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Q07374 (Q07374_SIV) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
Gene names
Name:env EMBL BAA00871.1
OrganismSimian immunodeficiency virus (SIV) EMBL BAA00871.1
Taxonomic identifier11723 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostPan troglodytes (Chimpanzee) [TaxID: 9598]

Protein attributes

Sequence length878 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The envelope glyprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface By similarity. SAAS SAAS000328

The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves By similarity. SAAS SAAS000328

Subcellular location

Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein By similarity SAAS SAAS000328.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) PDB 3FUS PDB 2BF1
Glycosylation2111N-linked (GlcNAc...) PDB 3FUS PDB 2BF1
Glycosylation2431N-linked (GlcNAc...) PDB 3FUS PDB 2BF1
Glycosylation2771N-linked (GlcNAc...) PDB 3FUS PDB 2BF1
Glycosylation2941N-linked (GlcNAc...) PDB 3FUS
Glycosylation3051N-linked (GlcNAc...) PDB 3FUS PDB 2BF1
Glycosylation4591N-linked (GlcNAc...) PDB 3FUS PDB 2BF1
Glycosylation4751N-linked (GlcNAc...) PDB 3FUS PDB 2BF1
Glycosylation4781N-linked (GlcNAc...) PDB 3FUS

Sequences

Sequence LengthMass (Da)Tools
Q07374 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 210D7E30B417262A

FASTA878100,992
        10         20         30         40         50         60 
MGCLGNQLLI AILLLSVYGI YCTQYVTVFY GVPAWRNATI PLFCATENRD TWGTTQCLPD 

        70         80         90        100        110        120 
NGDYSELALN VTESFDAWEN TVTEQAIEDV WQLFETSIKP CVKLSPLCIT MRCNKSETDK 

       130        140        150        160        170        180 
WGLTKSLTTT APTAPTAASK IDMVNETSSC ITHDNCTGLE QEQMIGCKFN MTGLKRDKTK 

       190        200        210        220        230        240 
EYNETWYSTD LVCEQGNSTD NESRCYMNHC NTSIIQESCD KHYWDTIRFR YCAPPGYALL 

       250        260        270        280        290        300 
RCNDTNYSGF MPKCSKVVVS SCTRMMETQT STWFGFNGTR AENRTYIYWH GRDNRTIISL 

       310        320        330        340        350        360 
NKYYNLTMKC RRPGNKTVLP VTIMSGLVFH SQPINDRPKQ AWCWFGGNWK DAIKEMKQTI 

       370        380        390        400        410        420 
VKHPRYTGTN NTDKINLTAP RGGDPEVTFM WTNCRGEFLY CKMNWFLNWV EDRDVTNQRP 

       430        440        450        460        470        480 
KERHRRNYVP CHIRQIINTW HKVGKNVYLP PREGDLTCNS TVTSLIANID WTDGNQTNIT 

       490        500        510        520        530        540 
MSAEVAELYR LELGDYKLVE ITPIGLAPTD VKRYTTGGTS RNKRGVFVLG FLGFLATAGS 

       550        560        570        580        590        600 
AMGAASLTLT AQSRTLLAGI VQQQQQLLDV VKRQQELLRL TVWGTKNLQT RVTAIEKYLK 

       610        620        630        640        650        660 
DQAQLNAWGC AFRQVCHTTV PWPNASLTPD WNNDTWQEWE RKVDFLEENI TALLEEAQIQ 

       670        680        690        700        710        720 
QEKNMYELQK LNSWDVFGNW FDLASWIKYI QYGVYIVVGV ILLRIVIYIV QMLAKLRQGY 

       730        740        750        760        770        780 
RPVFSSPPSY FQQTHIQQDP ALPTREGKEG DGGEGGGNSS WPWQIEYIHF LIRQLIRLLT 

       790        800        810        820        830        840 
WLFSNCRTLL SRAYQILQPI LQRLSAALQR IREVLRTELT YLQYGWSYFQ EAVQVGWRSA 

       850        860        870 
TETLAGAWGD LWETLRRGGR WILAIPRRIR QGLELTLL 

« Hide

References

[1]"Infectious molecular clones of SIVmac32H: Nef deletion controls ability to reisolate virus from rhesus macaques."
Rud E.W., Yon J.R., Larder B.A., Clarke B.E., Cook N., Cranage M.P.
(In) Brown F., Chanock R.M., Ginsberg H.S. (eds.); Vaccines 92: Modern Approaches to New Vaccines Including Prevention of AIDS, pp.229-235, Cold Spring Harbor Laboratory Press, New York (1992)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SIVmac32H EMBL BAA00871.1.
[2]"Molecular cloning and sequence of the simian immunodeficiency virus, SIVmac32H."
Rud E.W., Yon J.R., Cranage M.P., Larder B.A., Clarke B.E.
J. Gen. Virol. 75:529-543(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SIVmac32H EMBL BAA00871.1.
[3]"Structure of an unliganded simian immunodeficiency virus gp120 core."
Chen B., Vogan E.M., Gong H., Skehel J.J., Wiley D.C., Harrison S.C.
Nature 433:834-841(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 209-311; 342-502 AND 66-109, GLYCOSYLATION AT ASN-70; ASN-211; ASN-243; ASN-277; ASN-305; ASN-459 AND ASN-475.
[4]"Structural improvement of unliganded simian immunodeficiency virus gp120 core by normal-mode-based X-ray crystallographic refinement."
Chen X., Lu M., Poon B.K., Wang Q., Ma J.
Acta Crystallogr. D 65:339-347(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 209-311; 342-502 AND 66-109, GLYCOSYLATION AT ASN-70; ASN-211; ASN-243; ASN-277; ASN-294; ASN-305; ASN-459; ASN-475 AND ASN-478.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D01065 Genomic DNA. Translation: BAA00871.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BF1X-ray4.00A209-311[»]
A342-502[»]
A66-109[»]
3FUSX-ray4.00A209-311[»]
A342-502[»]
A66-109[»]
ProteinModelPortalQ07374.
SMRQ07374. Positions 64-499, 551-673.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.170.40.20. 2 hits.
InterProIPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]
PfamPF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]
SUPFAMSSF56502. SSF56502. 3 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ07374.

Entry information

Entry nameQ07374_SIV
AccessionPrimary (citable) accession number: Q07374
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)