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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}.
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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
 
 
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