SPIKE_ADES1
ID SPIKE_ADES1 Reviewed; 415 AA.
AC A9CB96;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 02-JUN-2021, entry version 48.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Snake adenovirus serotype 1 (SnAdV-1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Atadenovirus.
OX NCBI_TaxID=189830;
OH NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12237421; DOI=10.1099/0022-1317-83-10-2403;
RA Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT guttata) implies common origin with the members of the proposed new genus
RT Atadenovirus.";
RL J. Gen. Virol. 83:2403-2410(2002).
RN [2]
RP SEQUENCE REVISION, AND SUBCELLULAR LOCATION.
RX PubMed=24316834; DOI=10.1107/s1744309113029308;
RA Singh A.K., Menendez-Conejero R., San Martin C., van Raaij M.J.;
RT "Crystallization of the C-terminal domain of the fibre protein from snake
RT adenovirus 1, an atadenovirus.";
RL Acta Crystallogr. F 69:1374-1379(2013).
CC -!- FUNCTION: Forms spikes that protrude from each vertex of the
CC icosahedral capsid. Interacts with host receptor 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Interacts (via N-terminal tail region) with
CC pentons (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24316834}. Host
CC nucleus {ECO:0000250}. Note=Anchored to the pentons, protrudes from the
CC virion surface. {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; DQ106414; ABA47246.1; -; Genomic_DNA.
DR RefSeq; YP_001552263.1; NC_009989.1.
DR PDB; 4D0U; X-ray; 1.60 A; A/B/C/D=234-339.
DR PDB; 4D0V; X-ray; 1.70 A; A/B/C/D=234-339.
DR PDB; 4D1F; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=234-339.
DR PDB; 4D1G; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=234-339.
DR PDB; 4UMI; X-ray; 1.33 A; A=171-339.
DR PDBsum; 4D0U; -.
DR PDBsum; 4D0V; -.
DR PDBsum; 4D1F; -.
DR PDBsum; 4D1G; -.
DR PDBsum; 4UMI; -.
DR SMR; A9CB96; -.
DR GeneID; 10973877; -.
DR KEGG; vg:10973877; -.
DR Proteomes; UP000136605; 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:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000931; Adeno_fibre.
DR InterPro; IPR009013; Attachment_protein_shaft_sf.
DR PRINTS; PR00307; ADENOVSFIBRE.
DR SUPFAM; SSF51225; SSF51225; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host nucleus; Host-virus interaction;
KW Late protein; Reference proteome; Viral attachment to host cell; Virion;
KW Virus entry into host cell.
FT CHAIN 1..415
FT /note="Fiber protein"
FT /id="PRO_0000425906"
FT CONFLICT 340..415
FT /note="STSLKVISIYFMDLFFPVPFIDRASHPAPRRSNNSRQLFHSKQRLFLKVKDF
FT KKRSWYSSLFTLINLNIQECPELS -> FYLTEK (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 238..249
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 268..279
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4UMI"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:4UMI"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:4UMI"
SQ SEQUENCE 415 AA; 43763 MW; CA41554158D50804 CRC64;
MKKIKRSAAD PDPVYPFGDE VPIPLPPFLV PGGGLTTDGL SLAVQTVDPL NVTLGGVGLK
IGDGLSVVDG KLTSEAKIVA DPPLQQSGDT LSLSTDSSMM VLPSGQLTIN NLPSISVTSS
GVGLVSPNAP LQLMSNGALQ LSVGGGLTVG AQGSLQISTG VGVNVNAAGV LESYPLPPLV
WDYSSKSLTL DIGPGLTVVN GKLQVIGATF SNQMSRMAPA PRADLQSNSI EPLPSPPSKT
SLDIAEELQN DKGVSFAFQA REEELGAFTK RTLFAYSGDG LTGPFKAPAS AELSSFLTAH
PKGRWLIAFP LGTGIVSVDE GILTLEISRS LPEVGSGSSS TSLKVISIYF MDLFFPVPFI
DRASHPAPRR SNNSRQLFHS KQRLFLKVKD FKKRSWYSSL FTLINLNIQE CPELS
