CAP3_ADEG1
ID CAP3_ADEG1 Reviewed; 575 AA.
AC Q64754;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 66.
DE RecName: Full=Pre-hexon-linking protein IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE AltName: Full=Capsid vertex-specific component IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE Short=CVSC {ECO:0000255|HAMAP-Rule:MF_04047};
DE AltName: Full=Protein IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE AltName: Full=pIIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE Contains:
DE RecName: Full=Hexon-linking protein IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
OS Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS adenovirus gal1 (strain Phelps)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX NCBI_TaxID=10553;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT "The complete DNA sequence and genomic organization of the avian adenovirus
RT CELO.";
RL J. Virol. 70:2939-2949(1996).
CC -!- FUNCTION: Structural component of the virion that acts as a cement
CC protein on the capsid exterior which mediates the interactions between
CC the hexons, including the peripentonal hexons, and reaches all the way
CC to the penton vertices. Two hexon linking proteins IIIa, one from each
CC facet, stabilize the unique edge interface between a pair of facets. As
CC the virus enters the host cell, hexon linking proteins IIIa are shed
CC concomitant with virion acidification in the endosome. During virus
CC assembly, seems to play a role in the serotype specificity of the
CC packaging of viral DNA via its interaction with packaging protein 3.
CC {ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- SUBUNIT: Interacts with hexon proteins; this interaction tethers the
CC peripentonal hexons to hexons situated in the facet. Interacts with the
CC penton protein (via N-terminus). Interacts with packaging protein 3;
CC this interaction is required to promote correct genome packaging.
CC {ECO:0000250|UniProtKB:P12537, ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P12537,
CC ECO:0000255|HAMAP-Rule:MF_04047}. Host nucleus
CC {ECO:0000250|UniProtKB:P12537, ECO:0000255|HAMAP-Rule:MF_04047}.
CC Note=Surrounds the border of each facet on the capsid exterior. Present
CC in around 60 copies per virion. {ECO:0000250|UniProtKB:P12537,
CC ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- PTM: Cleaved near the C-terminus by the viral protease during virion
CC maturation to form the mature protein. {ECO:0000250|UniProtKB:P03279,
CC ECO:0000255|HAMAP-Rule:MF_04047}.
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. {ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon-linking protein IIIa
CC family. {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000305}.
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DR EMBL; U46933; AAC54907.1; -; Genomic_DNA.
DR RefSeq; NP_043881.1; NC_001720.1.
DR SMR; Q64754; -.
DR GeneID; 1476560; -.
DR KEGG; vg:1476560; -.
DR Proteomes; UP000001594; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098021; C:viral capsid, decoration; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1500; -; 1.
DR HAMAP; MF_04047; ADV_CAP3; 1.
DR InterPro; IPR003479; Hex_IIIa.
DR InterPro; IPR043053; Hex_IIIa_N.
DR Pfam; PF02455; Hex_IIIa; 2.
PE 3: Inferred from homology;
KW Capsid decoration protein; Capsid protein; Host nucleus; Late protein;
KW Phosphoprotein; Reference proteome; Viral genome packaging;
KW Viral release from host cell; Virion.
FT CHAIN 1..575
FT /note="Pre-hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000221839"
FT CHAIN 1..514
FT /note="Hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000439410"
FT PROPEP 515..575
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000439411"
FT REGION 1..95
FT /note="Peripentonal hexon-tethering domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 129..243
FT /note="Binding to hexon-linking protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 525..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 514..515
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 497
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
SQ SEQUENCE 575 AA; 63775 MW; E1A5924388B2DB95 CRC64;
MTSSDTFLAL APYGRQEVAD ALSSLPDGKD ARSLRHAPYA NRLIKLQSAM VPPKVDGTSE
RVAEIVKGLA EQGAIYPDQM GAIHSDLLNR AYTWNSMGVQ ESIQALVNDV IHGQNRTLQD
ELARTKEIAN ASLLTQFFDS LYKTVDRGQR NFEGFKKLLR LFVNNVPNAE VYGSSGSFSV
QINLGGSSQN INLTNAFENL KPIWGARWDA VNNPRIGALL TPNTRALLFF VSSFYDYGAM
EPGSYLDNIM RLYKEAIRAD VDAEGDAIME LGEAGANLNL RFNDYKDTLN YLLQNREVVP
DTAPLELSAE QEMLLKYLMR QLRQALKDGV PADISISTMT QYLDPRLYQT NKVFVEKLQN
YLLAAQARNP VYYRLLVLDP NWRPPAGLYT GNYVIPDRYD FEDVQSELEY AGPSRDEYFD
DSLFAPGPQR RLNSAEEAQL ERDIESLTGH IDEELGVQSQ AGWLADHRLP VAFDGALSLT
ERNAYNTPLP PDSHMRSRSS SVASDLGLLN LSGTGGPGFF ASLRPSIGSR QPTGTAVGLR
PTTPYSGSGC MRGTGLARKV LNPAASRRGR KLRFY
