ENV - Envelope polyprotein

HIV ENV is a polyprotein precursor (gp160), which is processed by cellular proteases to give a non-covalent complex of an external glycoprotein (SU / gp120) and a transmembrane glycoprotein (TM / gp41)


PDB-1GC1: Envelope protein complex with gp120 (pink ribbon), CD4 (yellow ribbon), Antibody 17B light chain (blue ribbon) and Antibody 17B heavy chain (green ribbon) - produced using SwissModel/SPDBV/POVray
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PDB: 1GC1 (HIV-1 ENV)
SwissProt: P04578 (HIV-1 HXB2 ENV)
Chime Tutorial: not available
Los Alamos HIV structure DB: HIV ENV
EMBL: K03455 [EMBL/GenBank/DDBJ]
BioAfrica: Env Protein Data Mining Tool


Description:

HIV ENV is a polyprotein precursor (gp160), which is processed by cellular proteases to give a non-covalent complex of an external glycoprotein (SU / gp120) and a transmembrane glycoprotein (TM / gp41).


Localization:

  • Endoplasmic Reticulum
  • Golgi complex
  • virion

Function:

  • structural protein
  • polyprotein precursor for glycoproteins that occur on the surface of virions
  • form complexes with CD4 receptors within Endoplasmic Reticulum, decreases their presence on the cell surface

Additional Information:

  • translated from singly spliced mRNA
  • synthesized in the Endoplasmic Reticulum
  • migrates through the Golgi complex
  • undergoes glycosylation within Golgi complex
  • glycosylation consists of 25 to 30 complex N-linked carbohydrate side chains on Asparagine residues
  • glycosylation is required for infectivity (Ref. #3)

Genomic Location: [TOP]

Reference Sequences:

HIV-1 (HXB2): 

          10         20         30         40         50         60         70
           |          |          |          |          |          |          |
  MRVKEKYQHL WRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA YDTEVHNVWA 
          80         90        100        110        120        130        140
           |          |          |          |          |          |          |
  THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV KLTPLCVSLK CTDLKNDTNT 
         150        160        170        180        190        200        210
           |          |          |          |          |          |          |
  NSSSGRMIME KGEIKNCSFN ISTSIRGKVQ KEYAFFYKLD IIPIDNDTTS YKLTSCNTSV ITQACPKVSF 
         220        230        240        250        260        270        280
           |          |          |          |          |          |          |
  EPIPIHYCAP AGFAILKCNN KTFNGTGPCT NVSTVQCTHG IRPVVSTQLL LNGSLAEEEV VIRSVNFTDN 
         290        300        310        320        330        340        350
           |          |          |          |          |          |          |
  AKTIIVQLNT SVEINCTRPN NNTRKRIRIQ RGPGRAFVTI GKIGNMRQAH CNISRAKWNN TLKQIASKLR 
         360        370        380        390        400        410        420
           |          |          |          |          |          |          |
  EQFGNNKTII FKQSSGGDPE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW STEGSNNTEG SDTITLPCRI 
         430        440        450        460        470        480        490
           |          |          |          |          |          |          |
  KQIINMWQKV GKAMYAPPIS GQIRCSSNIT GLLLTRDGGN SNNESEIFRP GGGDMRDNWR SELYKYKVVK 
         500        510        520        530        540        550        560
           |          |          |          |          |          |          |
  IEPLGVAPTK AKRRVVQREK RAVGIGALFL GFLGAAGSTM GAASMTLTVQ ARQLLSGIVQ QQNNLLRAIE 
         570        580        590        600        610        620        630
           |          |          |          |          |          |          |
  AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG KLICTTAVPW NASWSNKSLE QIWNHTTWME 
         640        650        660        670        680        690        700
           |          |          |          |          |          |          |
  WDREINNYTS LIHSLIEESQ NQQEKNEQEL LELDKWASLW NWFNITNWLW YIKLFIMIVG GLVGLRIVFA 
         710        720        730        740        750        760        770
           |          |          |          |          |          |          |
  VLSIVNRVRQ GYSPLSFQTH LPTPRGPDRP EGIEEEGGER DRDRSIRLVN GSLALIWDDL RSLCLFSYHR 
         780        790        800        810        820        830        840
           |          |          |          |          |          |          |
  LRDLLLIVTR IVELLGRRGW EALKYWWNLL QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGACRAI 
         850 
           | 
  RHIPRRIRQG LERILL 
      [download in fasta format]

Length: 856 amino acids
Molecular Weight: 97212 Da
Theoretical pI: 9.17
Protein Domains/Folds/Motifs: [TOP]

InterPro signature for gp41 - IPR000328

InterPro signature for gp120 - IPR000777


Secondary Structure prediction:

Transmembrane Regions - tmhmm:


Coiled Coil Regions - ncoils:


Low Complexity Regions - seg:


Antigenic Sites - EMBOSS:


Signal peptide Region (residues 1 - 30)

gp120 Region (residues 31 - 511)


gp41 Region (residues 512 - 856)
Predicted Motifs: Printer-friendly version
N-glycosylation:
N-myristoylation:
Amidation:
Protein kinase C:
Casein kinase II:
Tyrosine kinase:
cAMP / cGMP kinase:
Cell attachment motif:
Asp Protease motif:
Asp Prot Retro motif:
Cysteine-rich Region:
Tryptophan-rich Region:
Zinc-finger CCHC motif:
Leucine Zipper motif:

Protein-Protein Interactions: [TOP]

  • Host endoproteases (including furin) cleave HIV Env polyprotein in the highly conserved domain at the carboxy terminus, consisting of residues: Arg-X-Lys/Arg-Arg (Ref. #4)
  • Env binds to the molecular chaperone BiP


Primary and Secondary Database Entries: [TOP]

Identifiers:

PDB/MMDB: Search for HIV-1 & Env

SwissProt: P04578 (HIV-1 HXB2 ENV)
EMBL: K03455; AAB50262.1 [EMBL/GenBank/DDBJ]

PIR: UNKNOWN
HIV: K03455; ENV$HXB2
InterPro: IPR000328 - gp41 family / IPR000777 - gp120 family
Pfam: PF00517 - gp41 family / PF00517 - gp120 family
Prints: none
ProDom: PD616511 (3 - 23) / PD551838 (20 - 194) / PD597348 (24 - 82) / PD553839 (82 - 132)
PD000193 (83 - 133) / PD000124 (83 - 172) / PD529973 (85 - 132) / PD591903 (128 - 157)
PD579607 (158 - 193)/ PD499504 (158 - 187) / PD000123 (178 - 203) / PD000124 (195 - 492)
PD614419 (330 - 391) / PD561449 (368 - 491) / PD527975 (403 - 492) / PD555302 (486 - 542)
PD598762 (493 - 541)/ PD001599 (508 - 679) / PD000125 (542 - 591) / PD605682 (592 - 618)
PD460876 (593 - 640) / PD628734 (619 - 640)/ PD657031 (620 - 639) / PD553288 (664 - 715)
PD653931 (670 - 716)/ PD000116 (670 - 716) / PD000205 (717 - 795) / PD000745 (796 - 856)
PD000212 (797 - 843)
SCOP: SSF56502 - gp120 core / SSF52440 - preATP-grasp domain / SSF56349 - DNA breaking-rejoining motif
BLOCKS: P04578
Prosite: P04578
ProtoNet: P04578
ProtoMap: P04578
PRESAGE: P04578
Database of Interacting Proteins: P04578
ModBase: P04578
Swiss-2DPAGE: 2D gel

BioAfrica Tools:
- Env Protein Data Mining Tool provides real-time analysis of HIV-1 Env isolates
- HIV Structure BLAST searches for similar HIV sequences that have known structures
- HIV Proteomics Resource contains protein sequence and structure analysis tools
Reviews and References: [TOP]

1 - HIV Sequence Compendium 2000
Kuiken CL, Foley B, Hahn B, Korber B, Marx PA, McCutchan F, Mellors JW, Mullins JI, Sodroski J, Wolinksy S.
Theoretical Biol. & Biophys. Group, Los Alamos Nat Lab, LA-UR 01-3860 [Read it online: Compendium]
2 - Retroviruses
Coffin JM, Hughes SH, Varmus HE.
CD-ROM ed. (2002) Cold Spring Harbor Laboratory Press [Read it online: NCBI Bookshelf]
3 - The CD4-gp120 interaction and AIDS pathogenesis.
Capon DJ, Ward RH.
Annu Rev Immunol. 9: 649-678 (1991) [pubmed: 92000518]
4 - Maturation of HIV envelope glycoprotein precursors by cellular endoproteases
Moulard M, Decroly E.
Biochim Biophys Acta 1469(3): 121-132 (2000) [pubmed: 11063880]


Page last updated by Tulio de Oliveira.