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Signal Peptide Database - Viruses
Entry Details
ID
271
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P05884 (Created: 1988-11-01 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
ENV_SIVMK
Protein Name
Envelope glycoprotein gp160
Gene
env
Organism Scientific
Simian immunodeficiency virus (isolate K6W)
Organism Common
SIV-mac
Lineage
Viruses
Retro-transcribing viruses
Retroviridae
Orthoretrovirinae
Lentivirus
Primate lentivirus group
Protein Length [aa]
881
Protein Mass [Da]
101186
Features
Type
Description
Status
Start
End
signal peptide
potential
1
19
chain
Envelope glycoprotein gp160
20
881
chain
Surface protein
by similarity
20
527
chain
Transmembrane protein
by similarity
528
881
disulfide bond
by similarity
44
57
disulfide bond
by similarity
101
222
disulfide bond
by similarity
108
213
disulfide bond
by similarity
113
170
disulfide bond
by similarity
235
265
disulfide bond
by similarity
245
257
disulfide bond
by similarity
313
346
disulfide bond
by similarity
397
461
disulfide bond
by similarity
404
434
transmembrane region
potential
697
717
topological domain
Extracellular
potential
20
696
topological domain
Cytoplasmic
potential
718
881
region of interest
V1
113
169
region of interest
V2
170
213
region of interest
V3
313
345
region of interest
V4
404
434
region of interest
V5
477
484
region of interest
Fusion peptide
potential
528
548
region of interest
Immunosuppression
by similarity
591
607
glycosylation site
N-linked (GlcNAc...)
potential
37
37
glycosylation site
N-linked (GlcNAc...)
potential
70
70
glycosylation site
N-linked (GlcNAc...)
potential
114
114
glycosylation site
N-linked (GlcNAc...)
potential
148
148
glycosylation site
N-linked (GlcNAc...)
potential
158
158
glycosylation site
N-linked (GlcNAc...)
potential
186
186
glycosylation site
N-linked (GlcNAc...)
potential
200
200
glycosylation site
N-linked (GlcNAc...)
potential
204
204
glycosylation site
N-linked (GlcNAc...)
potential
214
214
glycosylation site
N-linked (GlcNAc...)
potential
246
246
glycosylation site
N-linked (GlcNAc...)
potential
249
249
glycosylation site
N-linked (GlcNAc...)
potential
280
280
glycosylation site
N-linked (GlcNAc...)
potential
286
286
glycosylation site
N-linked (GlcNAc...)
potential
297
297
glycosylation site
N-linked (GlcNAc...)
potential
308
308
glycosylation site
N-linked (GlcNAc...)
potential
318
318
glycosylation site
N-linked (GlcNAc...)
potential
373
373
glycosylation site
N-linked (GlcNAc...)
potential
379
379
glycosylation site
N-linked (GlcNAc...)
potential
462
462
glycosylation site
N-linked (GlcNAc...)
potential
478
478
glycosylation site
N-linked (GlcNAc...)
potential
627
627
glycosylation site
N-linked (GlcNAc...)
potential
636
636
glycosylation site
N-linked (GlcNAc...)
potential
652
652
strand
208
212
strand
247
249
strand
271
279
strand
300
304
strand
309
314
strand
345
350
strand
365
367
strand
392
399
strand
401
405
strand
421
423
strand
438
440
strand
443
446
strand
467
470
strand
476
478
strand
496
498
helix
187
194
helix
268
270
helix
352
362
helix
488
495
site
Cleavage; by host furin
potential
527
528
site
In-frame UAG termination codon
736
736
compositionally biased region
Poly-Gln
565
569
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
789
789
turn
315
317
coiled-coil region
potential
557
607
coiled-coil region
potential
644
678
SP Length
19
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MGCLGNQLLIAILLLSVYG
Sequence
MGCLGNQLLIAILLLSVYG
IYCTQYVTVFYGVPAWR
N
ATIPLFCATKNRD
TWGTTQCLPDNGDYSELAL
N
VTESFDAWENTVTEQAIEDVWQLFETSIKP
CVKLSPLCITMR
C
N
KSETDRWGLTKSSTTITTAAPTSAPVSEKIDMV
N
ET
SSCIAQN
N
CTGLEQEQMIS
CKFTMTGLKRDKTKEY
N
ETWYSTDL
VCEQG
N
STD
N
ESR
CYMNH
C
N
TSVIQESCDKHYWDTIRFRYCAPPGYALLRC
N
DTN
Y
SGFMPKCSKVVVSSCTR
MME
TQTSTWFGF
N
GTRAE
N
RTYIYWHGRD
N
RT
I
ISLN
KYY
N
LTMKCR
RPG
N
KTVLPVTIMSGLVFHSQPLTDRPKQA
WCWFGG
K
WKDAIKEVKQT
IV
KHP
RYTGT
N
NTDKI
N
LTAPGGGDPEVT
FMWTNCRG
E
FLYCK
MNWFLNWVEDRDVTT
QRP
KERHRRNYVPC
HIR
QII
NT
WHKV
GKNV
YLPPREGDLTC
N
STVT
SLIA
NIDWT
DGN
QTSITM
SAE
VAELYRLE
LGD
YK
LVEITPIGLAPTDVKRYTTGGTSRNK
RG
VFVLGFLGFLATAGSAMGAA
SF
RLTAQS
RTLLAGIVQQQQQLLGVVKRQQELLRLTVWGTKNLQTRVTAIEK
YLEDQAQ
LNAWGCAFRQVCHTTVPWP
N
ASLTPDWN
N
DTWQEWE
RKVDFLE
ENITALLEEAQIQQEKNMYELQKLNSWD
VFGNWFDLASWIKYIQYG
IYVV
VGVILLRIVIYIVQMLA
KLRQGYRPVFSSPPSYFQ
X
THTQQDPALPTREG
KEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSN
C
RTLLSRAYQIL
QPILQRLSATLRRIREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGA
WGDLWETLRRGGRWILAIPRRIRQGLELTLL
Original
MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRD
TWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKP
CVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNET
SSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGN
STDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNY
SGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTI
ISLNKYYNLTMKCRRPGNKTVLPVTIMSGLVFHSQPLTDRPKQAWCWFGG
KWKDAIKEVKQTIVKHPRYTGTNNTDKINLTAPGGGDPEVTFMWTNCRGE
FLYCKMNWFLNWVEDRDVTTQRPKERHRRNYVPCHIRQIINTWHKVGKNV
YLPPREGDLTCNSTVTSLIANIDWTDGNQTSITMSAEVAELYRLELGDYK
LVEITPIGLAPTDVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASF
RLTAQSRTLLAGIVQQQQQLLGVVKRQQELLRLTVWGTKNLQTRVTAIEK
YLEDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNDTWQEWERKVDFLE
ENITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLASWIKYIQYGIYVV
VGVILLRIVIYIVQMLAKLRQGYRPVFSSPPSYFQXTHTQQDPALPTREG
KEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQIL
QPILQRLSATLRRIREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGA
WGDLWETLRRGGRWILAIPRRIRQGLELTLL
----+----1----+----2----+----3----+----4----+----5
Hydropathies
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Dr. Katja Kapp
, Kassel &
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, Dresden, Germany, last update 2010-06-11