CAP3_ADES1
ID CAP3_ADES1 Reviewed; 615 AA.
AC A9CB89;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 02-JUN-2021, entry version 39.
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};
GN ORFNames=L1;
OS Snake adenovirus serotype 1 (SnAdV-1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Atadenovirus.
OX NCBI_TaxID=189830;
OH NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12237421; DOI=10.1099/0022-1317-83-10-2403;
RA Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT guttata) implies common origin with the members of the proposed new genus
RT Atadenovirus.";
RL J. Gen. Virol. 83:2403-2410(2002).
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:0000255|HAMAP-Rule:MF_04047}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04047}. Note=Surrounds the border of
CC each facet on the capsid exterior. Present in around 60 copies per
CC virion. {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}.
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; DQ106414; ABA47239.1; -; Genomic_DNA.
DR RefSeq; YP_001552250.1; NC_009989.1.
DR SMR; A9CB89; -.
DR GeneID; 10973892; -.
DR KEGG; vg:10973892; -.
DR Proteomes; UP000136605; 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; 1.
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..615
FT /note="Pre-hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000425926"
FT CHAIN 1..601
FT /note="Hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000439414"
FT PROPEP 602..615
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000439415"
FT REGION 1..92
FT /note="Peripentonal hexon-tethering domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 124..238
FT /note="Binding to hexon-linking protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 400..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 601..602
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 212
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 262
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 451
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
SQ SEQUENCE 615 AA; 67718 MW; A257FFE10961FE39 CRC64;
MDPGLKPSSS WTHKIVDSII ANRSQTAVQN FRRQPLANKL TALEDAIVQP RKDSTPDSIA
AILQELVSMG ALKPSEVGPM FSDLLIRVHK YNSTNVQSNL NVLLGDIRAA QSEAIRSTNV
GELSNQVILN DFLSRLPPVV PMGQHNYEAF KQSLRLMVNE APNVTLFKSG PDTMMQVNIR
GVNTVNLNSA FSNLQNLWGV VLDSDRVPGS ISSKLSSNTR VLLLFLAPFT NENTFTPDTF
LWQIMQLYRE TVAASIEAPL ETEREVAETV RDMGGDIDDV GRTMAYLLKN KEEVMANPRT
LSPRQLGVVR YVQESLMDRI DRNGEEPIDA LRNIVFSFAP SYFEANGSFI RKLLSYLEVA
LRNSPNYFRE IYSNKYWTPP PSFWTQNYGD FFVEREAEAE REALEEAGPR ESYSFLEDPS
SSPQSSKIQS LGTCGMTMLR PMSPSVPPTP SVRSAPPSVS YGGPSRSSLS VDSASNRNFG
ATLARAVLPS AAAAIGNAAG EALYPSLGQF LAPAASLAAT RFLSGNRGER IKRQRQRRRA
EIERRRIAEL TPPSPAPSLS SESSAPSLSS VRTSYTPLAG AKYWNPVDDP EGDRDVSGTG
LGNPFDYLRP RNGLK
