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Signal Peptide Database - Viruses
Entry Details
ID
5308
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P05878 (Created: 1988-11-01 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1SC
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate SC 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]
97056
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
206
disulfide bond
by similarity
125
197
disulfide bond
by similarity
130
160
disulfide bond
by similarity
219
247
disulfide bond
by similarity
228
239
disulfide bond
by similarity
296
330
disulfide bond
by similarity
376
439
disulfide bond
by similarity
383
412
transmembrane region
potential
685
705
topological domain
Extracellular
potential
30
684
topological domain
Cytoplasmic
potential
706
856
region of interest
V1
130
159
region of interest
V2
160
197
region of interest
V3
296
329
region of interest
V4
383
412
region of interest
V5
455
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
129
129
glycosylation site
N-linked (GlcNAc...)
potential
135
135
glycosylation site
N-linked (GlcNAc...)
potential
140
140
glycosylation site
N-linked (GlcNAc...)
potential
143
143
glycosylation site
N-linked (GlcNAc...)
potential
159
159
glycosylation site
N-linked (GlcNAc...)
potential
163
163
glycosylation site
N-linked (GlcNAc...)
potential
189
189
glycosylation site
N-linked (GlcNAc...)
potential
198
198
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
295
295
glycosylation site
N-linked (GlcNAc...)
potential
301
301
glycosylation site
N-linked (GlcNAc...)
potential
302
302
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
384
384
glycosylation site
N-linked (GlcNAc...)
potential
394
394
glycosylation site
N-linked (GlcNAc...)
potential
400
400
glycosylation site
N-linked (GlcNAc...)
potential
405
405
glycosylation site
N-linked (GlcNAc...)
potential
442
442
glycosylation site
N-linked (GlcNAc...)
potential
457
457
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
site
Cleavage; by host furin
by similarity
510
511
site
In-frame UAG termination codon
760
760
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
31
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MRVKGSGRNYQHLWRWGTMLLGILMICSAAE
Sequence
MRVKGSGRNYQHLWRWGTMLLGILMICSA
AEQLWVTVYYGVPVWKEATTT
LFCASDAKAYDTEVHNIWATHACVPTDPNPQEVVLG
N
VTENFNMWKNNMV
EQMHEDIISLWDQSLKPCVKLTPLCVTL
N
CTNLR
N
DTST
N
AT
N
TTSSNRG
KMEGGEMT
N
CSF
N
ITTSIRSKVQKEYALFYKLDVVPID
N
TSYTLINC
N
TS
VITQACPKVSFEPIPIHYCARWFAILNCNNKKF
N
GTGPCT
N
VSTVQCTHG
IRPVVSTHLLL
N
GSLAEEEVVLRSE
N
FTDNAKTIIVQLKEAVEI
N
CTRPN
N
N
TTRSIHIGPGRAFYATGDIIGDIRQAH
C
N
ISRAKW
N
NTLKQIVIKLRD
QFE
N
KTIIF
N
RSSGGDPEIVMHSFNCGGEFFY
C
N
STQLFSSTW
N
GTEGS
N
NTGG
N
DTITLPC
RIKEIINMWQEVGKAMYAPPIKGQVKCSS
N
ITGLLLTR
DGGN
SK
N
GSKNENTEIFRPG
GGDMRDNWRSELYKYKVVKIEPLGVAPTKA
KRRVVQREK
RA
VGTIGAMFLGFLGAAGSTMG
ATSMTLTVQA
RLLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQL
LGIWGCSG
KLICTTTVPW
N
TSWS
N
KSLDKIWG
N
MTWMEWE
REIDNYTSLIYTLIEESQ
NQQEKNEQELLELDKWA
SLWNWF
N
ITNWLWYIKI
FIMIVGGLVGLRIVFT
VLSIV
NRVRQG
YSPL
SFQTRLPSQRGPDRPEGIEEEGGERDRDRSGRLVD
GFLAIIWVD
X
RSL
C
LFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELRNSAVSFVNATAIAVAEGTDRVIELLQRAFRAILHIPTRIRQG
LERALQ
Original
MRVKGSGRNYQHLWRWGTMLLGILMICSAAEQLWVTVYYGVPVWKEATTT
LFCASDAKAYDTEVHNIWATHACVPTDPNPQEVVLGNVTENFNMWKNNMV
EQMHEDIISLWDQSLKPCVKLTPLCVTLNCTNLRNDTSTNATNTTSSNRG
KMEGGEMTNCSFNITTSIRSKVQKEYALFYKLDVVPIDNTSYTLINCNTS
VITQACPKVSFEPIPIHYCARWFAILNCNNKKFNGTGPCTNVSTVQCTHG
IRPVVSTHLLLNGSLAEEEVVLRSENFTDNAKTIIVQLKEAVEINCTRPN
NNTTRSIHIGPGRAFYATGDIIGDIRQAHCNISRAKWNNTLKQIVIKLRD
QFENKTIIFNRSSGGDPEIVMHSFNCGGEFFYCNSTQLFSSTWNGTEGSN
NTGGNDTITLPCRIKEIINMWQEVGKAMYAPPIKGQVKCSSNITGLLLTR
DGGNSKNGSKNENTEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKA
KRRVVQREKRAVGTIGAMFLGFLGAAGSTMGATSMTLTVQARLLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSG
KLICTTTVPWNTSWSNKSLDKIWGNMTWMEWEREIDNYTSLIYTLIEESQ
NQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFT
VLSIVNRVRQGYSPLSFQTRLPSQRGPDRPEGIEEEGGERDRDRSGRLVD
GFLAIIWVDXRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELRNSAVSFVNATAIAVAEGTDRVIELLQRAFRAILHIPTRIRQG
LERALQ
----+----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