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Signal Peptide Database - Viruses
Entry Details
ID
5307
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P03378 (Created: 1986-07-21 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV1A2
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 1 (isolate ARV2/SF2 group M subtype B)
Organism Common
HIV-1
Lineage
Viruses
Retro-transcribing viruses
Retroviridae
Orthoretrovirinae
Lentivirus
Primate lentivirus group
Protein Length [aa]
855
Protein Mass [Da]
97438
Features
Type
Description
Status
Start
End
signal peptide
by similarity
1
31
chain
Envelope glycoprotein gp160
32
855
chain
Surface protein
by similarity
32
509
chain
Transmembrane protein
by similarity
510
855
disulfide bond
by similarity
53
73
disulfide bond
by similarity
118
208
disulfide bond
by similarity
125
199
disulfide bond
by similarity
130
155
disulfide bond
by similarity
221
250
disulfide bond
by similarity
231
242
disulfide bond
by similarity
299
333
disulfide bond
by similarity
380
442
disulfide bond
by similarity
387
415
transmembrane region
potential
684
704
topological domain
Extracellular
potential
32
683
topological domain
Cytoplasmic
potential
705
855
region of interest
V1
130
154
region of interest
V2
155
199
region of interest
V3
299
332
region of interest
V4
387
415
region of interest
V5
458
469
region of interest
Fusion peptide
potential
510
530
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
154
154
glycosylation site
N-linked (GlcNAc...)
potential
158
158
glycosylation site
N-linked (GlcNAc...)
potential
184
184
glycosylation site
N-linked (GlcNAc...)
potential
190
190
glycosylation site
N-linked (GlcNAc...)
potential
200
200
glycosylation site
N-linked (GlcNAc...)
potential
233
233
glycosylation site
N-linked (GlcNAc...)
potential
244
244
glycosylation site
N-linked (GlcNAc...)
potential
265
265
glycosylation site
N-linked (GlcNAc...)
potential
279
279
glycosylation site
N-linked (GlcNAc...)
potential
292
292
glycosylation site
N-linked (GlcNAc...)
potential
298
298
glycosylation site
N-linked (GlcNAc...)
potential
304
304
glycosylation site
N-linked (GlcNAc...)
potential
334
334
glycosylation site
N-linked (GlcNAc...)
potential
341
341
glycosylation site
N-linked (GlcNAc...)
potential
358
358
glycosylation site
N-linked (GlcNAc...)
potential
364
364
glycosylation site
N-linked (GlcNAc...)
potential
388
388
glycosylation site
N-linked (GlcNAc...)
potential
394
394
glycosylation site
N-linked (GlcNAc...)
potential
400
400
glycosylation site
N-linked (GlcNAc...)
potential
408
408
glycosylation site
N-linked (GlcNAc...)
potential
445
445
glycosylation site
N-linked (GlcNAc...)
potential
458
458
glycosylation site
N-linked (GlcNAc...)
potential
461
461
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
site
Cleavage; by host furin
by similarity
509
510
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
coiled-coil region
potential
541
591
coiled-coil region
potential
632
666
SP Length
31
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MKVKGTRRNYQHLWRWGTLLLGMLMICSATE
Sequence
MKVKGTRRNYQHLWRWGTLLLGMLMICSATE
KLWVTVYYGVPVWKEATTT
LFCASDARAYDTEVHNVWATHACVPTDPNPQEVVLG
N
VTENFNMWKNNMV
EQMQEDIISLWDQSLKPCVKLTPLCVTL
N
CTDLGKATNT
N
SSNWKEEIKG
EIK
N
CSF
N
ITTSIRDKIQKENALFRNLDVVPID
N
ASTTT
N
YTNYRLIHC
N
RSVITQACPKVSFEPIPIHYCTPAGFAILKCN
N
KTFNGKGPCT
N
VSTVQC
THGIRPIVSTQLLL
N
GSLAEEEVVIRSD
N
FTNNAKTIIVQL
N
ESVAI
N
CT
RPN
N
NTRKSIYIGPGRAFHTTGRIIGDIRKAH
C
N
ISRAQW
N
NTLEQIVKK
LREQFGN
N
KTIVF
N
QSSGGDPEIVMHSFNCRGEFFY
C
N
TTQLF
N
NTWRL
N
HTEGTKG
N
DTIILPC
RIKQIINMWQEVGKAMYAPPIGGQISCSS
N
ITGLL
LTRDGGT
N
VT
N
DTEVFRPG
GGDMRDNWRSELYKYKVIKIEPLGIAPTKAK
RRVVQREK
RA
VGIVGAMFLGFLGAAGSTMG
AVSLTLTVQA
RQLLSGIVQQ
QNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQL
LGIWGCSGK
LICTTAVPW
N
ASWS
N
KSLEDIWD
N
MTWMQWE
REIDNYTNTIYTLLEESQN
QQEKNEQELLELDKWA
SLWNWFSITNWLWYIKI
FIMIVGGLVGLRIVFAV
LSIV
NRVRQG
YSPL
SFQTRLPVPRGPDRPDGIEEEGGERDRDRSVRLVDG
FLALIWEDLRSL
C
LFSYRRLRDLLLIAARTVEILGHRGWEALKYWWSLLQ
YWIQELKNSAVSWLNATAIAVTEGTDRVIEVAQRAYRAILHIHRRIRQGL
ERLLL
Original
MKVKGTRRNYQHLWRWGTLLLGMLMICSATEKLWVTVYYGVPVWKEATTT
LFCASDARAYDTEVHNVWATHACVPTDPNPQEVVLGNVTENFNMWKNNMV
EQMQEDIISLWDQSLKPCVKLTPLCVTLNCTDLGKATNTNSSNWKEEIKG
EIKNCSFNITTSIRDKIQKENALFRNLDVVPIDNASTTTNYTNYRLIHCN
RSVITQACPKVSFEPIPIHYCTPAGFAILKCNNKTFNGKGPCTNVSTVQC
THGIRPIVSTQLLLNGSLAEEEVVIRSDNFTNNAKTIIVQLNESVAINCT
RPNNNTRKSIYIGPGRAFHTTGRIIGDIRKAHCNISRAQWNNTLEQIVKK
LREQFGNNKTIVFNQSSGGDPEIVMHSFNCRGEFFYCNTTQLFNNTWRLN
HTEGTKGNDTIILPCRIKQIINMWQEVGKAMYAPPIGGQISCSSNITGLL
LTRDGGTNVTNDTEVFRPGGGDMRDNWRSELYKYKVIKIEPLGIAPTKAK
RRVVQREKRAVGIVGAMFLGFLGAAGSTMGAVSLTLTVQARQLLSGIVQQ
QNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGK
LICTTAVPWNASWSNKSLEDIWDNMTWMQWEREIDNYTNTIYTLLEESQN
QQEKNEQELLELDKWASLWNWFSITNWLWYIKIFIMIVGGLVGLRIVFAV
LSIVNRVRQGYSPLSFQTRLPVPRGPDRPDGIEEEGGERDRDRSVRLVDG
FLALIWEDLRSLCLFSYRRLRDLLLIAARTVEILGHRGWEALKYWWSLLQ
YWIQELKNSAVSWLNATAIAVTEGTDRVIEVAQRAYRAILHIHRRIRQGL
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