P15141 (SPIKE_ADE07) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 70.
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: Fiber protein Short name=SPIKE Alternative name(s): Protein IV | ||
| Gene names |
| ||
| Organism | Human adenovirus B serotype 7 (HAdV-7) (Human adenovirus 7) | ||
| Taxonomic identifier | 10519 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Adenoviridae › Mastadenovirus › Human adenovirus B › ![]() | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 343 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Ref.2 |
| Subunit structure | Homotrimer. Interacts with host receptor CD46. Interacts (via N-terminal tail region) with pentons By similarity. Ref.3 |
| Subcellular location | Virion By similarity. Host nucleus By similarity. Note: Anchored to the pentons, protrudes from the virion surface By similarity. |
| Induction | Expressed in the late phase of the viral replicative cycle. |
| Domain | The tail region anchors the fiber to penton base capsomers, whereas the shaft, built from several repeated motifs, allows the knob to protrude from the virion By similarity. |
| Miscellaneous | All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell By similarity. |
| Sequence similarities | Belongs to the adenoviridae fiber family. |
| Sequence caution | The sequence AAA53254.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction Viral attachment to host cell Virus entry into host cell |
| Cellular component | Host nucleus Virion |
| Developmental stage | Late protein |
| Molecular function | Capsid protein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological_process | cell adhesion Inferred from electronic annotation. Source: InterPro pathogenesisInferred from electronic annotation. Source: InterPro viral attachment to host cellInferred from electronic annotation. Source: UniProtKB-KW viral entry into host cellInferred from electronic annotation. Source: UniProtKB-KW viral infectious cycleInferred from electronic annotation. Source: InterPro |
| Cellular_component | host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsidInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 343 | 343 | Fiber protein | PRO_0000221790 | |||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Helix | 147 – 150 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 153 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 174 – 183 | 10 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 186 – 195 | 10 | |||||||||||||||||||||||||||||||||||||
| Helix | 198 – 201 | 4 | |||||||||||||||||||||||||||||||||||||
| Helix | 202 – 205 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 207 – 217 | 11 | |||||||||||||||||||||||||||||||||||||
| Turn | 225 – 227 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 228 – 230 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 250 – 253 | 4 | |||||||||||||||||||||||||||||||||||||
| Turn | 257 – 259 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 265 – 271 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 272 – 280 | 9 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 286 – 298 | 13 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 305 – 315 | 11 | |||||||||||||||||||||||||||||||||||||
| Turn | 323 – 325 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 334 – 340 | 7 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Characterization of the early region 3 and fiber genes of Ad7." Hong J.S., Mullis K.G., Engler J.A. Virology 167:545-553(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Gomen. |
| [2] | "Adenovirus serotype 7 retention in a late endosomal compartment prior to cytosol escape is modulated by fiber protein." Miyazawa N., Crystal R.G., Leopold P.L. J. Virol. 75:1387-1400(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [3] | "Avidity binding of human adenovirus serotypes 3 and 7 to the membrane cofactor CD46 triggers infection." Trinh H.V., Lesage G., Chennamparampil V., Vollenweider B., Burckhardt C.J., Schauer S., Havenga M., Greber U.F., Hemmi S. J. Virol. 86:1623-1637(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN CD46. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M23696 Genomic DNA. Translation: AAA53254.1. Different initiation. | ||||||||||||
| PIR | ERADF7. F31830. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P15141. | ||||||||||||
| SMR | P15141. Positions 147-343. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 2.10.25.20. 1 hit. 2.60.90.10. 1 hit. | ||||||||||||
| InterPro | IPR000931. Adeno_fibre. IPR000978. Adeno_fibre_knob. IPR000939. Adenobir_fibre_prot_rpt/shaft. IPR008982. Adenovirus_pIV-rel_att. IPR009013. Attachment_protein_shaft_dom. [Graphical view] | ||||||||||||
| Pfam | PF00541. Adeno_knob. 1 hit. PF00608. Adeno_shaft. 2 hits. [Graphical view] | ||||||||||||
| PRINTS | PR00307. ADENOVSFIBRE. | ||||||||||||
| SUPFAM | SSF49835. Viral_att. 1 hit. SSF51225. Viral_att_shaft. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P15141. | ||||||||||||
Entry information
| Entry name | SPIKE_ADE07 | ||||||||
| Accession | Primary (citable) accession number: P15141 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
