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Signal Peptide Database - Viruses
Entry Details
ID
1293
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P04578 (Created: 1987-08-13 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1H2
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate HXB2 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]
97213
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
by similarity
54
74
disulfide bond
by similarity
119
205
disulfide bond
by similarity
126
196
disulfide bond
by similarity
131
157
disulfide bond
by similarity
218
247
disulfide bond
by similarity
228
239
disulfide bond
by similarity
296
331
disulfide bond
by similarity
378
445
disulfide bond
by similarity
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
576
592
region of interest
Involved in GalCer binding
by similarity
662
667
glycosylation site
N-linked (GlcNAc...)
potential
88
88
glycosylation site
N-linked (GlcNAc...)
potential
136
136
glycosylation site
N-linked (GlcNAc...)
potential
141
141
glycosylation site
N-linked (GlcNAc...)
potential
156
156
glycosylation site
N-linked (GlcNAc...)
potential
160
160
glycosylation site
N-linked (GlcNAc...)
potential
186
186
glycosylation site
N-linked (GlcNAc...)
potential
197
197
glycosylation site
N-linked (GlcNAc...)
potential
230
230
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
301
301
glycosylation site
N-linked (GlcNAc...)
potential
332
332
glycosylation site
N-linked (GlcNAc...)
potential
339
339
glycosylation site
N-linked (GlcNAc...)
potential
356
356
glycosylation site
N-linked (GlcNAc...)
potential
386
386
glycosylation site
N-linked (GlcNAc...)
potential
392
392
glycosylation site
N-linked (GlcNAc...)
potential
397
397
glycosylation site
N-linked (GlcNAc...)
potential
406
406
glycosylation site
N-linked (GlcNAc...)
potential
448
448
glycosylation site
N-linked (GlcNAc...)
potential
463
463
glycosylation site
N-linked (GlcNAc...)
potential
611
611
glycosylation site
N-linked (GlcNAc...)
potential
616
616
glycosylation site
N-linked (GlcNAc...)
potential
624
624
glycosylation site
N-linked (GlcNAc...)
potential
637
637
glycosylation site
N-linked (GlcNAc...)
potential
674
674
strand
183
187
strand
192
195
strand
199
201
strand
223
228
strand
235
247
strand
256
258
strand
260
262
strand
267
269
strand
271
273
strand
284
297
strand
330
334
strand
359
361
strand
374
378
strand
381
385
strand
393
395
strand
413
417
strand
420
425
strand
427
430
strand
432
434
strand
444
456
strand
466
470
strand
486
490
helix
163
177
helix
335
352
helix
369
372
helix
388
390
helix
475
483
helix
549
577
helix
587
593
site
Cleavage; by host furin
by similarity
511
512
short sequence motif
YXXL motif; contains endocytosis signal
712
715
lipid moiety-binding region
S-palmitoyl cysteine; by host
764
764
lipid moiety-binding region
S-palmitoyl cysteine; by host
837
837
mutagenesis site
Complete loss of palmitoylation, decreased association with host cell membrane lipid rafts, decreased incorporation onto virions and severe reduction of infectivity; when associated with S-837
0
0
mutagenesis site
Complete loss of palmitoylation, decreased association with host cell membrane lipid rafts, decreased incorporation onto virions and severe reduction of infectivity; when associated with S-764
0
0
turn
327
329
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
IS
TSIRGKVQKEYAFFY
KLDII
PIDND
TTSY
KLTS
C
N
T
SV
I
TQACPKVSFEPIPIHYCAPAG
FAILKC
N
N
KTF
N
GTGPCTNVSTVQC
THG
IRPVV
STQ
L
LLN
GSLA
EEE
V
VIR
SV
N
FTDNAKT
IIVQLNTSVEINCT
RPN
N
NTRKRIRIQRGPGRAFVTIGKIGNM
RQA
HCNIS
RAKWNNTLKQIASKLR
EQ
FGN
N
KT
IIF
KQSSGGD
PEIV
T
HSFNC
GG
EFFYC
N
S
TQL
F
N
STW
F
N
STW
STEGS
N
NTEGSD
TITLP
C
R
IKQIIN
M
WQKV
G
KAM
YAPPISGQI
RCSSNIT
GLLLTR
DGGN
SN
N
ES
EIFRP
G
GGD
MRDNWRSEL
YK
YKVVK
IEPLGVAPTK
AKRRVVQREK
RA
VGIGALFLGFLGAAGSTMGA
ASMTLTVQA
RQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQL
L
GIWGCSG
KLICTTAVPW
N
ASWS
N
KSLEQIW
N
HTTWMEWD
REINNYTSLIHSLIEESQ
NQQEKNEQELLELDKWA
SLWNWF
N
ITNWLWYIKL
FIMIVGGLVGLRIVFA
VLSIV
NRVRQG
YSPL
SFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVN
GSLALIWDDLRSL
C
LFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGA
C
RAIRHIPRRIRQG
LERILL
Original
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATT
TLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDM
VEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIME
KGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSV
ITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHG
IRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPN
NNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLR
EQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTW
STEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNIT
GLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTK
AKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSG
KLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQ
NQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFA
VLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVN
GSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQG
LERILL
----+----1----+----2----+----3----+----4----+----5
Hydropathies
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Dr. Katja Kapp
, Kassel &
thpr.net e. K.
, Dresden, Germany, last update 2010-06-11