ID SPIKE_ADE12 Reviewed; 587 AA. AC P36711; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 129. DE RecName: Full=Fiber protein; DE Short=SPIKE; DE AltName: Full=Protein IV; GN ORFNames=L5; OS Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12). OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Polisuviricotina; OC Pharingeaviricetes; Rowavirales; Adenoviridae; Mastadenovirus; OC Mastadenovirus adami; Human mastadenovirus A. OX NCBI_TaxID=28282; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994; RA Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.; RT "Nucleotide sequence of human adenovirus type 12 DNA: comparative RT functional analysis."; RL J. Virol. 68:379-389(1994). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 403-587 IN COMPLEX WITH CXADR, AND RP MUTAGENESIS OF PRO-417; PRO-418; SER-421; GLU-425; LEU-426; GLY-550 AND RP ILE-551. RX PubMed=10567268; DOI=10.1126/science.286.5444.1579; RA Bewley M.C., Springer K., Zhang Y.-B., Freimuth P., Flanagan J.M.; RT "Structural analysis of the mechanism of adenovirus binding to its human RT cellular receptor, CAR."; RL Science 286:1579-1583(1999). 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}. 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; X73487; CAA51900.1; -; Genomic_DNA. DR PIR; S33951; S33951. DR RefSeq; NP_040933.1; NC_001460.1. DR PDB; 1KAC; X-ray; 2.60 A; A=403-587. DR PDB; 1NOB; X-ray; 2.60 A; A/B/C/D/E/F=403-587. DR PDB; 1P69; X-ray; 3.10 A; A=403-587. DR PDB; 1P6A; X-ray; 2.90 A; A=403-587. DR AlphaFoldDB; P36711; -. DR MDposit; P36711; -. DR SMR; P36711; -. DR MINT; P36711; -. DR GeneID; 1460847; -. DR KEGG; vg:1460847; -. DR EvolutionaryTrace; P36711; -. DR Proteomes; UP000004993; Segment. 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:symbiont entry into host cell; IEA:UniProtKB-KW. DR Gene3D; 6.20.10.20; -; 2. DR Gene3D; 2.60.90.10; Adenovirus pIV-related, attachment domain; 1. DR Gene3D; 2.10.25.20; reovirus attachment protein sigma1, domain 1; 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; 6. DR PRINTS; PR00307; ADENOVSFIBRE. DR SUPFAM; SSF51225; Fibre shaft of virus attachment proteins; 5. DR SUPFAM; SSF49835; Virus attachment protein globular domain; 1. DR PDBsum; 1KAC; -. DR PDBsum; 1NOB; -. DR PDBsum; 1P69; -. DR PDBsum; 1P6A; -. PE 1: Evidence at protein level; KW 3D-structure; Capsid protein; Host nucleus; Host-virus interaction; KW Late protein; Reference proteome; KW Viral attachment to host adhesion receptor; Viral attachment to host cell; KW Virion; Virus entry into host cell. FT CHAIN 1..587 FT /note="Fiber protein" FT /id="PRO_0000221795" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 417 FT /note="P->E: Loss of interaction with CXADR." FT /evidence="ECO:0000269|PubMed:10567268" FT MUTAGEN 418 FT /note="P->E: Loss of interaction with CXADR." FT /evidence="ECO:0000269|PubMed:10567268" FT MUTAGEN 421 FT /note="S->TIS: Loss of interaction with CXADR." FT /evidence="ECO:0000269|PubMed:10567268" FT MUTAGEN 425 FT /note="Missing: Loss of interaction with CXADR." FT /evidence="ECO:0000269|PubMed:10567268" FT MUTAGEN 426 FT /note="Missing: Loss of interaction with CXADR." FT /evidence="ECO:0000269|PubMed:10567268" FT MUTAGEN 550 FT /note="Missing: Loss of interaction with CXADR." FT /evidence="ECO:0000269|PubMed:10567268" FT MUTAGEN 551 FT /note="Missing: Loss of interaction with CXADR." FT /evidence="ECO:0000269|PubMed:10567268" FT STRAND 405..412 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 422..424 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 428..437 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 440..449 FT /evidence="ECO:0007829|PDB:1KAC" FT HELIX 452..455 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 463..470 FT /evidence="ECO:0007829|PDB:1KAC" FT TURN 472..474 FT /evidence="ECO:0007829|PDB:1NOB" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 491..494 FT /evidence="ECO:0007829|PDB:1KAC" FT HELIX 506..508 FT /evidence="ECO:0007829|PDB:1KAC" FT TURN 513..515 FT /evidence="ECO:0007829|PDB:1KAC" FT HELIX 518..520 FT /evidence="ECO:0007829|PDB:1KAC" FT HELIX 524..526 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 527..533 FT /evidence="ECO:0007829|PDB:1KAC" FT HELIX 534..536 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 540..551 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 557..564 FT /evidence="ECO:0007829|PDB:1KAC" FT HELIX 566..568 FT /evidence="ECO:0007829|PDB:1KAC" FT STRAND 579..585 FT /evidence="ECO:0007829|PDB:1KAC" SQ SEQUENCE 587 AA; 61699 MW; 6D285B5B61008A4C CRC64; MKRSRTQYAE ETEENDDFNP VYPFDPFDTS DVPFVTPPFT SSNGLQEKPP GVLALNYKDP IVTENGTLTL KLGDGIKLNA QGQLTASNNI NVLEPLTNTS QGLKLSWSAP LAVKASALTL NTRAPLTTTD ESLALITAPP ITVESSRLGL ATIAPLSLDG GGNLGLNLSA PLDVSNNNLH LTTETPLVVN SSGALSVATA DPISVRNNAL TLPTADPLMV SSDGLGISVT SPITVINGSL ALSTTAPLNS TGSTLSLSVA NPLTISQDTL TVSTGNGLQV SGSQLVTRIG DGLTFDNGVM KVNVAGGMRT SGGRIILDVN YPFDASNNLS LRRGLGLIYN QSTNWNLTTD ISTEKGLMFS GNQIALNAGQ GLTFNNGQLR VKLGAGLIFD SNNNIALGSS SNTPYDPLTL WTTPDPPPNC SLIQELDAKL TLCLTKNGSI VNGIVSLVGV KGNLLNIQST TTTVGVHLVF DEQGRLITST PTALVPQASW GYRQGQSVST NTVTNGLGFM PNVSAYPRPN ASEAKSQMVS LTYLQGDTSK PITMKVAFNG ITSLNGYSLT FMWSGLSNYI NQPFSTPSCS FSYITQE //