SPIK2_ADE41
ID SPIK2_ADE41 Reviewed; 387 AA.
AC P16883;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 02-JUN-2021, entry version 97.
DE RecName: Full=Fiber protein 2;
OS Human adenovirus F serotype 41 (HAdV-41) (Human adenovirus 41).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=10524;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tak;
RX PubMed=2336370; DOI=10.1093/nar/18.7.1901;
RA Pieniazek N.J., Slemenda S.B., Pieniazek D., Velarde J. Jr., Luftig R.B.;
RT "Human enteric adenovirus type 41 (Tak) contains a second fiber protein
RT gene.";
RL Nucleic Acids Res. 18:1901-1901(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-387.
RC STRAIN=FB585;
RX PubMed=2219717; DOI=10.1016/0042-6822(90)90283-w;
RA Kidd A.H., Erasmus M.J., Tiemessen C.T.;
RT "Fiber sequence heterogeneity in subgroup F adenoviruses.";
RL Virology 179:139-150(1990).
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; X17016; CAA34882.1; -; Genomic_DNA.
DR EMBL; M60327; AAA42505.1; -; Genomic_DNA.
DR PIR; S09217; ERADN1.
DR PDB; 2BZU; X-ray; 1.50 A; A=215-387.
DR PDB; 2BZV; X-ray; 1.15 A; A=215-387.
DR PDBsum; 2BZU; -.
DR PDBsum; 2BZV; -.
DR SMR; P16883; -.
DR EvolutionaryTrace; P16883; -.
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; 4.
DR PRINTS; PR00307; ADENOVSFIBRE.
DR SUPFAM; SSF49835; SSF49835; 1.
DR SUPFAM; SSF51225; SSF51225; 2.
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..387
FT /note="Fiber protein 2"
FT /id="PRO_0000221802"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:2BZV"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2BZV"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:2BZV"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2BZV"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2BZV"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:2BZU"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:2BZU"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 356..367
FT /evidence="ECO:0007829|PDB:2BZV"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:2BZV"
SQ SEQUENCE 387 AA; 41397 MW; 8652E785276573C7 CRC64;
MKRTRIEDDF NPVYPYDTFS TPSIPYVAPP FVSSDGLQEK PPGVLALKYT DPITTNAKHE
LTLKLGSNIT LENGLLSATV PTVSPPLTNS NNSLGLATSA PIAVSANSLT LATAAPLTVS
NNQLSINAGR GLVITNNALT VNPTGALGFN NTGALQLNAA GGMRVDGANL ILHVAYPFEA
INQLTLRLEN GLEVTSGGKL NVKLGSGLQF DSNGRIAISN SNRTRSVPSL TTIWSISPTP
NCSIYETQDA NLFLCLTKNG AHVLGTITIK GLKGALREMH DNALSLKLPF DNQGNLLNCA
LESSTWRYQE TNAVASNALT FMPNSTVYPR NKTAHPGNML IQISPNITFS VVYNEINSGY
AFTFKWSAEP GKPFHPPTAV FCYITEQ
