Signal Peptide Database - Viruses

 Entry Details
ID   1293
Source Database   UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number   P04578    (Created: 1987-08-13 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name   ENV_HV1H2
Protein Name   Envelope glycoprotein gp160
Gene   env
Organism Scientific   Human immunodeficiency virus type 1 (isolate HXB2 group M subtype B)
Organism Common   HIV-1
Lineage   Viruses
  Retro-transcribing viruses
    Retroviridae
      Orthoretrovirinae
        Lentivirus
          Primate lentivirus group
Protein Length [aa]   856
Protein Mass [Da]   97213
Features  
TypeDescriptionStatusStartEnd
signal peptide      by similarity   1   32
chain   Envelope glycoprotein gp160      33   856
chain   Surface protein   by similarity   33   511
chain   Transmembrane protein   by similarity   512   856
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   445
disulfide bond      by similarity   385   418
transmembrane region      potential   685   705
topological domain   Extracellular   potential   33   684
topological domain   Cytoplasmic   potential   706   856
region of interest   V1      131   156
region of interest   V2      157   196
region of interest   V3      296   330
region of interest   V4      385   418
region of interest   V5      461   471
region of interest   Fusion peptide   potential   512   532
region of interest   Immunosuppression      576   592
region of interest   Involved in GalCer binding   by similarity   662   667
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   289   289
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   397   397
glycosylation site   N-linked (GlcNAc...)   potential   406   406
glycosylation site   N-linked (GlcNAc...)   potential   448   448
glycosylation site   N-linked (GlcNAc...)   potential   463   463
glycosylation site   N-linked (GlcNAc...)   potential   611   611
glycosylation site   N-linked (GlcNAc...)   potential   616   616
glycosylation site   N-linked (GlcNAc...)   potential   624   624
glycosylation site   N-linked (GlcNAc...)   potential   637   637
glycosylation site   N-linked (GlcNAc...)   potential   674   674
strand         183   187
strand         192   195
strand         199   201
strand         223   228
strand         235   247
strand         256   258
strand         260   262
strand         267   269
strand         271   273
strand         284   297
strand         330   334
strand         359   361
strand         374   378
strand         381   385
strand         393   395
strand         413   417
strand         420   425
strand         427   430
strand         432   434
strand         444   456
strand         466   470
strand         486   490
helix         163   177
helix         335   352
helix         369   372
helix         388   390
helix         475   483
helix         549   577
helix         587   593
site   Cleavage; by host furin   by similarity   511   512
short sequence motif   YXXL motif; contains endocytosis signal      712   715
lipid moiety-binding region   S-palmitoyl cysteine; by host      764   764
lipid moiety-binding region   S-palmitoyl cysteine; by host      837   837
mutagenesis site   Complete loss of palmitoylation, decreased association with host cell membrane lipid rafts, decreased incorporation onto virions and severe reduction of infectivity; when associated with S-837      0   0
mutagenesis site   Complete loss of palmitoylation, decreased association with host cell membrane lipid rafts, decreased incorporation onto virions and severe reduction of infectivity; when associated with S-764      0   0
turn         327   329
coiled-coil region      potential   542   592
coiled-coil region      potential   633   667
SP Length   32
 ----+----1----+----2----+----3----+----4----+----5
Signal Peptide MRVKEKYQHLWRWGWRWGTMLLGMLMICSATE
Sequence MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATT
TLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLV
NVTENFNMWKNDM
VEQMHEDIISLWDQSLKPCVKLTPLCVSLK
CTDLKNDTNTNSSSGRMIME
KGEIK
NCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSV
I
TQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHG
IRPVV
STQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPN
NNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLR
EQ
FGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTW
STEGS
NNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNIT
GLLLTR
DGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTK
AKRRVVQREK
RAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQL
LGIWGCSG
KLICTTAVPW
NASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQ
NQQEKNEQELLELDKWA
SLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFA
VLSIV
NRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVN
GSLALIWDDLRSL
CLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGA
CRAIRHIPRRIRQG
LERILL
Original MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATT
TLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDM
VEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIME
KGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSV
ITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHG
IRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPN
NNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLR
EQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTW
STEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNIT
GLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTK
AKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQ
QQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSG
KLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQ
NQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFA
VLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVN
GSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLL
QYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQG
LERILL
 ----+----1----+----2----+----3----+----4----+----5
Hydropathies  
 

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