SPIKE_ADE12
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 23-FEB-2022, entry version 117.
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; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; 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}.
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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 PDBsum; 1KAC; -.
DR PDBsum; 1NOB; -.
DR PDBsum; 1P69; -.
DR PDBsum; 1P6A; -.
DR SMR; P36711; -.
DR MINT; P36711; -.
DR GeneID; 1460847; -.
DR KEGG; vg:1460847; -.
DR EvolutionaryTrace; P36711; -.
DR Proteomes; UP000004993; Genome.
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; 6.
DR PRINTS; PR00307; ADENOVSFIBRE.
DR SUPFAM; SSF49835; SSF49835; 1.
DR SUPFAM; SSF51225; SSF51225; 5.
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..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
