SPIKE_ADECT
ID SPIKE_ADECT Reviewed; 542 AA.
AC Q65914;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 02-JUN-2021, entry version 90.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Canine adenovirus serotype 2 (strain Toronto A 26-61) (CAdV-2) (Canine
OS adenovirus 2 (strain Toronto A 26-61)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX NCBI_TaxID=69152;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7622065; DOI=10.1016/0378-1119(95)00110-r;
RA Rasmussen U., Schlesinger Y., Pavirani A., Mehtali M.;
RT "Sequence analysis of the canine adenovirus 2 fiber-encoding gene.";
RL Gene 159:279-280(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Campbell J.B., Zhao Y.;
RT "Complete DNA sequence and genomic organization of canine adenovirus type
RT 2.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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: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; Z37498; CAA85723.1; -; Genomic_DNA.
DR EMBL; U77082; AAB38734.1; -; Genomic_DNA.
DR PIR; S49219; S49219.
DR RefSeq; AP_000632.1; AC_000020.1.
DR PDB; 2J1K; X-ray; 2.30 A; C/D/E/F/H/I/L/M/N/Q/R/S=358-542.
DR PDB; 2J2J; X-ray; 1.50 A; A/B/C/D/E/F=358-542.
DR PDB; 2W9L; X-ray; 2.91 A; C/D/E/F/H/I/L/M/N/Q/R/S=358-542.
DR PDB; 2WBV; X-ray; 1.90 A; A/B/C/D/E/F=358-542.
DR PDBsum; 2J1K; -.
DR PDBsum; 2J2J; -.
DR PDBsum; 2W9L; -.
DR PDBsum; 2WBV; -.
DR SMR; Q65914; -.
DR UniLectin; Q65914; -.
DR EvolutionaryTrace; Q65914; -.
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; IPR000939; Adenobir_fibre_prot_rpt/shaft.
DR InterPro; IPR008982; Adenovirus_pIV-like_att.
DR InterPro; IPR009013; Attachment_protein_shaft_sf.
DR Pfam; PF00608; Adeno_shaft; 7.
DR PRINTS; PR00307; ADENOVSFIBRE.
DR SUPFAM; SSF49835; SSF49835; 1.
DR SUPFAM; SSF51225; SSF51225; 3.
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..542
FT /note="Fiber protein"
FT /id="PRO_0000221807"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 380..391
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 393..404
FT /evidence="ECO:0007829|PDB:2J2J"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 418..424
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:2J1K"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:2J2J"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 474..483
FT /evidence="ECO:0007829|PDB:2J2J"
FT TURN 484..489
FT /evidence="ECO:0007829|PDB:2J2J"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 494..502
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 509..517
FT /evidence="ECO:0007829|PDB:2J2J"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:2J2J"
FT STRAND 533..539
FT /evidence="ECO:0007829|PDB:2J2J"
SQ SEQUENCE 542 AA; 57004 MW; B71131829ADA7400 CRC64;
MKRTRRALPA NYDPVYPYDA PGSSTQPPFF NNKQGLTESP PGTLAVNVSP PLTFSTLGAI
KLSTGPGLTL NEGKLQASLG PGLITNTEGQ ITVENVNKVL SFTSPLHKNE NTVSLALGDG
LEDENGTLKV TFPTPPPPLQ FSPPLTKTGG TVSLPLQDSM QVTNGKLGVK PTTYAPPLKK
TDQQVSLQVG SGLTVINEQL QAVQPPATTY NEPLSKTDNS VSLQVGAGLA VQSGALVATP
PPPLTFTSPL EKNENTVSLQ VGAGLSVQNN ALVATPPPPL TFAYPLVKND NHVALSAGSG
LRISGGSLTV ATGPGLSHQN GTIGAVVGAG LKFENNAILA KLGNGLTIRD GAIEATQPPA
APITLWTGPG PSINGFINDT PVIRCFICLT RDSNLVTVNA SFVGEGGYRI VSPTQSQFSL
IMEFDQFGQL MSTGNINSTT TWGEKPWGNN TVQPRPSHTW KLCMPNREVY STPAATISRC
GLDSIAVDGA PSRSIDCMLI INKPKGVATY TLTFRFLNFN RLSGGTLFKT DVLTFTYVGE
NQ
