SPIKE_ADE05
ID SPIKE_ADE05 Reviewed; 581 AA.
AC P11818;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 29-SEP-2021, entry version 118.
DE RecName: Full=Fiber protein;
DE Short=SPIKE;
DE AltName: Full=Protein IV;
GN ORFNames=L5;
OS Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3686830; DOI=10.1016/0042-6822(87)90150-4;
RA Chroboczek J., Jacrot B.;
RT "The sequence of adenovirus fiber: similarities and differences between
RT serotypes 2 and 5.";
RL Virology 161:549-554(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23142869; DOI=10.1038/nmeth.2227;
RA Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT "De novo derivation of proteomes from transcriptomes for transcript and
RT protein identification.";
RL Nat. Methods 9:1207-1211(2012).
RN [4]
RP GLYCOSYLATION.
RX PubMed=2120471; DOI=10.1128/jvi.64.11.5317-5323.1990;
RA Mullis K.G., Haltiwanger R.S., Hart G.W., Marchase R.B., Engler J.A.;
RT "Relative accessibility of N-acetylglucosamine in trimers of the adenovirus
RT types 2 and 5 fiber proteins.";
RL J. Virol. 64:5317-5323(1990).
RN [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 386-581.
RX PubMed=7704534; DOI=10.1016/s0969-2126(94)00126-x;
RA Xia D., Henry L.J., Gerard R.D., Deisenhofer J.;
RT "Crystal structure of the receptor-binding domain of adenovirus type 5
RT fiber protein at 1.7-A resolution.";
RL Structure 2:1259-1270(1994).
CC -!- FUNCTION: Forms spikes that protrude from each vertex of the
CC icosahedral capsid. Interacts with host coxsackievirus and adenovirus
CC receptor CXADR located at the cell tight junctions to provide virion
CC initial attachment to target cell. The fiber protein binds to CXADR
CC with a higher affinity than CXADR binds to itself, thereby blocking the
CC cell-cell adhesion function of CXADR dimers and leading to local
CC disruption of the tight junction. Fiber protein present on neo-
CC synthesized particles may thus disrupt the junctional integrity in
CC order to facilitate further neighboring cells infection. Fiber proteins
CC are shed during virus entry, when virus is still at the cell surface.
CC Fiber shedding is dependent on viral CXADR drifting motion and
CC subsequent binding to immobile integrins. Heparan sulfate might also
CC play a role in virus binding (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; arranged in a triple beta-spiral. Interacts with
CC host receptor CXADR. 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 Present in 36 copies per virion (By similarity). {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 -!- PTM: O-glycosylated; glycans contain N-acetylglucosamine and may play a
CC role in fiber assembly and stabilization. {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; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M18369; AAA42504.1; -; Genomic_DNA.
DR PIR; A27404; ERADF5.
DR RefSeq; AP_000226.1; AC_000008.1.
DR PDB; 1KNB; X-ray; 1.70 A; A=386-581.
DR PDB; 4ATZ; X-ray; 1.95 A; A/B/C=387-581.
DR PDBsum; 1KNB; -.
DR PDBsum; 4ATZ; -.
DR SMR; P11818; -.
DR GlyConnect; 156; 1 O-Linked glycan.
DR EvolutionaryTrace; P11818; -.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098022; C:viral capsid, fiber; IMP:CACAO.
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; 5.
DR PRINTS; PR00307; ADENOVSFIBRE.
DR SUPFAM; SSF49835; SSF49835; 1.
DR SUPFAM; SSF51225; SSF51225; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host nucleus; Host-virus interaction;
KW Late protein; Repeat; Viral attachment to host adhesion receptor;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..581
FT /note="Fiber protein"
FT /id="PRO_0000221789"
FT REPEAT 45..59
FT /note="Shaft 1"
FT REPEAT 60..75
FT /note="Shaft 2"
FT REPEAT 76..95
FT /note="Shaft 3"
FT REPEAT 96..109
FT /note="Shaft 4"
FT REPEAT 110..124
FT /note="Shaft 5"
FT REPEAT 125..139
FT /note="Shaft 6"
FT REPEAT 140..154
FT /note="Shaft 7"
FT REPEAT 155..170
FT /note="Shaft 8"
FT REPEAT 171..185
FT /note="Shaft 9"
FT REPEAT 186..200
FT /note="Shaft 10"
FT REPEAT 201..217
FT /note="Shaft 11"
FT REPEAT 218..232
FT /note="Shaft 12"
FT REPEAT 233..248
FT /note="Shaft 13"
FT REPEAT 249..265
FT /note="Shaft 14"
FT REPEAT 266..279
FT /note="Shaft 15"
FT REPEAT 280..296
FT /note="Shaft 16"
FT REPEAT 297..316
FT /note="Shaft 17"
FT REPEAT 317..333
FT /note="Shaft 18"
FT REPEAT 334..354
FT /note="Shaft 19"
FT REPEAT 355..370
FT /note="Shaft 20"
FT REPEAT 371..386
FT /note="Shaft 21"
FT REPEAT 387..392
FT /note="Shaft 22"
FT REGION 1..44
FT /note="Tail (penton base attachment)"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..392
FT /note="Shaft region"
FT /evidence="ECO:0000250"
FT REGION 393..398
FT /note="Spacer"
FT /evidence="ECO:0000250"
FT REGION 399..581
FT /note="Head"
FT /evidence="ECO:0000250"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:4ATZ"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 419..428
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 431..440
FT /evidence="ECO:0007829|PDB:1KNB"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:1KNB"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:4ATZ"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:1KNB"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:4ATZ"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:1KNB"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:1KNB"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:1KNB"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 515..522
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 528..537
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 549..557
FT /evidence="ECO:0007829|PDB:1KNB"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:1KNB"
SQ SEQUENCE 581 AA; 61585 MW; C3FDDFCF9E5E599F CRC64;
MKRARPSEDT FNPVYPYDTE TGPPTVPFLT PPFVSPNGFQ ESPPGVLSLR LSEPLVTSNG
MLALKMGNGL SLDEAGNLTS QNVTTVSPPL KKTKSNINLE ISAPLTVTSE ALTVAAAAPL
MVAGNTLTMQ SQAPLTVHDS KLSIATQGPL TVSEGKLALQ TSGPLTTTDS STLTITASPP
LTTATGSLGI DLKEPIYTQN GKLGLKYGAP LHVTDDLNTL TVATGPGVTI NNTSLQTKVT
GALGFDSQGN MQLNVAGGLR IDSQNRRLIL DVSYPFDAQN QLNLRLGQGP LFINSAHNLD
INYNKGLYLF TASNNSKKLE VNLSTAKGLM FDATAIAINA GDGLEFGSPN APNTNPLKTK
IGHGLEFDSN KAMVPKLGTG LSFDSTGAIT VGNKNNDKLT LWTTPAPSPN CRLNAEKDAK
LTLVLTKCGS QILATVSVLA VKGSLAPISG TVQSAHLIIR FDENGVLLNN SFLDPEYWNF
RNGDLTEGTA YTNAVGFMPN LSAYPKSHGK TAKSNIVSQV YLNGDKTKPV TLTITLNGTQ
ETGDTTPSAY SMSFSWDWSG HNYINEIFAT SSYTFSYIAQ E