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Protein

Endogenous retrovirus group K member 19 Env polyprotein

Gene

env

Organism
Human immunodeficiency virus 1
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ApoptosisSAAS annotation, Fusion of virus membrane with host membraneSAAS annotation, Host-virus interaction, Viral attachment to host cellSAAS annotation, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Endogenous retrovirus group K member 19 Env polyproteinSAAS annotation
Alternative name(s):
Endogenous retrovirus group K member 113 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 13-1 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 18 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 21 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 24 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 25 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 6 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 7 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 8 Env polyproteinSAAS annotation
Endogenous retrovirus group K member 9 Env polyproteinSAAS annotation
Envelope glycoprotein gp160SAAS annotation
Gene namesi
Name:envImported
OrganismiHuman immunodeficiency virus 1Imported
Taxonomic identifieri11676 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneSAAS annotation, Host endosomeSAAS annotation, Host membrane, Membrane, Viral envelope proteinUniRule annotationSAAS annotation, Virion

Pathology & Biotechi

Keywords - Diseasei

AIDSUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 69Combined sources
Disulfide bondi114 ↔ 194Combined sources
Glycosylationi184 – 1841N-linked (GlcNAc...)Combined sources
Disulfide bondi207 ↔ 236Combined sources
Disulfide bondi217 ↔ 228Combined sources
Disulfide bondi285 ↔ 319Combined sources
Glycosylationi291 – 2911N-linked (GlcNAc...)Combined sources
Disulfide bondi365 ↔ 429Combined sources
Disulfide bondi372 ↔ 402Combined sources

Keywords - PTMi

Disulfide bondSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TGRX-ray2.80A/B39-478[»]
3TGSX-ray2.70A/B39-478[»]
4I53X-ray2.50A/B39-478[»]
4LSVX-ray3.00G39-478[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

Family and domain databases

Gene3Di2.170.40.20. 2 hits.
InterProiIPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]
PfamiPF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]
SUPFAMiSSF56502. SSF56502. 2 hits.

Sequencei

Sequence statusi: Complete.

C6G099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVRGIWKNW PQWLIWSILG FWIGNMEGSW VTVYYGVPVW KEAKTTLFCA
60 70 80 90 100
SDAKAYEKEV HNVWATHACV PTDPNPQEMV LANVTENFNM WKNDMVEQMH
110 120 130 140 150
EDIISLWDES LKPCVKLTPL CVTLNCTNVK GNESDTSEVM KNCSFKATTE
160 170 180 190 200
LKDKKHKVHA LFYKLDVVPL NGNSSSSGEY RLINCNTSAI TQACPKVSFD
210 220 230 240 250
PIPLHYCAPA GFAILKCNNK TFNGTGPCRN VSTVQCTHGI KPVVSTQLLL
260 270 280 290 300
NGSLAEEEII IRSENLTNNA KTIIVHLNES VNIVCTRPNN NTRKSIRIGP
310 320 330 340 350
GQTFYATGDI IGNIRQAHCN INESKWNNTL QKVGEELAKH FPSKTIKFEP
360 370 380 390 400
SSGGDLEITT HSFNCRGEFF YCNTSDLFNG TYRNGTYNHT GRSSNGTITL
410 420 430 440 450
QCKIKQIINM WQEVGRAIYA PPIEGEITCN SNITGLLLLR DGGQSNETND
460 470 480 490 500
TETFRPGGGD MRDNWRSELY KYKVVEIKPL GVAPTEAKRR VVEREKRAVG
510 520 530 540 550
IGAVFLGFLG AAGSTMGAAS MTLTVQARQL LSGIVQQQSN LLRAIEAQQH
560 570 580 590 600
MLQLTVWGIK QLQARVLAIE RYLKDQQLLG MWGCSGKLIC TTAVPWNSSW
610 620 630 640 650
SNKSQNEIWG NMTWMQWDRE INNYTNTIYR LLEDSQNQQE KNEKDLLALD
660 670 680 690 700
SWKNLWNWFD ISKWLWYIKI FIMIIGGLIG LRIIFAVLSI VKRVRQGYSP
710 720 730 740 750
LSFQTLTPNP RGPDRPGGIE EEGGEQDRDR SARLASGFLT LVWDDLRSLC
760 770 780 790 800
LFSYHLLRDF ILVATRTVEL LGRSSLKGLQ RGWEILRYLG SLVQYWGLEL
810 820 830 840
KKSAISLIDT IAIAVAERTD RIIEIVQRIC RAIRNIPRRI RQGFETALL
Length:849
Mass (Da):96,054
Last modified:September 1, 2009 - v1
Checksum:iAE4C240E240E501F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ444394 Genomic DNA. Translation: ACS67968.1.
FJ444395 Genomic DNA. Translation: ACS67969.1.
FJ444396 Genomic DNA. Translation: ACS67970.1.
FJ444399 Genomic DNA. Translation: ACS67972.1.
FJ444404 Genomic DNA. Translation: ACS67973.1.
FJ444407 Genomic DNA. Translation: ACS67976.1.
FJ444409 Genomic DNA. Translation: ACS67978.1.
FJ444410 Genomic DNA. Translation: ACS67979.1.
FJ444411 Genomic DNA. Translation: ACS67980.1.
FJ444414 Genomic DNA. Translation: ACS67982.1.
FJ444415 Genomic DNA. Translation: ACS67983.1.
KC894079 Genomic RNA. Translation: AGV38303.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ444394 Genomic DNA. Translation: ACS67968.1.
FJ444395 Genomic DNA. Translation: ACS67969.1.
FJ444396 Genomic DNA. Translation: ACS67970.1.
FJ444399 Genomic DNA. Translation: ACS67972.1.
FJ444404 Genomic DNA. Translation: ACS67973.1.
FJ444407 Genomic DNA. Translation: ACS67976.1.
FJ444409 Genomic DNA. Translation: ACS67978.1.
FJ444410 Genomic DNA. Translation: ACS67979.1.
FJ444411 Genomic DNA. Translation: ACS67980.1.
FJ444414 Genomic DNA. Translation: ACS67982.1.
FJ444415 Genomic DNA. Translation: ACS67983.1.
KC894079 Genomic RNA. Translation: AGV38303.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TGRX-ray2.80A/B39-478[»]
3TGSX-ray2.70A/B39-478[»]
4I53X-ray2.50A/B39-478[»]
4LSVX-ray3.00G39-478[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.170.40.20. 2 hits.
InterProiIPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]
PfamiPF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]
SUPFAMiSSF56502. SSF56502. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. Hraber P.T.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 1086-B12Imported, 1086-B2Imported, 1086-B5Imported, 1086-C2Imported, 1086-E12Imported, 1086-F8Imported, 1086-G1Imported, 1086-G12Imported, 1086-G2Imported, 1086-H1Imported and 1086-H9Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 1086-B12Imported, 1086-B2Imported, 1086-B5Imported, 1086-C2Imported, 1086-E12Imported, 1086-F8Imported, 1086-G1Imported, 1086-G12Imported, 1086-G2Imported, 1086-H1Imported and 1086-H9Imported.
  3. "Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops."
    Kwon Y.D., Finzi A., Wu X., Dogo-Isonagie C., Lee L.K., Moore L.R., Schmidt S.D., Stuckey J., Yang Y., Zhou T., Zhu J., Vicic D.A., Debnath A.K., Shapiro L., Bewley C.A., Mascola J.R., Sodroski J.G., Kwong P.D.
    Proc. Natl. Acad. Sci. U.S.A. 109:5663-5668(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 39-478, DISULFIDE BONDS, GLYCOSYLATION AT ASN-184 AND ASN-291.
  4. "Structure-Based Design and Synthesis of an HIV-1 Entry Inhibitor Exploiting X-Ray and Thermodynamic Characterization."
    Lalonde J.M., Le-Khac M., Jones D.M., Courter J.R., Park J., Schon A., Princiotto A.M., Wu X., Mascola J.R., Freire E., Sodroski J., Madani N., Hendrickson W.A., Smith A.B.
    ACS Med. Chem. Lett. 4:338-343(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 39-478, DISULFIDE BONDS, GLYCOSYLATION AT ASN-184 AND ASN-291.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 39-478, DISULFIDE BONDS, GLYCOSYLATION AT ASN-184 AND ASN-291.
  6. "Comparison of viral Env proteins from acute and chronic infections with subtype C human immunodeficiency virus type 1 identifies differences in glycosylation and CCR5 utilization and suggests a new strategy for immunogen design."
    Ping L.H., Joseph S.B., Anderson J.A., Abrahams M.R., Salazar-Gonzalez J.F., Kincer L.P., Treurnicht F.K., Arney L., Ojeda S., Zhang M., Keys J., Potter E.L., Chu H., Moore P., Salazar M.G., Iyer S., Jabara C., Kirchherr J.
    , Mapanje C., Ngandu N., Seoighe C., Hoffman I., Gao F., Tang Y., Labranche C., Lee B., Saville A., Vermeulen M., Fiscus S., Morris L., Karim S.A., Haynes B.F., Shaw G.M., Korber B.T., Hahn B.H., Cohen M.S., Montefiori D., Williamson C., Swanstrom R.
    J. Virol. 87:7218-7233(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 1086-B2Imported.
  7. Ping L.-H.
    Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 1086-B2Imported.

Entry informationi

Entry nameiC6G099_9HIV1
AccessioniPrimary (citable) accession number: C6G099
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: June 24, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.