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Signal Peptide Database - Viruses
Entry Details
ID
2298
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P20872 (Created: 1991-02-01 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_HV2ST
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Human immunodeficiency virus type 2 (isolate ST subtype A)
Organism Common
HIV-2
Lineage
Viruses
Retro-transcribing viruses
Retroviridae
Orthoretrovirinae
Lentivirus
Primate lentivirus group
Protein Length [aa]
859
Protein Mass [Da]
99070
Features
Type
Description
Status
Start
End
signal peptide
potential
1
24
chain
Envelope glycoprotein gp160
25
859
chain
Surface protein
by similarity
25
505
chain
Transmembrane protein
by similarity
506
859
disulfide bond
by similarity
43
56
disulfide bond
by similarity
100
208
disulfide bond
by similarity
107
199
disulfide bond
by similarity
112
157
disulfide bond
by similarity
221
251
disulfide bond
by similarity
231
243
disulfide bond
by similarity
299
332
disulfide bond
by similarity
384
441
disulfide bond
by similarity
391
414
transmembrane region
potential
674
694
topological domain
Extracellular
potential
25
673
topological domain
Cytoplasmic
potential
695
859
region of interest
V1
112
156
region of interest
V2
157
199
region of interest
V3
299
331
region of interest
V4
391
414
region of interest
V5
457
463
region of interest
Fusion peptide
potential
506
526
region of interest
Immunosuppression
by similarity
569
585
glycosylation site
N-linked (GlcNAc...)
potential
36
36
glycosylation site
N-linked (GlcNAc...)
potential
69
69
glycosylation site
N-linked (GlcNAc...)
potential
78
78
glycosylation site
N-linked (GlcNAc...)
potential
113
113
glycosylation site
N-linked (GlcNAc...)
potential
119
119
glycosylation site
N-linked (GlcNAc...)
potential
131
131
glycosylation site
N-linked (GlcNAc...)
potential
137
137
glycosylation site
N-linked (GlcNAc...)
potential
145
145
glycosylation site
N-linked (GlcNAc...)
potential
160
160
glycosylation site
N-linked (GlcNAc...)
potential
173
173
glycosylation site
N-linked (GlcNAc...)
potential
186
186
glycosylation site
N-linked (GlcNAc...)
potential
200
200
glycosylation site
N-linked (GlcNAc...)
potential
232
232
glycosylation site
N-linked (GlcNAc...)
potential
235
235
glycosylation site
N-linked (GlcNAc...)
potential
242
242
glycosylation site
N-linked (GlcNAc...)
potential
266
266
glycosylation site
N-linked (GlcNAc...)
potential
272
272
glycosylation site
N-linked (GlcNAc...)
potential
283
283
glycosylation site
N-linked (GlcNAc...)
potential
294
294
glycosylation site
N-linked (GlcNAc...)
potential
304
304
glycosylation site
N-linked (GlcNAc...)
potential
359
359
glycosylation site
N-linked (GlcNAc...)
potential
392
392
glycosylation site
N-linked (GlcNAc...)
potential
402
402
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
460
460
glycosylation site
N-linked (GlcNAc...)
potential
605
605
glycosylation site
N-linked (GlcNAc...)
potential
614
614
glycosylation site
N-linked (GlcNAc...)
potential
630
630
site
Cleavage; by host furin
potential
505
506
compositionally biased region
Poly-Thr
120
129
compositionally biased region
Poly-Gln
543
547
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
767
767
coiled-coil region
potential
535
585
coiled-coil region
potential
622
656
SP Length
24
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MCGRNQLFVASLLASACLIYCVQY
Sequence
MCGRNQLFVASLLASACLIYCVQY
VTVFYGVPVWR
N
ASIPLFCATKNRDT
WGTIQCLPDNDDYQEIAL
N
VTEAFDAW
N
NTVTEQAVEDVWSLFETSIKPC
VKLTPLCVAMR
C
N
STTAK
N
TTSTPTTTTT
A
N
TTIGE
N
SSCIRTD
N
CTGLG
EEEMVD
CQF
N
MTGLERDKKKLY
N
ETWYSKDVVCES
N
DTKKEKTCYMNHC
N
TSVITESCDKHYWDTMRFRYCAPPGFALLRC
N
DT
N
YSGFEP
N
CSKVVAAT
CTRMMETQTSTWFGF
N
GTRAE
N
RTYIYWHGRD
N
RTIISLNKFY
N
LTVH
CK
RPG
N
KTVVPITLMSGLVFHSQPINRRPRQAW
CWFKGEWKEAMKEVKLTLA
KHPRYKGT
N
DTEKIRFIAPGERSDPEVAYMWTNCRGEFLY
C
N
MTWFLNWV
E
N
RT
N
QTQHNYVPC
HIKQIINTWHKVGKNVYLPPREGQLTC
N
STVTSIIA
NIDGGE
N
QT
N
ITF
SAEVAELYRLELGDYKLIEVTPIGFAPTPVKRYSSAP
VRNK
RG
VFVLGFLGFLTTAGAAMGAA
SLTLSAQS
RTLLAGIVQQQQQLLD
VVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQ
LNSWGCAFRQVCHTT
VPWV
N
DTLTPDWN
N
MTWQEWE
QRIRNLEANISESLEQAQIQQEKNMYELQ
KLNSWD
VFGNWFDLTSWIKYIQY
GVYIVVGIIVLRIVIYVVQML
SRLRKG
YRPVFSSPPAYFQQIHIHKDREQPAREETEEDVGNSVGDNWWPWPIRYIH
FLIRQLIRLLNRLYNI
C
RDLLSRSFQTLQLISQSLRRALTAVRDWLRFNT
AYLQYGGEWIQEAFRAFARATGETLTNAWRGFWGTLGQIGRGILAVPRRI
RQGAEIALL
Original
MCGRNQLFVASLLASACLIYCVQYVTVFYGVPVWRNASIPLFCATKNRDT
WGTIQCLPDNDDYQEIALNVTEAFDAWNNTVTEQAVEDVWSLFETSIKPC
VKLTPLCVAMRCNSTTAKNTTSTPTTTTTANTTIGENSSCIRTDNCTGLG
EEEMVDCQFNMTGLERDKKKLYNETWYSKDVVCESNDTKKEKTCYMNHCN
TSVITESCDKHYWDTMRFRYCAPPGFALLRCNDTNYSGFEPNCSKVVAAT
CTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKFYNLTVHCK
RPGNKTVVPITLMSGLVFHSQPINRRPRQAWCWFKGEWKEAMKEVKLTLA
KHPRYKGTNDTEKIRFIAPGERSDPEVAYMWTNCRGEFLYCNMTWFLNWV
ENRTNQTQHNYVPCHIKQIINTWHKVGKNVYLPPREGQLTCNSTVTSIIA
NIDGGENQTNITFSAEVAELYRLELGDYKLIEVTPIGFAPTPVKRYSSAP
VRNKRGVFVLGFLGFLTTAGAAMGAASLTLSAQSRTLLAGIVQQQQQLLD
VVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTT
VPWVNDTLTPDWNNMTWQEWEQRIRNLEANISESLEQAQIQQEKNMYELQ
KLNSWDVFGNWFDLTSWIKYIQYGVYIVVGIIVLRIVIYVVQMLSRLRKG
YRPVFSSPPAYFQQIHIHKDREQPAREETEEDVGNSVGDNWWPWPIRYIH
FLIRQLIRLLNRLYNICRDLLSRSFQTLQLISQSLRRALTAVRDWLRFNT
AYLQYGGEWIQEAFRAFARATGETLTNAWRGFWGTLGQIGRGILAVPRRI
RQGAEIALL
----+----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