P03275 (SPIKE_ADE02) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fiber protein
Short name=SPIKE

Alternative name(s):
Protein IV

Gene names

ORF Names:

L5

Organism

Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) [Reference proteome]

Taxonomic identifier

10515 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Adenoviridae › Mastadenovirus › Human adenovirus C

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	582 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 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. Ref.5 Ref.7 Ref.8 Ref.10
Subunit structure	Homotrimer; arranged in a triple beta-spiral. Interacts with host receptor CXADR. Interacts (via N-terminal tail region) with pentons Probable. Ref.6 Ref.12
Subcellular location	Virion. Host nucleus Probable. Note: Anchored to the pentons, protrudes from the virion surface. Present in 36 copies per virion. Ref.12
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.
Post-translational modification	O-glycosylated; glycans contain N-acetylglucosamine and may play a role in fiber assembly and stabilization. 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.
Sequence similarities	Belongs to the adenoviridae fiber family. Contains 22 Shaft repeats.

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
Domain	Repeat
Molecular function	Capsid protein
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: InterPro pathogenesis Inferred from electronic annotation. Source: InterPro viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW viral infectious cycle Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsid Inferred 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 – 582

582

Fiber protein

PRO_0000221786

Regions

Repeat

45 – 59

15

Shaft 1

Repeat

60 – 75

16

Shaft 2

Repeat

76 – 95

20

Shaft 3

Repeat

96 – 109

14

Shaft 4

Repeat

110 – 124

15

Shaft 5

Repeat

125 – 139

15

Shaft 6

Repeat

140 – 154

15

Shaft 7

Repeat

155 – 170

16

Shaft 8

Repeat

171 – 185

15

Shaft 9

Repeat

186 – 200

15

Shaft 10

Repeat

201 – 217

17

Shaft 11

Repeat

218 – 232

15

Shaft 12

Repeat

233 – 248

16

Shaft 13

Repeat

249 – 263

15

Shaft 14

Repeat

264 – 277

14

Shaft 15

Repeat

278 – 294

17

Shaft 16

Repeat

295 – 314

20

Shaft 17

Repeat

315 – 331

17

Shaft 18

Repeat

332 – 354

23

Shaft 19

Repeat

355 – 370

16

Shaft 20

Repeat

371 – 386

16

Shaft 21

Repeat

387 – 392

6

Shaft 22

Region

1 – 44

44

Tail (penton base attachment)

Region

45 – 392

348

Shaft region

Region

393 – 398

6

Spacer

Region

399 – 582

184

Head

Amino acid modifications

Modified residue

325

1

Phosphoserine; by host Ref.2

Modified residue

351

1

Phosphoserine; by host Ref.2

Secondary structure

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582

Helix Strand Turn

Details...

Helix

323 – 325

3

Beta strand

327 – 330

4

Beta strand

333 – 336

4

Beta strand

342 – 344

3

Turn

349 – 353

5

Beta strand

357 – 359

3

Beta strand

365 – 367

3

Beta strand

373 – 375

3

Beta strand

381 – 383

3

Turn

385 – 387

3

Beta strand

389 – 391

3

Helix

397 – 399

3

Beta strand

400 – 403

4

Beta strand

413 – 415

3

Beta strand

419 – 428

10

Beta strand

431 – 440

10

Helix

446 – 448

3

Beta strand

450 – 461

12

Beta strand

469 – 473

5

Beta strand

479 – 482

4

Helix

495 – 497

3

Turn

501 – 503

3

Helix

512 – 514

3

Beta strand

515 – 521

7

Helix

522 – 524

3

Beta strand

528 – 537

10

Helix

538 – 540

3

Beta strand

550 – 558

9

Beta strand

574 – 580

7

Sequences

	Sequence		Length	Mass (Da)
	P03275 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 8C315CE5EDC9505F	FASTA	582	61,919
	10 20 30 40 50 60 MKRARPSEDT FNPVYPYDTE TGPPTVPFLT PPFVSPNGFQ ESPPGVLSLR VSEPLDTSHG 70 80 90 100 110 120 MLALKMGSGL TLDKAGNLTS QNVTTVTQPL KKTKSNISLD TSAPLTITSG ALTVATTAPL 130 140 150 160 170 180 IVTSGALSVQ SQAPLTVQDS KLSIATKGPI TVSDGKLALQ TSAPLSGSDS DTLTVTASPP 190 200 210 220 230 240 LTTATGSLGI NMEDPIYVNN GKIGIKISGP LQVAQNSDTL TVVTGPGVTV EQNSLRTKVA 250 260 270 280 290 300 GAIGYDSSNN MEIKTGGGMR INNNLLILDV DYPFDAQTKL RLKLGQGPLY INASHNLDIN 310 320 330 340 350 360 YNRGLYLFNA SNNTKKLEVS IKKSSGLNFD NTAIAINAGK GLEFDTNTSE SPDINPIKTK 370 380 390 400 410 420 IGSGIDYNEN GAMITKLGAG LSFDNSGAIT IGNKNDDKLT LWTTPDPSPN CRIHSDNDCK 430 440 450 460 470 480 FTLVLTKCGS QVLATVAALA VSGDLSSMTG TVASVSIFLR FDQNGVLMEN SSLKKHYWNF 490 500 510 520 530 540 RNGNSTNANP YTNAVGFMPN LLAYPKTQSQ TAKNNIVSQV YLHGDKTKPM ILTITLNGTS 550 560 570 580 ESTETSEVST YSMSFTWSWE SGKYTTETFA TNSYTFSYIA QE

References

[1]	"Nucleotide sequence of the EcoRI E fragment of adenovirus 2 genome." Herisse J., Galibert F. Nucleic Acids Res. 9:1229-1240(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-411.
[2]	"The phosphoproteome of the adenovirus type 2 virion." Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J., Pettersson U. Virology 433:253-261(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 324-358, PHOSPHORYLATION AT SER-325 AND SER-351.
[3]	"Nucleotide sequence of adenovirus 2 DNA fragment encoding for the carboxylic region of the fiber protein and the entire E4 region." Herisse J., Rigolet M., Dupont de Dinechin S., Galibert F. Nucleic Acids Res. 9:4023-4042(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 382-582.
[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. Strain: Human adenovirus C serotype 5.
[5]	"Adenovirus internalization and infection require dynamin." Wang K., Huang S., Kapoor-Munshi A., Nemerow G. J. Virol. 72:3455-3458(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F." Roelvink P.W., Lizonova A., Lee J.G.M., Li Y., Bergelson J.M., Finberg R.W., Brough D.E., Kovesdi I., Wickham T.J. J. Virol. 72:7909-7915(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN CXADR.
[7]	"Heparan sulfate glycosaminoglycans are involved in adenovirus type 5 and 2-host cell interactions." Dechecchi M.C., Tamanini A., Bonizzato A., Cabrini G. Virology 268:382-390(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape." Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J. Cell 110:789-799(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Adenovirus endocytosis." Meier O., Greber U.F. J. Gene Med. 6:S152-S163(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[10]	"Drifting motions of the adenovirus receptor CAR and immobile integrins initiate virus uncoating and membrane lytic protein exposure." Burckhardt C.J., Suomalainen M., Schoenenberger P., Boucke K., Hemmi S., Greber U.F. Cell Host Microbe 10:105-117(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Latest insights on adenovirus structure and assembly." San Martin C. Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[12]	"A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein." van Raaij M.J., Mitraki A., Lavigne G., Cusack S. Nature 401:935-938(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 319-582, INTERACTION WITH PENTON PROTEIN, SUBCELLULAR LOCATION.
[13]	"Structure of the human adenovirus serotype 2 fiber head domain at 1.5 A resolution." van Raaij M.J., Louis N., Chroboczek J., Cusack S. Virology 262:333-343(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 388-582.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01917 Genomic DNA. Translation: AAA92223.1.

PIR

ERADF2. A93722.

RefSeq

AP_000190.1. AC_000007.1.
NP_040533.1. NC_001405.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QHV	X-ray	1.51	A	388-582	[»]
1QIU	X-ray	2.40	A/B/C/D/E/F	319-582	[»]
1V1H	X-ray	1.90	A/B/C/D/E/F	319-392	[»]
1V1I	X-ray	1.90	A/B/C	319-398	[»]
2C9F	electron microscopy	16.50	S/T/U/V/W	1-19	[»]
4AR2	X-ray	3.80	P	1-20	[»]

ProteinModelPortal

P03275.

SMR

P03275. Positions 319-582.

ModBase

Search...

PTM databases

GlycoSuiteDB

P03275.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2652999.

Family and domain databases

Gene3D

2.10.25.20. 3 hits.
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. 6 hits.
[Graphical view]

PRINTS

PR00307. ADENOVSFIBRE.

SUPFAM

SSF49835. Viral_att. 1 hit.
SSF51225. Viral_att_shaft. 4 hits.

ProtoNet

Search...

Other

EvolutionaryTrace

P03275.

Entry information

Entry name

SPIKE_ADE02

Accession

Primary (citable) accession number: P03275

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program