0
0
sequence variant
(in strain: Isolate PV22)
0
0
sequence variant
(in strain: Isolate PV22)
0
0
sequence variant
(in strain: Isolate PV22)
0
0
site
Cleavage; by host furin
by similarity
511
512
short sequence motif
YXXL motif; contains endocytosis signal
by similarity
712
715
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
764
764
coiled-coil region
potential
542
592
coiled-coil region
potential
633
667
SP Length
32
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATE
Sequence
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATE
KLWVTVYYGVPVWKEATT
TLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLV
N
VTENFNMWKNDM
VEQMHEDIISLWDQSLKPCVKLTPLCVSLK
CTDLK
N
DTNT
N
SSSGRMIME
KGEIK
N
CSF
N
ISTSIRGKVQKEYAFFYKLDIIPID
N
DTTSYTLTSC
N
TSV
ITQACPKVSFEPIPIHYCAPAGFAILKCN
N
KTF
N
GTGPCT
N
VSTVQCTHG
IRPVVSTQLLL
N
GSLAEEEVVIRSA
N
FTDNAKTIIVQL
N
QSVEI
N
CTRPN
N
NTRKSIRIQRGPGRAFVTIGKIGNMRQAH
C
N
ISRAKW
N
NTLKQIDSKLR
EQFGN
N
KTIIFKQSSGGDPEIVTHSFNCGGEFFY
C
N
STQLF
N
STWF
N
STW
STKGS
N
NTEGSDTITLPC
RIKQIINMWQEVGKAMYAPPISGQIRCSS
N
IT
GLLLTRDGGN
SN
N
ESEIFRPG
GGDMRDNWRSELYKYKVVKIEPLGVAPTK
AKRRVVQREK
RA
VGIGALFLGFLGAAGSTMGA
ASMTLTVQA
RQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQL
LGIWGCSG
KLICTTAVPW
N
ASWS
N
KSLEQIWN
N
MTWMEWD
REINNYTSLIHSLIEESQ
NQQEKNEQELLELDKWA
SLWNWF
N
ITNWLWYIKL
FIMIVGGLVGLRIVFA
VLSVV
NRVRQG
YSPL
SFQTHLPIPRGPDRPEGIEEEGGERDRDRSIRLVN
GSLALIWDDLRSL
C
LFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGAYRAIRHIPRRIRQG
LERILL
Original
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATT
TLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDM
VEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIME
KGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSV
ITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHG
IRPVVSTQLLLNGSLAEEEVVIRSANFTDNAKTIIVQLNQSVEINCTRPN
NNTRKSIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIDSKLR
EQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTW
STKGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNIT
GLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTK
AKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSG
KLICTTAVPWNASWSNKSLEQIWNNMTWMEWDREINNYTSLIHSLIEESQ
NQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFA
VLSVVNRVRQGYSPLSFQTHLPIPRGPDRPEGIEEEGGERDRDRSIRLVN
GSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGAYRAIRHIPRRIRQG
LERILL
----+----1----+----2----+----3----+----4----+----5
Hydropathies
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Dr. Katja Kapp
, Kassel &
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, Dresden, Germany, last update 2010-06-11