SPIKE_ADE03
ID SPIKE_ADE03 Reviewed; 319 AA.
AC P04501;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Human adenovirus B serotype 3 (HAdV-3) (Human adenovirus 3).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=45659;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2982041; DOI=10.1128/jvi.53.2.672-678.1985;
RA Signaes C., Akusjaervi G., Pettersson U.;
RT "Adenovirus 3 fiber polypeptide gene: implications for the structure of the
RT fiber protein.";
RL J. Virol. 53:672-678(1985).
RN [2]
RP INTERACTION WITH HUMAN CD46.
RX PubMed=15078926; DOI=10.1128/jvi.78.9.4454-4462.2004;
RA Sirena D., Lilienfeld B., Eisenhut M., Kaelin S., Boucke K., Beerli R.R.,
RA Vogt L., Ruedl C., Bachmann M.F., Greber U.F., Hemmi S.;
RT "The human membrane cofactor CD46 is a receptor for species B adenovirus
RT serotype 3.";
RL J. Virol. 78:4454-4462(2004).
RN [3]
RP REVIEW.
RX PubMed=16160140; DOI=10.1128/jvi.79.19.12125-12131.2005;
RA Zhang Y., Bergelson J.M.;
RT "Adenovirus receptors.";
RL J. Virol. 79:12125-12131(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 126-319.
RX PubMed=11437664; DOI=10.1006/viro.2001.0967;
RA Durmort C., Stehlin C., Schoehn G., Mitraki A., Drouet E., Cusack S.,
RA Burmeister W.P.;
RT "Structure of the fiber head of Ad3, a non-CAR-binding serotype of
RT adenovirus.";
RL Virology 285:302-312(2001).
CC -!- FUNCTION: Forms spikes that protrude from each vertex of the
CC icosahedral capsid. Interacts with host receptor CD46 to provide virion
CC initial attachment to target cell. Fiber proteins are shed during virus
CC entry, when virus is still at the cell surface. Heparan sulfate might
CC also play a role in virus binding.
CC -!- SUBUNIT: Homotrimer. Interacts with host receptor CD46. Interacts (via
CC N-terminal tail region) with pentons (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host nucleus {ECO:0000250}.
CC Note=Anchored to the pentons, protrudes from the virion surface.
CC {ECO:0000250}.
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. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adenoviridae fiber family. {ECO:0000305}.
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DR EMBL; X01998; CAA26029.1; -; Genomic_DNA.
DR PIR; A03846; ERADF3.
DR PDB; 1H7Z; X-ray; 1.60 A; A/B/C=126-319.
DR PDB; 4LIY; X-ray; 2.10 A; A/B/C=123-319.
DR PDB; 4WYJ; X-ray; 2.65 A; A/B/C=127-319.
DR PDB; 6F6O; X-ray; 1.49 A; A=124-319.
DR PDB; 6QNT; EM; 3.50 A; A/B/C=130-318.
DR PDB; 6QNU; EM; 3.80 A; A/B/C=130-318.
DR PDB; 6SIT; X-ray; 4.50 A; A=129-319.
DR PDBsum; 1H7Z; -.
DR PDBsum; 4LIY; -.
DR PDBsum; 4WYJ; -.
DR PDBsum; 6F6O; -.
DR PDBsum; 6QNT; -.
DR PDBsum; 6QNU; -.
DR PDBsum; 6SIT; -.
DR SASBDB; P04501; -.
DR SMR; P04501; -.
DR EvolutionaryTrace; P04501; -.
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; 2.
DR PRINTS; PR00307; ADENOVSFIBRE.
DR SUPFAM; SSF49835; SSF49835; 1.
DR SUPFAM; SSF51225; SSF51225; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host nucleus; Host-virus interaction;
KW Late protein; Repeat; Viral attachment to host adhesion receptor;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..319
FT /note="Fiber protein"
FT /id="PRO_0000221787"
FT REPEAT 44..73
FT /note="Shaft 1"
FT /evidence="ECO:0000255"
FT REPEAT 82..103
FT /note="Shaft 2"
FT /evidence="ECO:0000255"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:6F6O"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6QNT"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1H7Z"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6F6O"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:6F6O"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:6QNT"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:6F6O"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:6F6O"
SQ SEQUENCE 319 AA; 34815 MW; 7B9C9A26FE6C70D2 CRC64;
MAKRARLSTS FNPVYPYEDE SSSQHPFINP GFISPDGFTQ SPNGVLSLKC VNPLTTASGS
LQLKVGSGLT VDTTDGSLEE NIKVNTPLTK SNHSINLPIG NGLQIEQNKL CSKLGNGLTF
DSSNSIALKN NTLWTGPKPE ANCIIEYGKQ NPDSKLTLIL VKNGGIVNGY VTLMGASDYV
NTLFKNKNVS INVELYFDAT GHILPDSSSL KTDLELKYKQ TADFSARGFM PSTTAYPFVL
PNAGTHNENY IFGQCYYKAS DGALFPLEVT VMLNKRLPDS RTSYVMTFLW SLNAGLAPET
TQATLITSPF TFSYIREDD
