SPIKE_ADE07
ID SPIKE_ADE07 Reviewed; 343 AA.
AC P15141;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Human adenovirus B serotype 7 (HAdV-7) (Human adenovirus 7).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=10519;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Gomen;
RX PubMed=2849239;
RA Hong J.S., Mullis K.G., Engler J.A.;
RT "Characterization of the early region 3 and fiber genes of Ad7.";
RL Virology 167:545-553(1988).
RN [2]
RP FUNCTION.
RX PubMed=11152512; DOI=10.1128/jvi.75.3.1387-1400.2001;
RA Miyazawa N., Crystal R.G., Leopold P.L.;
RT "Adenovirus serotype 7 retention in a late endosomal compartment prior to
RT cytosol escape is modulated by fiber protein.";
RL J. Virol. 75:1387-1400(2001).
RN [3]
RP INTERACTION WITH HUMAN CD46.
RX PubMed=22130529; DOI=10.1128/jvi.06181-11;
RA Trinh H.V., Lesage G., Chennamparampil V., Vollenweider B.,
RA Burckhardt C.J., Schauer S., Havenga M., Greber U.F., Hemmi S.;
RT "Avidity binding of human adenovirus serotypes 3 and 7 to the membrane
RT cofactor CD46 triggers infection.";
RL J. Virol. 86:1623-1637(2012).
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.
CC {ECO:0000269|PubMed:11152512}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA53254.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M23696; AAA53254.1; ALT_INIT; Genomic_DNA.
DR PIR; F31830; ERADF7.
DR PDB; 3EXW; X-ray; 1.75 A; A/B/C=135-343.
DR PDB; 7AGF; EM; 3.10 A; A/B/C=135-343.
DR PDB; 7AGG; EM; 3.30 A; A/B/C=135-343.
DR PDBsum; 3EXW; -.
DR PDBsum; 7AGF; -.
DR PDBsum; 7AGG; -.
DR SMR; P15141; -.
DR EvolutionaryTrace; P15141; -.
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; Viral attachment to host adhesion receptor;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..343
FT /note="Fiber protein"
FT /id="PRO_0000221790"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:3EXW"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:3EXW"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 207..217
FT /evidence="ECO:0007829|PDB:3EXW"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3EXW"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:3EXW"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:3EXW"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 286..298
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:7AGF"
FT STRAND 305..315
FT /evidence="ECO:0007829|PDB:3EXW"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:3EXW"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:3EXW"
SQ SEQUENCE 343 AA; 37287 MW; 8AC724C472607CD2 CRC64;
MSNFNSSPVP TIFMSFFQMT KRVRLSDSFN PVYPYEDEST SQHPFINPGF ISPNGFTQSP
DGVLTLKCLT PLTTTGGSLQ LKVGGGLTID DTDGFLKENI SAATPLVKTG HSIGLSLGPG
LGTNENKLCA KLGEGLTFNS NNICIDDNIN TLWTGVNPTT ANCQIMASSE SNDCKLILTL
VKTGGLVTAF VYVIGVSNDF NMLTTHKNIN FTAELFFDST GNLLTSLSSL KTPLNHKSGQ
NMATGALTNA KGFMPSTTAY PFNVNSREKE NYIYGTCYYT ASDHTAFPID ISVMLNQRAL
NNETSYCIRV TWSWNTGVAP EVQTSATTLV TSPFTFYYIR EDD