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Signal Peptide Database - Viruses
Entry Details
ID
268
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P04582 (Created: 1987-08-13 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1B8
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate BH8 group M subtype B)
Organism Common
HIV-1
Lineage
Viruses
Retro-transcribing viruses
Retroviridae
Orthoretrovirinae
Lentivirus
Primate lentivirus group
Protein Length [aa]
851
Protein Mass [Da]
96644
Features
Type
Description
Status
Start
End
signal peptide
by similarity
1
32
chain
Envelope glycoprotein gp160
33
851
chain
Surface protein
by similarity
33
506
chain
Transmembrane protein
by similarity
507
851
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
440
disulfide bond
by similarity
385
413
transmembrane region
potential
680
700
topological domain
Extracellular
potential
33
679
topological domain
Cytoplasmic
potential
701
851
region of interest
V1
131
156
region of interest
V2
157
196
region of interest
V3
296
330
region of interest
V4
385
413
region of interest
V5
456
466
region of interest
Fusion peptide
potential
507
527
region of interest
Immunosuppression
by similarity
571
587
region of interest
Involved in GalCer binding
by similarity
657
662
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
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
401
401
glycosylation site
N-linked (GlcNAc...)
potential
443
443
glycosylation site
N-linked (GlcNAc...)
potential
458
458
glycosylation site
N-linked (GlcNAc...)
potential
606
606
glycosylation site
N-linked (GlcNAc...)
potential
611
611
glycosylation site
N-linked (GlcNAc...)
potential
620
620
glycosylation site
N-linked (GlcNAc...)
potential
632
632
glycosylation site
N-linked (GlcNAc...)
potential
669
669
strand
578
580
helix
543
575
helix
582
588
site
Cleavage; by host furin
by similarity
506
507
short sequence motif
YXXL motif; contains endocytosis signal
by similarity
707
710
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
759
759
coiled-coil region
potential
537
587
coiled-coil region
potential
628
662
SP Length
32
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATE
Sequence
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATE
KLWVTVYFGVPVWKEATT
TLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLV
N
VTENFNMWKNDM
VEQMHEDIISLWDQSLKPCVKLTPLCVSLK
CTDLK
N
DTNT
N
SSSGRMIME
KGEIK
N
CSF
N
ISTSKRGKVQKEYAFFYKLDIIPID
N
DTTSYTLTSC
N
TSV
ITQACPKVSFEPIPIHYCAPAGFAILKCN
N
KTF
N
GTGPCT
N
VSTVQCTHG
IRPVVSTQLLL
N
GSLAEEEVVIRSV
N
FTDNAKTIIVQLDTSVEI
N
CTRPN
N
NTRKKIRIQRGPGRAFVTIGKIGNMRQAH
C
N
ISRAKW
N
ATLKQIDSKLR
EQFGN
N
KTIIFKQSSGGDPEIVTHSFNCGGEFFY
C
N
STQLF
N
STWSTKGS
N
NTEGSDTITLPC
RIKQIINMWQEVGKAMYAPPISGQIRCSS
N
ITGLLLT
RDGGN
SN
N
ESEIFRPG
GGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRV
VQREK
RA
VGIGALFLGFLGAAGSTMGA
ASMTLTVQA
RQLLSGIVQQQNNL
LRAIEGQQHLLQLTVWGIKQLQARILAVERYLKDQQL
L
GIWGCSGKLICT
TAVPW
N
ASWS
N
KSLEQIWN
N
MTWMEWD
REINNYTSLIHSLIEESQNQQEK
NEQELLELDKWA
SLWNWF
N
ITNWLWYIKL
FIMIVGGLVGLRIVFAVLSIV
NRVRQG
YSPL
SFQTHLPNPRGPDRPEGIEEEGGERDRDRSIRLVNGSLAL
IWDDLRSL
C
LFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQ
ELKNSAVNLLNATAIAVAEGTDRVIELVQAAYRAIRHIPRRIRQGLERIL
L
Original
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYFGVPVWKEATT
TLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDM
VEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIME
KGEIKNCSFNISTSKRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSV
ITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHG
IRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLDTSVEINCTRPN
NNTRKKIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNATLKQIDSKLR
EQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWSTKGS
NNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLT
RDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRV
VQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNL
LRAIEGQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICT
TAVPWNASWSNKSLEQIWNNMTWMEWDREINNYTSLIHSLIEESQNQQEK
NEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIV
NRVRQGYSPLSFQTHLPNPRGPDRPEGIEEEGGERDRDRSIRLVNGSLAL
IWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQ
ELKNSAVNLLNATAIAVAEGTDRVIELVQAAYRAIRHIPRRIRQGLERIL
L
----+----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