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Signal Peptide Database - Viruses
Entry Details
ID
269
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P31872 (Created: 1993-07-01 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1W1
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate WMJ1 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]
97526
Features
Type
Description
Status
Start
End
signal peptide
by similarity
1
31
chain
Envelope glycoprotein gp160
32
856
chain
Surface protein
by similarity
32
510
chain
Transmembrane protein
by similarity
511
856
disulfide bond
by similarity
53
73
disulfide bond
by similarity
118
205
disulfide bond
by similarity
125
196
disulfide bond
by similarity
130
152
disulfide bond
by similarity
218
247
disulfide bond
by similarity
228
239
disulfide bond
by similarity
296
330
disulfide bond
by similarity
376
444
disulfide bond
by similarity
383
417
transmembrane region
potential
685
705
topological domain
Extracellular
potential
33
684
topological domain
Cytoplasmic
potential
706
856
region of interest
V1
130
151
region of interest
V2
152
196
region of interest
V3
296
329
region of interest
V4
383
417
region of interest
V5
460
470
region of interest
Fusion peptide
potential
511
531
region of interest
Immunosuppression
by similarity
576
592
region of interest
Involved in GalCer binding
by similarity
662
667
glycosylation site
N-linked (GlcNAc...)
potential
87
87
glycosylation site
N-linked (GlcNAc...)
potential
134
134
glycosylation site
N-linked (GlcNAc...)
potential
140
140
glycosylation site
N-linked (GlcNAc...)
potential
151
151
glycosylation site
N-linked (GlcNAc...)
potential
155
155
glycosylation site
N-linked (GlcNAc...)
potential
183
183
glycosylation site
N-linked (GlcNAc...)
potential
197
197
glycosylation site
N-linked (GlcNAc...)
potential
234
234
glycosylation site
N-linked (GlcNAc...)
potential
241
241
glycosylation site
N-linked (GlcNAc...)
potential
262
262
glycosylation site
N-linked (GlcNAc...)
potential
276
276
glycosylation site
N-linked (GlcNAc...)
potential
289
289
glycosylation site
N-linked (GlcNAc...)
potential
295
295
glycosylation site
N-linked (GlcNAc...)
potential
331
331
glycosylation site
N-linked (GlcNAc...)
potential
338
338
glycosylation site
N-linked (GlcNAc...)
potential
354
354
glycosylation site
N-linked (GlcNAc...)
potential
360
360
glycosylation site
N-linked (GlcNAc...)
potential
390
390
glycosylation site
N-linked (GlcNAc...)
potential
394
394
glycosylation site
N-linked (GlcNAc...)
potential
404
404
glycosylation site
N-linked (GlcNAc...)
potential
447
447
glycosylation site
N-linked (GlcNAc...)
potential
459
459
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
helix
662
670
site
Cleavage; by host furin
by similarity
510
511
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
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
837
837
coiled-coil region
potential
542
592
coiled-coil region
potential
633
667
SP Length
31
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MRVKGIRRNCQHLWIWGTMLFGMWMICSAVE
Sequence
MRVKGIRRNCQHLWIWGTMLFGMWMICSAVE
Q
LWVTVYYGVPVWKEATTT
LFCASDAKAYSTEAHKVWATHACVPTNPNPQEVVLE
N
VTENFNMWKNNMV
EQMHEDIISLWDQSLKPCVKLTPLCVTLN
CIDK
N
ITDWE
N
KTIIGGGEVK
N
CSF
N
ITTSIRDKVHKEYALFYKLDVVPIKSN
N
DSSTYTRYRLIHC
N
TSV
ITQACSKVSFEPIPIHYCAPAGFAILKCNDKKF
N
GTGPCT
N
VSTVQCTHG
IRPVVSTQLLL
N
GSLAEEEIVIRSE
N
FTDNAKTIIVHL
N
ESVEI
N
CTRPN
NNVRRRHIHIGPGRAFYTGEIRGNIRQAH
C
N
ISRAKW
N
NTLKQIVEKLRE
QFK
N
KTIVF
N
HSSGGDPEIVTHSFNCGGEFFY
CDSTQLF
N
STW
N
VTGIST
EGN
N
NTEENGDTITLPC
RIKQIINMWQGVGKAMYAPPIGGQIRCSS
N
ITG
LLLTRDGG
N
SSSREEIFRPG
GGNMRDNWRSELYKYKVVKIEPLGVAPTKA
KRRVVQREK
RA
VGAIGAMFLGFLGAAGSTMG
AASLTLTVQA
RQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQL
LGIWGCSG
KLICTTTVPW
N
ASWS
N
KSMDQIWN
N
MTWMEWE
REIDNYTSLIYNLIEESQ
NQQEKNEQELLELDKWA
SLW
NWFSITNWLWYIKI
FIMIVGGLVGLRIVFS
VLSIV
NRVRQG
YSPL
SFQTHLPTPRGPDRPEGTEEEGGERDRDRSVRLVH
GFLALIWDDLRSL
C
LFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSKELKNSAVGLLNAIAIAVAEGTDRVIEVVQRI
C
RAIIHIPRRIRQG
LERALL
Original
MRVKGIRRNCQHLWIWGTMLFGMWMICSAVEQLWVTVYYGVPVWKEATTT
LFCASDAKAYSTEAHKVWATHACVPTNPNPQEVVLENVTENFNMWKNNMV
EQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDKNITDWENKTIIGGGEVK
NCSFNITTSIRDKVHKEYALFYKLDVVPIKSNNDSSTYTRYRLIHCNTSV
ITQACSKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHG
IRPVVSTQLLLNGSLAEEEIVIRSENFTDNAKTIIVHLNESVEINCTRPN
NNVRRRHIHIGPGRAFYTGEIRGNIRQAHCNISRAKWNNTLKQIVEKLRE
QFKNKTIVFNHSSGGDPEIVTHSFNCGGEFFYCDSTQLFNSTWNVTGIST
EGNNNTEENGDTITLPCRIKQIINMWQGVGKAMYAPPIGGQIRCSSNITG
LLLTRDGGNSSSREEIFRPGGGNMRDNWRSELYKYKVVKIEPLGVAPTKA
KRRVVQREKRAVGAIGAMFLGFLGAAGSTMGAASLTLTVQARQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSG
KLICTTTVPWNASWSNKSMDQIWNNMTWMEWEREIDNYTSLIYNLIEESQ
NQQEKNEQELLELDKWASLWNWFSITNWLWYIKIFIMIVGGLVGLRIVFS
VLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGTEEEGGERDRDRSVRLVH
GFLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSKELKNSAVGLLNAIAIAVAEGTDRVIEVVQRICRAIIHIPRRIRQG
LERALL
----+----1----+----2----+----3----+----4----+----5
Hydropathies
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© 2007-2017
Dr. Katja Kapp
, Kassel &
thpr.net e. K.
, Dresden, Germany, last update 2010-06-11