SPIKE_ADE1P
ID SPIKE_ADE1P Reviewed; 325 AA.
AC P35774;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 96.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Human adenovirus B serotype 11 (strain Slobiski) (HAdV-11) (Human
OS adenovirus 11P (strain Slobiski)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=343462;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8503168; DOI=10.1006/viro.1993.1284;
RA Mei Y.-F., Wadell G.;
RT "Hemagglutination properties and nucleotide sequence analysis of the fiber
RT gene of adenovirus genome types 11p and 11a.";
RL Virology 194:453-462(1993).
RN [2]
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).
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 -!- 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; AF532578; AAA42490.1; -; Genomic_DNA.
DR PIR; D37476; D37476.
DR PDB; 2O39; X-ray; 2.85 A; A/B=129-325.
DR PDB; 3EXV; X-ray; 1.45 A; A=117-325.
DR PDBsum; 2O39; -.
DR PDBsum; 3EXV; -.
DR SMR; P35774; -.
DR EvolutionaryTrace; P35774; -.
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..325
FT /note="Fiber protein"
FT /id="PRO_0000221794"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:3EXV"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3EXV"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:3EXV"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3EXV"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3EXV"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:3EXV"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 268..279
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2O39"
FT STRAND 288..297
FT /evidence="ECO:0007829|PDB:3EXV"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:3EXV"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:3EXV"
SQ SEQUENCE 325 AA; 35538 MW; 3B3ACCA4CBDB3EFD CRC64;
MTKRVRLSDS FNPVYPYEDE STSQHPFINP GFISPNGFTQ SPNGVLTLKC LTPLTTTGGS
LQLKVGGGLT VDDTNGFLKE NISATTPLVK TGHSIGLPLG AGLGTNENKL CIKLGQGLTF
NSNNICIDDN INTLWTGVNP TEANCQIMNS SESNDCKLIL TLVKTGALVT AFVYVIGVSN
NFNMLTTHRN INFTAELFFD STGNLLTRLS SLKTPLNHKS GQNMATGAIT NAKGFMPSTT
AYPFNDNSRE KENYIYGTCY YTASDRTAFP IDISVMLNRR AINDETSYCI RITWSWNTGD
APEVQTSATT LVTSPFTFYY IREDD
