SPIKE_ADE15
ID SPIKE_ADE15 Reviewed; 367 AA.
AC P36847;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Human adenovirus D serotype 15 (HAdV-15) (Human adenovirus 15).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus D.
OX NCBI_TaxID=28276;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate HXB2956;
RX PubMed=7491756; DOI=10.1006/viro.1995.0004;
RA Eiz B., Adrian T., Pring-Akerblom P.;
RT "Immunological adenovirus variant strains of subgenus D: comparison of the
RT hexon and fiber sequences.";
RL Virology 213:313-320(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate HXB2956, and Isolate HXH10009;
RX PubMed=7831811; DOI=10.1016/s0042-6822(95)80073-5;
RA Pring-Akerblom P., Adrian T.;
RT "Characterization of adenovirus subgenus D fiber genes.";
RL Virology 206:564-571(1995).
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).
CC -!- FUNCTION: Forms spikes that protrude from each vertex of the
CC icosahedral capsid. Interacts with host receptor CXCAR to provide
CC virion initial attachment to target cell. Fiber proteins are shed
CC during virus entry, when virus is still at the cell surface (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Interacts with host receptor CXCAR. 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; X72935; CAA51440.1; -; Genomic_DNA.
DR EMBL; X72936; CAA51441.1; -; Genomic_DNA.
DR EMBL; X74669; CAA52733.1; -; Genomic_DNA.
DR PIR; S32664; S32664.
DR PDB; 6STW; X-ray; 1.37 A; A/B/C=178-367.
DR PDBsum; 6STW; -.
DR SMR; P36847; -.
DR PRIDE; P36847; -.
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; IPR008982; Adenovirus_pIV-like_att.
DR InterPro; IPR009013; Attachment_protein_shaft_sf.
DR Pfam; PF00541; Adeno_knob; 1.
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..367
FT /note="Fiber protein"
FT /id="PRO_0000221796"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:6STW"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6STW"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6STW"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:6STW"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6STW"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 335..344
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6STW"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:6STW"
SQ SEQUENCE 367 AA; 39983 MW; E7A4B930929C5E0C CRC64;
MSKRLRVEDD FNPVYPYGYA RNQNIPFLTP PFVSSDGFQN FPPGVLSLKL ADPIAIANGN
VSLKMGGGLT LQEGTGNLTV NTEPPLQLTN NRIGIALDAP FDVIGGKLTL LAGHGLSIIT
EETSPLPGLV NTLVVLTGKG LGTDTTDNGG SIRVRVGEGG GLSFNEAGDL VAFNKKEDMR
TLWTTPDPSP NCKIIEDKDS KLTLILTKCG SQILGSVSLL VVKGKFSNIN NTTNPNEADK
QITVKLLFDA NGVLKQGSTM DSSYWNYRSD NSNLSQPYKK AVGFMPSKTA YPKQTKPTNK
EISQAKNKIV SNVYLGGKID QPCVIIISFN EEADSDYSIV FYFKWYKTYE NVQFDSSSFN
FSYIAQE
