SPIKE_ADE02
ID SPIKE_ADE02 Reviewed; 582 AA.
AC P03275;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 132.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-411.
RX PubMed=6262722; DOI=10.1093/nar/9.5.1229;
RA Herisse J., Galibert F.;
RT "Nucleotide sequence of the EcoRI E fragment of adenovirus 2 genome.";
RL Nucleic Acids Res. 9:1229-1240(1981).
RN [2]
RP PROTEIN SEQUENCE OF 324-358, AND PHOSPHORYLATION AT SER-325 AND SER-351.
RX PubMed=22939182; DOI=10.1016/j.virol.2012.08.012;
RA Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J.,
RA Pettersson U.;
RT "The phosphoproteome of the adenovirus type 2 virion.";
RL Virology 433:253-261(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 382-582.
RX PubMed=6985482; DOI=10.1093/nar/9.16.4023;
RA Herisse J., Rigolet M., Dupont de Dinechin S., Galibert F.;
RT "Nucleotide sequence of adenovirus 2 DNA fragment encoding for the
RT carboxylic region of the fiber protein and the entire E4 region.";
RL Nucleic Acids Res. 9:4023-4042(1981).
RN [4]
RP GLYCOSYLATION.
RC STRAIN=Human adenovirus C serotype 5;
RX PubMed=2120471; DOI=10.1128/jvi.64.11.5317-5323.1990;
RA Mullis K.G., Haltiwanger R.S., Hart G.W., Marchase R.B., Engler J.A.;
RT "Relative accessibility of N-acetylglucosamine in trimers of the adenovirus
RT types 2 and 5 fiber proteins.";
RL J. Virol. 64:5317-5323(1990).
RN [5]
RP FUNCTION.
RX PubMed=9525681; DOI=10.1128/jvi.72.4.3455-3458.1998;
RA Wang K., Huang S., Kapoor-Munshi A., Nemerow G.;
RT "Adenovirus internalization and infection require dynamin.";
RL J. Virol. 72:3455-3458(1998).
RN [6]
RP INTERACTION WITH HUMAN CXADR.
RX PubMed=9733828; DOI=10.1128/jvi.72.10.7909-7915.1998;
RA Roelvink P.W., Lizonova A., Lee J.G.M., Li Y., Bergelson J.M.,
RA Finberg R.W., Brough D.E., Kovesdi I., Wickham T.J.;
RT "The coxsackievirus-adenovirus receptor protein can function as a cellular
RT attachment protein for adenovirus serotypes from subgroups A, C, D, E, and
RT F.";
RL J. Virol. 72:7909-7915(1998).
RN [7]
RP FUNCTION.
RX PubMed=10704346; DOI=10.1006/viro.1999.0171;
RA Dechecchi M.C., Tamanini A., Bonizzato A., Cabrini G.;
RT "Heparan sulfate glycosaminoglycans are involved in adenovirus type 5 and
RT 2-host cell interactions.";
RL Virology 268:382-390(2000).
RN [8]
RP FUNCTION.
RX PubMed=12297051; DOI=10.1016/s0092-8674(02)00912-1;
RA Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J.;
RT "Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing
RT virus escape.";
RL Cell 110:789-799(2002).
RN [9]
RP REVIEW.
RX PubMed=14978758; DOI=10.1002/jgm.553;
RA Meier O., Greber U.F.;
RT "Adenovirus endocytosis.";
RL J. Gene Med. 6:S152-S163(2004).
RN [10]
RP FUNCTION.
RX PubMed=21843868; DOI=10.1016/j.chom.2011.07.006;
RA Burckhardt C.J., Suomalainen M., Schoenenberger P., Boucke K., Hemmi S.,
RA Greber U.F.;
RT "Drifting motions of the adenovirus receptor CAR and immobile integrins
RT initiate virus uncoating and membrane lytic protein exposure.";
RL Cell Host Microbe 10:105-117(2011).
RN [11]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 319-582, INTERACTION WITH PENTON
RP PROTEIN, AND SUBCELLULAR LOCATION.
RX PubMed=10553913; DOI=10.1038/44880;
RA van Raaij M.J., Mitraki A., Lavigne G., Cusack S.;
RT "A triple beta-spiral in the adenovirus fibre shaft reveals a new
RT structural motif for a fibrous protein.";
RL Nature 401:935-938(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 388-582.
RX PubMed=10502512; DOI=10.1006/viro.1999.9849;
RA van Raaij M.J., Louis N., Chroboczek J., Cusack S.;
RT "Structure of the human adenovirus serotype 2 fiber head domain at 1.5 A
RT resolution.";
RL Virology 262:333-343(1999).
CC -!- FUNCTION: Forms spikes that protrude from each vertex of the
CC icosahedral capsid. Interacts with host coxsackievirus and adenovirus
CC receptor CXADR located at the cell tight junctions to provide virion
CC initial attachment to target cell. The fiber protein binds to CXADR
CC with a higher affinity than CXADR binds to itself, thereby blocking the
CC cell-cell adhesion function of CXADR dimers and leading to local
CC disruption of the tight junction. Fiber protein present on neo-
CC synthesized particles may thus disrupt the junctional integrity in
CC order to facilitate further neighboring cells infection. Fiber proteins
CC are shed during virus entry, when virus is still at the cell surface.
CC Fiber shedding is dependent on viral CXADR drifting motion and
CC subsequent binding to immobile integrins. Heparan sulfate might also
CC play a role in virus binding. {ECO:0000269|PubMed:10704346,
CC ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:21843868,
CC ECO:0000269|PubMed:9525681}.
CC -!- SUBUNIT: Homotrimer; arranged in a triple beta-spiral. Interacts with
CC host receptor CXADR. Interacts (via N-terminal tail region) with
CC pentons (Probable). {ECO:0000305|PubMed:10553913,
CC ECO:0000305|PubMed:9733828}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:10553913}. Host
CC nucleus {ECO:0000305|PubMed:10553913}. Note=Anchored to the pentons,
CC protrudes from the virion surface. Present in 36 copies per virion.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- DOMAIN: The tail region anchors the fiber to penton base capsomers,
CC whereas the shaft, built from several repeated motifs, allows the knob
CC to protrude from the virion.
CC -!- PTM: O-glycosylated; glycans contain N-acetylglucosamine and may play a
CC role in fiber assembly and stabilization. {ECO:0000269|PubMed:2120471}.
CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC are produced by alternative splicing and alternative polyadenylation of
CC the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC present in the N-terminus of all these mRNAs and is recognized by the
CC viral shutoff protein to provide expression although conventional
CC translation via ribosome scanning from the cap has been shut off in the
CC host cell.
CC -!- SIMILARITY: Belongs to the adenoviridae fiber family. {ECO:0000305}.
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DR EMBL; J01917; AAA92223.1; -; Genomic_DNA.
DR PIR; A93722; ERADF2.
DR RefSeq; AP_000190.1; AC_000007.1.
DR RefSeq; NP_040533.1; NC_001405.1.
DR PDB; 1QHV; X-ray; 1.51 A; A=388-582.
DR PDB; 1QIU; X-ray; 2.40 A; A/B/C/D/E/F=319-582.
DR PDB; 1V1H; X-ray; 1.90 A; A/B/C/D/E/F=319-392.
DR PDB; 1V1I; X-ray; 1.90 A; A/B/C=319-398.
DR PDB; 1X9T; X-ray; 3.50 A; B=1-20.
DR PDB; 2C9F; EM; 16.50 A; S/T/U/V/W=1-19.
DR PDB; 4AR2; X-ray; 3.80 A; P=1-20.
DR PDB; 4V4U; EM; 10.00 A; S/T/U/V/W=10-19.
DR PDBsum; 1QHV; -.
DR PDBsum; 1QIU; -.
DR PDBsum; 1V1H; -.
DR PDBsum; 1V1I; -.
DR PDBsum; 1X9T; -.
DR PDBsum; 2C9F; -.
DR PDBsum; 4AR2; -.
DR PDBsum; 4V4U; -.
DR SMR; P03275; -.
DR iPTMnet; P03275; -.
DR GeneID; 2652999; -.
DR KEGG; vg:2652999; -.
DR EvolutionaryTrace; P03275; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.90.10; -; 1.
DR InterPro; IPR000931; Adeno_fibre.
DR InterPro; IPR000978; Adeno_fibre_knob.
DR InterPro; IPR000939; Adenobir_fibre_prot_rpt/shaft.
DR InterPro; IPR008982; Adenovirus_pIV-like_att.
DR InterPro; IPR009013; Attachment_protein_shaft_sf.
DR Pfam; PF00541; Adeno_knob; 1.
DR Pfam; PF00608; Adeno_shaft; 6.
DR PRINTS; PR00307; ADENOVSFIBRE.
DR SUPFAM; SSF49835; SSF49835; 1.
DR SUPFAM; SSF51225; SSF51225; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing; Glycoprotein;
KW Host nucleus; Host-virus interaction; Late protein; Phosphoprotein;
KW Reference proteome; Repeat; Viral attachment to host adhesion receptor;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..582
FT /note="Fiber protein"
FT /id="PRO_0000221786"
FT REPEAT 45..59
FT /note="Shaft 1"
FT REPEAT 60..75
FT /note="Shaft 2"
FT REPEAT 76..95
FT /note="Shaft 3"
FT REPEAT 96..109
FT /note="Shaft 4"
FT REPEAT 110..124
FT /note="Shaft 5"
FT REPEAT 125..139
FT /note="Shaft 6"
FT REPEAT 140..154
FT /note="Shaft 7"
FT REPEAT 155..170
FT /note="Shaft 8"
FT REPEAT 171..185
FT /note="Shaft 9"
FT REPEAT 186..200
FT /note="Shaft 10"
FT REPEAT 201..217
FT /note="Shaft 11"
FT REPEAT 218..232
FT /note="Shaft 12"
FT REPEAT 233..248
FT /note="Shaft 13"
FT REPEAT 249..263
FT /note="Shaft 14"
FT REPEAT 264..277
FT /note="Shaft 15"
FT REPEAT 278..294
FT /note="Shaft 16"
FT REPEAT 295..314
FT /note="Shaft 17"
FT REPEAT 315..331
FT /note="Shaft 18"
FT REPEAT 332..354
FT /note="Shaft 19"
FT REPEAT 355..370
FT /note="Shaft 20"
FT REPEAT 371..386
FT /note="Shaft 21"
FT REPEAT 387..392
FT /note="Shaft 22"
FT REGION 1..44
FT /note="Tail (penton base attachment)"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..392
FT /note="Shaft region"
FT REGION 393..398
FT /note="Spacer"
FT REGION 399..582
FT /note="Head"
FT MOD_RES 325
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:22939182"
FT MOD_RES 351
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:22939182"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:1V1H"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1V1H"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1V1H"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1V1H"
FT TURN 349..353
FT /evidence="ECO:0007829|PDB:1V1H"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1V1H"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1V1H"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1V1H"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:1V1I"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:1QIU"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1V1H"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 419..428
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 431..440
FT /evidence="ECO:0007829|PDB:1QHV"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 450..461
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:1QHV"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:1QHV"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:1QHV"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:1QHV"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 528..537
FT /evidence="ECO:0007829|PDB:1QHV"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 550..558
FT /evidence="ECO:0007829|PDB:1QHV"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:1QHV"
SQ SEQUENCE 582 AA; 61919 MW; 8C315CE5EDC9505F CRC64;
MKRARPSEDT FNPVYPYDTE TGPPTVPFLT PPFVSPNGFQ ESPPGVLSLR VSEPLDTSHG
MLALKMGSGL TLDKAGNLTS QNVTTVTQPL KKTKSNISLD TSAPLTITSG ALTVATTAPL
IVTSGALSVQ SQAPLTVQDS KLSIATKGPI TVSDGKLALQ TSAPLSGSDS DTLTVTASPP
LTTATGSLGI NMEDPIYVNN GKIGIKISGP LQVAQNSDTL TVVTGPGVTV EQNSLRTKVA
GAIGYDSSNN MEIKTGGGMR INNNLLILDV DYPFDAQTKL RLKLGQGPLY INASHNLDIN
YNRGLYLFNA SNNTKKLEVS IKKSSGLNFD NTAIAINAGK GLEFDTNTSE SPDINPIKTK
IGSGIDYNEN GAMITKLGAG LSFDNSGAIT IGNKNDDKLT LWTTPDPSPN CRIHSDNDCK
FTLVLTKCGS QVLATVAALA VSGDLSSMTG TVASVSIFLR FDQNGVLMEN SSLKKHYWNF
RNGNSTNANP YTNAVGFMPN LLAYPKTQSQ TAKNNIVSQV YLHGDKTKPM ILTITLNGTS
ESTETSEVST YSMSFTWSWE SGKYTTETFA TNSYTFSYIA QE
