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Signal Peptide Database - Viruses
Entry Details
ID
4290
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
Q9QBZ0 (Created: 2006-06-27 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1M2
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate MP257 group M subtype F2)
Organism Common
HIV-1
Lineage
Viruses
Retro-transcribing viruses
Retroviridae
Orthoretrovirinae
Lentivirus
Primate lentivirus group
Protein Length [aa]
850
Protein Mass [Da]
96359
Features
Type
Description
Status
Start
End
signal peptide
by similarity
1
31
chain
Envelope glycoprotein gp160
by similarity
32
850
chain
Surface protein
by similarity
32
505
chain
Transmembrane protein
by similarity
506
850
disulfide bond
by similarity
53
73
disulfide bond
by similarity
118
206
disulfide bond
by similarity
125
197
disulfide bond
by similarity
130
158
disulfide bond
by similarity
219
248
disulfide bond
by similarity
229
240
disulfide bond
by similarity
297
331
disulfide bond
by similarity
376
440
disulfide bond
by similarity
383
413
transmembrane region
potential
679
699
topological domain
Extracellular
potential
32
678
topological domain
Cytoplasmic
potential
700
850
region of interest
V1
130
157
region of interest
V2
158
197
region of interest
V3
297
330
region of interest
V4
383
413
region of interest
V5
456
465
region of interest
Fusion peptide
potential
506
526
region of interest
Immunosuppression
by similarity
570
586
region of interest
Involved in GalCer binding
by similarity
656
661
glycosylation site
N-linked (GlcNAc...)
potential
87
87
glycosylation site
N-linked (GlcNAc...)
potential
129
129
glycosylation site
N-linked (GlcNAc...)
potential
136
136
glycosylation site
N-linked (GlcNAc...)
potential
141
141
glycosylation site
N-linked (GlcNAc...)
potential
142
142
glycosylation site
N-linked (GlcNAc...)
potential
148
148
glycosylation site
N-linked (GlcNAc...)
potential
157
157
glycosylation site
N-linked (GlcNAc...)
potential
161
161
glycosylation site
N-linked (GlcNAc...)
potential
186
186
glycosylation site
N-linked (GlcNAc...)
potential
189
189
glycosylation site
N-linked (GlcNAc...)
potential
198
198
glycosylation site
N-linked (GlcNAc...)
potential
231
231
glycosylation site
N-linked (GlcNAc...)
potential
235
235
glycosylation site
N-linked (GlcNAc...)
potential
242
242
glycosylation site
N-linked (GlcNAc...)
potential
263
263
glycosylation site
N-linked (GlcNAc...)
potential
277
277
glycosylation site
N-linked (GlcNAc...)
potential
296
296
glycosylation site
N-linked (GlcNAc...)
potential
302
302
glycosylation site
N-linked (GlcNAc...)
potential
332
332
glycosylation site
N-linked (GlcNAc...)
potential
354
354
glycosylation site
N-linked (GlcNAc...)
potential
384
384
glycosylation site
N-linked (GlcNAc...)
potential
390
390
glycosylation site
N-linked (GlcNAc...)
potential
401
401
glycosylation site
N-linked (GlcNAc...)
potential
406
406
glycosylation site
N-linked (GlcNAc...)
potential
443
443
glycosylation site
N-linked (GlcNAc...)
potential
457
457
glycosylation site
N-linked (GlcNAc...)
potential
605
605
glycosylation site
N-linked (GlcNAc...)
potential
610
610
glycosylation site
N-linked (GlcNAc...)
potential
619
619
glycosylation site
N-linked (GlcNAc...)
potential
631
631
site
Cleavage; by host furin
by similarity
505
506
short sequence motif
YXXL motif; contains endocytosis signal
by similarity
706
709
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
758
758
coiled-coil region
potential
536
586
coiled-coil region
potential
627
661
SP Length
31
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MRVREMQRNWQHLGRWGLLFLGILIICSAAD
Sequence
MRVREMQRNWQHLGRWGLLFLGILIICSAAD
KLWVTVYYGVPVWKEATTT
LFCASDAKAYEREVHNVWATYACVPTDPSPQELVLG
N
VSEKFNMWKNNMV
DQMHEDIISLWDESLKPCVKLTPLCVTL
N
CTKAII
N
VTSS
N
N
TTLAP
N
VT
ISEEMK
N
CSF
N
ITTEIRDKQKKEYALFYKLDVVQI
N
NS
N
TSYRLINC
N
TS
TLTQACPKVSFDPIPIHYCAPAGFAILKCN
N
KTF
N
GTGLCR
N
VSTVQCTH
GIKPVVSTQLLL
N
GSLAEEKMIIRSE
N
ISDNTKTIIVQFKNPVKI
N
CTRP
N
N
NTRRSIHIGPGRAFYATGEIIGDTRKAH
C
N
ISEKQWYDTLIKIATEFK
DQY
N
KTVGFQPSAGGDLEITTHSFNCRGEFFY
C
N
TTILF
N
HTRVNDILSN
N
HTRE
N
DTITLPC
RIKQIVNMWQRVGQAMYAPPIAGKIQCNS
N
ITGLLLT
IDGGE
G
N
ESETLRPG
GGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRQVV
QREK
RA
VGMGAMFLGFLGAAGSTMGA
ASITLTVQA
RNLLSGIVQQQSNLL
KAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQL
LGIWGCSGKLICPT
TVPW
N
LSWS
N
KSQDEIWG
N
MTWMEWE
KEIGNYTDTIYRLIESAQNQQEKN
EQDLLALDKWD
NLWNWFSITRWLWYIEI
FIMIIGSLIGLRIVFTVLSII
N
RVRQG
YSPL
SLQTLIPNSRGPERPGGIEEEGGEQDKDRSIRLVSGFLALA
WDDFRSL
C
VFSYHCLRNFILIAARTVDKGLKRGWEVLKYLWNLAQYWGQE
LKNSAISLLDRTAIAVAEGTDRIIEILQRAGRAVLNIPRRIRQGLERALL
Original
MRVREMQRNWQHLGRWGLLFLGILIICSAADKLWVTVYYGVPVWKEATTT
LFCASDAKAYEREVHNVWATYACVPTDPSPQELVLGNVSEKFNMWKNNMV
DQMHEDIISLWDESLKPCVKLTPLCVTLNCTKAIINVTSSNNTTLAPNVT
ISEEMKNCSFNITTEIRDKQKKEYALFYKLDVVQINNSNTSYRLINCNTS
TLTQACPKVSFDPIPIHYCAPAGFAILKCNNKTFNGTGLCRNVSTVQCTH
GIKPVVSTQLLLNGSLAEEKMIIRSENISDNTKTIIVQFKNPVKINCTRP
NNNTRRSIHIGPGRAFYATGEIIGDTRKAHCNISEKQWYDTLIKIATEFK
DQYNKTVGFQPSAGGDLEITTHSFNCRGEFFYCNTTILFNHTRVNDILSN
NHTRENDTITLPCRIKQIVNMWQRVGQAMYAPPIAGKIQCNSNITGLLLT
IDGGEGNESETLRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRQVV
QREKRAVGMGAMFLGFLGAAGSTMGAASITLTVQARNLLSGIVQQQSNLL
KAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICPT
TVPWNLSWSNKSQDEIWGNMTWMEWEKEIGNYTDTIYRLIESAQNQQEKN
EQDLLALDKWDNLWNWFSITRWLWYIEIFIMIIGSLIGLRIVFTVLSIIN
RVRQGYSPLSLQTLIPNSRGPERPGGIEEEGGEQDKDRSIRLVSGFLALA
WDDFRSLCVFSYHCLRNFILIAARTVDKGLKRGWEVLKYLWNLAQYWGQE
LKNSAISLLDRTAIAVAEGTDRIIEILQRAGRAVLNIPRRIRQGLERALL
----+----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