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 27-MAR-2024, entry version 99. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8QJX; EM; 3.30 A; A/B/C=1-325. DR PDB; 8QJY; EM; 3.50 A; A/B/C=1-325. DR PDB; 8QK3; EM; 3.20 A; A/B/C=1-325. DR PDBsum; 2O39; -. DR PDBsum; 3EXV; -. DR PDBsum; 8QJX; -. DR PDBsum; 8QJY; -. DR PDBsum; 8QK3; -. DR EMDB; EMD-18453; -. DR EMDB; EMD-18454; -. DR EMDB; EMD-18455; -. 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 CDD; cd07964; RBP-H; 1. DR Gene3D; 2.60.90.10; Adenovirus pIV-related, attachment domain; 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; SSF51225; Fibre shaft of virus attachment proteins; 1. DR SUPFAM; SSF49835; Virus attachment protein globular domain; 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 //