Q8JSZ3 (GP_CCHFI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 29.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Envelope glycoprotein Short name=GP Alternative name(s): M polyprotein Cleaved into the following 3 chains: | ||
| Gene names |
| ||
| Organism | Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970) (CCHFV) [Reference proteome] | ||
| Taxonomic identifier | 652961 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Bunyaviridae › Nairovirus › ![]() | ||
| Virus host | Boophilus microplus (Cattle tick) [TaxID: 6941] Bos taurus (Bovine) [TaxID: 9913] Capra hircus (Goat) [TaxID: 9925] Homo sapiens (Human) [TaxID: 9606] Hyalomma [TaxID: 34625] Ovis aries (Sheep) [TaxID: 9940] |
Protein attributes
| Sequence length | 1684 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Glycoprotein G1 and glycoprotein G2 interact with each other and are present at the surface of the virion. They are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Also promote fusion of viral membrane with host endosomal membrane after endocytosis of the virion By similarity. Ref.3 |
| Subunit structure | G1 and G2 interacts with each other By similarity. |
| Subcellular location | Glycoprotein G1: Virion membrane; Single-pass type I membrane protein Potential. Host Golgi apparatus membrane; Single-pass type I membrane protein Potential. Host endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Note: Interaction between G1 and G2 is essential for proper targeting of G1 to the Golgi complex, where virion budding occurs By similarity. Glycoprotein G2: Virion membrane; Multi-pass membrane protein Potential. Host Golgi apparatus membrane; Multi-pass membrane protein Potential. |
| Post-translational modification | Specific enzymatic cleavages in vivo yield mature proteins including glycoprotein G1 and glycoprotein G2. |
| Sequence similarities | Belongs to the nairovirus envelope glycoprotein family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||
| Chain | 19 – 1684 | 1666 | Envelope glycoprotein By similarity | PRO_0000406564 | |||||
| Chain | 19 – 515 | 497 | Mucin-like variable region By similarity | PRO_0000406565 | |||||
| Chain | 516 – 1037 | 522 | Glycoprotein G2 Potential | PRO_0000406566 | |||||
| Chain | 1038 – 1684 | 647 | Glycoprotein G1 Potential | PRO_0000406567 | |||||
Regions | |||||||||
| Transmembrane | 699 – 719 | 21 | Helical; Potential | ||||||
| Transmembrane | 822 – 842 | 21 | Helical; Potential | ||||||
| Transmembrane | 860 – 880 | 21 | Helical; Potential | ||||||
| Transmembrane | 973 – 993 | 21 | Helical; Potential | ||||||
| Transmembrane | 1595 – 1615 | 21 | Helical; Potential | ||||||
| Compositional bias | 27 – 242 | 216 | Thr-rich | ||||||
| Compositional bias | 1165 – 1208 | 44 | Cys-rich | ||||||
Sites | |||||||||
| Site | 516 – 517 | 2 | Cleavage; by host By similarity | ||||||
| Site | 1037 – 1038 | 2 | Cleavage; by host signal peptidase By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 25 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 30 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 196 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 200 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 243 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 376 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 426 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 557 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 755 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 1054 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 1345 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 1563 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
Sequences
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References
| [1] | "Characterization of the glycoproteins of Crimean-Congo hemorrhagic fever virus." Sanchez A.J., Vincent M.J., Nichol S.T. J. Virol. 76:7263-7275(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [2] | Sanchez A.J., Vincent M.J., Deyde V.M., Khristova M.L., Nichol S.T. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [3] | "Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-, pH- and cholesterol-dependent." Simon M., Johansson C., Mirazimi A. J. Gen. Virol. 90:210-215(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF467768 Genomic RNA. Translation: AAM48106.1. |
| RefSeq | NP_950235.1. NC_005300.2. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2943074. |
Family and domain databases | |
| InterPro | IPR012487. Nairovirus_M. [Graphical view] |
| Pfam | PF07948. Nairovirus_M. 1 hit. [Graphical view] |
| PIRSF | PIRSF003962. M_poly_NairoV. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GP_CCHFI | ||||||||
| Accession | Primary (citable) accession number: Q8JSZ3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
