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P11818 (SPIKE_ADE05) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fiber protein

Short name=SPIKE
Alternative name(s):
Protein IV
Gene names
ORF Names:L5
OrganismHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) [Complete proteome]
Taxonomic identifier28285 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host coxsackievirus and adenovirus receptor CXADR located at the cell tight junctions to provide virion initial attachment to target cell. The fiber protein binds to CXADR with a higher affinity than CXADR binds to itself, thereby blocking the cell-cell adhesion function of CXADR dimers and leading to local disruption of the tight junction. Fiber protein present on neo-synthesized particles may thus disrupt the junctional integrity in order to facilitate further neighboring cells infection. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Fiber shedding is dependent on viral CXADR drifting motion and subsequent binding to immobile integrins. Heparan sulfate might also play a role in virus binding By similarity.

Subunit structure

Homotrimer; arranged in a triple beta-spiral. Interacts with host receptor CXADR. Interacts (via N-terminal tail region) with pentons By similarity.

Subcellular location

Virion By similarity. Host nucleus By similarity. Note: Anchored to the pentons, protrudes from the virion surface. Present in 36 copies per virion 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.

Post-translational modification

O-glycosylated; glycans contain N-acetylglucosamine and may play a role in fiber assembly and stabilization By similarity. Ref.4

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.

Contains 22 Shaft repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 581581Fiber protein
PRO_0000221789

Regions

Repeat45 – 5915Shaft 1
Repeat60 – 7516Shaft 2
Repeat76 – 9520Shaft 3
Repeat96 – 10914Shaft 4
Repeat110 – 12415Shaft 5
Repeat125 – 13915Shaft 6
Repeat140 – 15415Shaft 7
Repeat155 – 17016Shaft 8
Repeat171 – 18515Shaft 9
Repeat186 – 20015Shaft 10
Repeat201 – 21717Shaft 11
Repeat218 – 23215Shaft 12
Repeat233 – 24816Shaft 13
Repeat249 – 26517Shaft 14
Repeat266 – 27914Shaft 15
Repeat280 – 29617Shaft 16
Repeat297 – 31620Shaft 17
Repeat317 – 33317Shaft 18
Repeat334 – 35421Shaft 19
Repeat355 – 37016Shaft 20
Repeat371 – 38616Shaft 21
Repeat387 – 3926Shaft 22
Region1 – 4444Tail (penton base attachment) By similarity
Region45 – 392348Shaft region By similarity
Region393 – 3986Spacer By similarity
Region399 – 581183Head By similarity

Secondary structure

........................................ 581
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11818 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: C3FDDFCF9E5E599F

FASTA58161,585
        10         20         30         40         50         60 
MKRARPSEDT FNPVYPYDTE TGPPTVPFLT PPFVSPNGFQ ESPPGVLSLR LSEPLVTSNG 

        70         80         90        100        110        120 
MLALKMGNGL SLDEAGNLTS QNVTTVSPPL KKTKSNINLE ISAPLTVTSE ALTVAAAAPL 

       130        140        150        160        170        180 
MVAGNTLTMQ SQAPLTVHDS KLSIATQGPL TVSEGKLALQ TSGPLTTTDS STLTITASPP 

       190        200        210        220        230        240 
LTTATGSLGI DLKEPIYTQN GKLGLKYGAP LHVTDDLNTL TVATGPGVTI NNTSLQTKVT 

       250        260        270        280        290        300 
GALGFDSQGN MQLNVAGGLR IDSQNRRLIL DVSYPFDAQN QLNLRLGQGP LFINSAHNLD 

       310        320        330        340        350        360 
INYNKGLYLF TASNNSKKLE VNLSTAKGLM FDATAIAINA GDGLEFGSPN APNTNPLKTK 

       370        380        390        400        410        420 
IGHGLEFDSN KAMVPKLGTG LSFDSTGAIT VGNKNNDKLT LWTTPAPSPN CRLNAEKDAK 

       430        440        450        460        470        480 
LTLVLTKCGS QILATVSVLA VKGSLAPISG TVQSAHLIIR FDENGVLLNN SFLDPEYWNF 

       490        500        510        520        530        540 
RNGDLTEGTA YTNAVGFMPN LSAYPKSHGK TAKSNIVSQV YLNGDKTKPV TLTITLNGTQ 

       550        560        570        580 
ETGDTTPSAY SMSFSWDWSG HNYINEIFAT SSYTFSYIAQ E 

« Hide

References

[1]"The sequence of adenovirus fiber: similarities and differences between serotypes 2 and 5."
Chroboczek J., Jacrot B.
Virology 161:549-554(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2."
Chroboczek J., Bieber F., Jacrot B.
Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"De novo derivation of proteomes from transcriptomes for transcript and protein identification."
Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.
Nat. Methods 9:1207-1211(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Relative accessibility of N-acetylglucosamine in trimers of the adenovirus types 2 and 5 fiber proteins."
Mullis K.G., Haltiwanger R.S., Hart G.W., Marchase R.B., Engler J.A.
J. Virol. 64:5317-5323(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[5]"Adenovirus receptors."
Zhang Y., Bergelson J.M.
J. Virol. 79:12125-12131(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7-A resolution."
Xia D., Henry L.J., Gerard R.D., Deisenhofer J.
Structure 2:1259-1270(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 386-581.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73260 Genomic DNA. No translation available.
M18369 Genomic DNA. Translation: AAA42504.1.
PIRERADF5. A27404.
RefSeqAP_000226.1. AC_000008.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNBX-ray1.70A386-581[»]
4ATZX-ray1.95A/B/C387-581[»]
ProteinModelPortalP11818.
SMRP11818. Positions 321-581.
ModBaseSearch...
MobiDBSearch...

PTM databases

UniCarbKBP11818.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.25.20. 3 hits.
2.60.90.10. 1 hit.
InterProIPR000931. Adeno_fibre.
IPR000978. Adeno_fibre_knob.
IPR000939. Adenobir_fibre_prot_rpt/shaft.
IPR008982. Adenovirus_pIV-rel_att.
IPR009013. Attachment_protein_shaft_dom.
[Graphical view]
PfamPF00541. Adeno_knob. 1 hit.
PF00608. Adeno_shaft. 6 hits.
[Graphical view]
PRINTSPR00307. ADENOVSFIBRE.
SUPFAMSSF49835. SSF49835. 1 hit.
SSF51225. SSF51225. 4 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP11818.

Entry information

Entry nameSPIKE_ADE05
AccessionPrimary (citable) accession number: P11818
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references