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Signal Peptide Database - Viruses
Entry Details
ID
1294
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P04580 (Created: 1987-08-13 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1Z6
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate Z6 group M subtype D)
Organism Common
HIV-1
Lineage
Viruses
Retro-transcribing viruses
Retroviridae
Orthoretrovirinae
Lentivirus
Primate lentivirus group
Protein Length [aa]
855
Protein Mass [Da]
96971
Features
Type
Description
Status
Start
End
signal peptide
by similarity
1
30
chain
Envelope glycoprotein gp160
31
855
chain
Surface protein
by similarity
31
510
chain
Transmembrane protein
by similarity
511
855
disulfide bond
by similarity
53
73
disulfide bond
by similarity
118
207
disulfide bond
by similarity
125
198
disulfide bond
by similarity
130
155
disulfide bond
by similarity
220
249
disulfide bond
by similarity
230
241
disulfide bond
by similarity
298
332
disulfide bond
by similarity
378
444
disulfide bond
by similarity
385
417
transmembrane region
potential
684
704
topological domain
Extracellular
potential
31
683
topological domain
Cytoplasmic
potential
705
855
region of interest
V1
130
154
region of interest
V2
155
198
region of interest
V3
298
331
region of interest
V4
385
417
region of interest
V5
459
470
region of interest
Fusion peptide
potential
511
531
region of interest
Immunosuppression
by similarity
575
591
region of interest
Involved in GalCer binding
by similarity
661
666
glycosylation site
N-linked (GlcNAc...)
potential
87
87
glycosylation site
N-linked (GlcNAc...)
potential
129
129
glycosylation site
N-linked (GlcNAc...)
potential
140
140
glycosylation site
N-linked (GlcNAc...)
potential
145
145
glycosylation site
N-linked (GlcNAc...)
potential
154
154
glycosylation site
N-linked (GlcNAc...)
potential
158
158
glycosylation site
N-linked (GlcNAc...)
potential
186
186
glycosylation site
N-linked (GlcNAc...)
potential
189
189
glycosylation site
N-linked (GlcNAc...)
potential
199
199
glycosylation site
N-linked (GlcNAc...)
potential
236
236
glycosylation site
N-linked (GlcNAc...)
potential
243
243
glycosylation site
N-linked (GlcNAc...)
potential
264
264
glycosylation site
N-linked (GlcNAc...)
potential
278
278
glycosylation site
N-linked (GlcNAc...)
potential
291
291
glycosylation site
N-linked (GlcNAc...)
potential
297
297
glycosylation site
N-linked (GlcNAc...)
potential
333
333
glycosylation site
N-linked (GlcNAc...)
potential
340
340
glycosylation site
N-linked (GlcNAc...)
potential
355
355
glycosylation site
N-linked (GlcNAc...)
potential
386
386
glycosylation site
N-linked (GlcNAc...)
potential
392
392
glycosylation site
N-linked (GlcNAc...)
potential
398
398
glycosylation site
N-linked (GlcNAc...)
potential
404
404
glycosylation site
N-linked (GlcNAc...)
potential
443
443
glycosylation site
N-linked (GlcNAc...)
potential
447
447
glycosylation site
N-linked (GlcNAc...)
potential
460
460
glycosylation site
N-linked (GlcNAc...)
potential
461
461
glycosylation site
N-linked (GlcNAc...)
potential
464
464
glycosylation site
N-linked (GlcNAc...)
potential
610
610
glycosylation site
N-linked (GlcNAc...)
potential
615
615
glycosylation site
N-linked (GlcNAc...)
potential
624
624
glycosylation site
N-linked (GlcNAc...)
potential
636
636
glycosylation site
N-linked (GlcNAc...)
potential
673
673
site
Cleavage; by host furin
by similarity
510
511
short sequence motif
YXXL motif; contains endocytosis signal
by similarity
711
714
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
763
763
turn
664
667
coiled-coil region
potential
541
591
coiled-coil region
potential
632
666
SP Length
30
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MRAREIERNCPNLWKWGIMLLGILMICSAA
Sequence
MRAREIERNCPNLWKWGIMLLGILMICSAA
DNLWVTVYYGVPVWKEATTT
LFCASDAKSYKTEAHNIWATHACVPTDPNPQEIELE
N
VTENFNMWRNNMV
EQIHEDIISLWDQSLKPCVKLTPLCVTL
N
CTDESDEWMG
N
VTGK
N
VTEDI
RMK
N
CSF
N
ITTVVRDKTKQVHALFYRLDIVPIDND
N
ST
N
STNYRLINC
N
T
SAITQACPKVSFEPIPIHYCAPAGFAILKCRDKRF
N
GTGPCT
N
VSTVQCT
HGIRPVVSTQLLL
N
GSLAEEEIIIRSE
N
LTNNAKIIIVQL
N
ESVAI
N
CTR
PYKNTRQSTPIGLGQALYTTRGRTKIIGQAH
C
N
ISKEDW
N
KTLQRVAIKL
GNLL
N
KTTIIFKPSSGGDAEITTHSFNCGGEFFY
C
N
TSGLF
N
STWNI
N
NS
EGA
N
STESDNKLITLQC
RIKQIINMWQGVGKAMYAPPIEGQI
N
CSS
N
ITG
LLLTRDGG
T
N
N
SS
N
ETFRPG
GGDMRDNWRSELYKYKVVKIEPLGVAPTKA
KRRVVEREK
RA
IGLGAMFLGFLGAAGSTMGA
ASVTLTVQA
RQLMSGIVQQ
QNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQL
LGIWGCSGK
LICTTTVPW
N
SSWS
N
RSLNDIWQ
N
MTWMEWE
REIDNYTGLIYRLIEESQT
QQEKNEQELLELDKWA
S
LWNWF
N
ITQWLWYIKI
FIMIVGGLIGLRIVFAV
LSLV
NRVRQG
YSPL
SFQTLLPAPREPDRPEGIEEEGGERGRDRSIRLVNG
FSALIWDDLRNL
C
LFSYHRLRDLILIAARIVELLGRRGWEALKYLWNLLQ
YWSRELRNSASSLLDTIAIAVAEGTDRVIEIVRRTYRAVLNVPTRIRQGL
ERLLL
Original
MRAREIERNCPNLWKWGIMLLGILMICSAADNLWVTVYYGVPVWKEATTT
LFCASDAKSYKTEAHNIWATHACVPTDPNPQEIELENVTENFNMWRNNMV
EQIHEDIISLWDQSLKPCVKLTPLCVTLNCTDESDEWMGNVTGKNVTEDI
RMKNCSFNITTVVRDKTKQVHALFYRLDIVPIDNDNSTNSTNYRLINCNT
SAITQACPKVSFEPIPIHYCAPAGFAILKCRDKRFNGTGPCTNVSTVQCT
HGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNAKIIIVQLNESVAINCTR
PYKNTRQSTPIGLGQALYTTRGRTKIIGQAHCNISKEDWNKTLQRVAIKL
GNLLNKTTIIFKPSSGGDAEITTHSFNCGGEFFYCNTSGLFNSTWNINNS
EGANSTESDNKLITLQCRIKQIINMWQGVGKAMYAPPIEGQINCSSNITG
LLLTRDGGTNNSSNETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKA
KRRVVEREKRAIGLGAMFLGFLGAAGSTMGAASVTLTVQARQLMSGIVQQ
QNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGK
LICTTTVPWNSSWSNRSLNDIWQNMTWMEWEREIDNYTGLIYRLIEESQT
QQEKNEQELLELDKWASLWNWFNITQWLWYIKIFIMIVGGLIGLRIVFAV
LSLVNRVRQGYSPLSFQTLLPAPREPDRPEGIEEEGGERGRDRSIRLVNG
FSALIWDDLRNLCLFSYHRLRDLILIAARIVELLGRRGWEALKYLWNLLQ
YWSRELRNSASSLLDTIAIAVAEGTDRVIEIVRRTYRAVLNVPTRIRQGL
ERLLL
----+----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