CAP3_ADE05
ID CAP3_ADE05 Reviewed; 585 AA.
AC P12537;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 25-MAY-2022, entry version 79.
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 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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 469-585.
RX PubMed=3224820; DOI=10.1016/0378-1119(88)90389-7;
RA Neumann R., Chroboczek J., Jacrot B.;
RT "Determination of the nucleotide sequence for the penton-base gene of human
RT adenovirus type 5.";
RL Gene 69:153-157(1988).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=18786542; DOI=10.1016/j.jmb.2008.08.054;
RA San Martin C., Glasgow J.N., Borovjagin A., Beatty M.S., Kashentseva E.A.,
RA Curiel D.T., Marabini R., Dmitriev I.P.;
RT "Localization of the N-terminus of minor coat protein IIIa in the
RT adenovirus capsid.";
RL J. Mol. Biol. 383:923-934(2008).
RN [5]
RP FUNCTION, AND INTERACTION WITH PACKAGING PROTEIN 3.
RC STRAIN=Human adenovirus D serotype 17;
RX PubMed=21632753; DOI=10.1128/jvi.00467-11;
RA Ma H.C., Hearing P.;
RT "Adenovirus structural protein IIIa is involved in the serotype specificity
RT of viral DNA packaging.";
RL J. Virol. 85:7849-7855(2011).
RN [6]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE,
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE HEXON PROTEIN, AND
RP INTERACTION WITH THE PENTON PROTEIN.
RX PubMed=20798312; DOI=10.1126/science.1187433;
RA Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.;
RT "Atomic structure of human adenovirus by cryo-EM reveals interactions among
RT protein networks.";
RL Science 329:1038-1043(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), INTERACTION WITH THE HEXON PROTEIN,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25071205; DOI=10.1073/pnas.1408462111;
RA Reddy V.S., Nemerow G.R.;
RT "Structures and organization of adenovirus cement proteins provide insights
RT into the role of capsid maturation in virus entry and infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11715-11720(2014).
CC -!- FUNCTION: Structural component of the virion that acts as a cement
CC protein on the capsid exterior and which mediates the interactions
CC between the hexons, including the peripentonal hexons, and reaches all
CC the way to the penton vertices. Two hexon linking proteins IIIa, one
CC from each facet, stabilize the unique edge interface between a pair of
CC facets. As the virus enters the host cell, hexon linking proteins IIIa
CC are shed concomitant with virion acidification in the endosome. During
CC virus 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, ECO:0000269|PubMed:20798312,
CC ECO:0000269|PubMed:21632753, ECO:0000269|PubMed:25071205}.
CC -!- SUBUNIT: Interacts with hexon proteins; this interaction tethers the
CC peripentonal hexons to hexons situated in the facet (PubMed:20798312,
CC PubMed:25071205). Interacts with the penton protein (via N-terminus)
CC (PubMed:20798312). Interacts with packaging protein 3; this interaction
CC is required to promote correct genome packaging (PubMed:21632753).
CC {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000269|PubMed:20798312,
CC ECO:0000269|PubMed:21632753, ECO:0000269|PubMed:25071205}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04047,
CC ECO:0000269|PubMed:18786542, ECO:0000269|PubMed:20798312,
CC ECO:0000269|PubMed:25071205}. Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04047, ECO:0000305}. Note=Surrounds the border of each facet on
CC the capsid exterior. Present in around 60 copies per virion.
CC {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000269|PubMed:25071205}.
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 -!- CAUTION: An interaction between hexon-linking protein IIIa and hexon-
CC linking protein VIII as been described in PubMed:20798312. However, the
CC subcellular location of hexon-linking protein IIIa was incorrectly
CC assigned to the capsid interior. {ECO:0000305}.
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DR EMBL; M73260; AAA96407.1; -; Genomic_DNA.
DR EMBL; M22141; AAA42518.1; -; Genomic_DNA.
DR PIR; B39449; SXADH5.
DR RefSeq; AP_000205.1; AC_000008.1.
DR PDB; 6B1T; EM; 3.20 A; N=1-585.
DR PDB; 6CGV; X-ray; 3.80 A; M=1-585.
DR PDB; 7S78; EM; 3.72 A; M=1-585.
DR PDBsum; 6B1T; -.
DR PDBsum; 6CGV; -.
DR PDBsum; 7S78; -.
DR SMR; P12537; -.
DR PRIDE; P12537; -.
DR EvolutionaryTrace; P12537; -.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR GO; GO:0098021; C:viral capsid, decoration; IDA:UniProtKB.
DR DisProt; DP02508; -.
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 1: Evidence at protein level;
KW 3D-structure; Capsid decoration protein; Capsid protein; Host nucleus;
KW Late protein; Phosphoprotein; Viral genome packaging;
KW Viral release from host cell; Virion.
FT CHAIN 1..585
FT /note="Pre-hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000221835"
FT CHAIN 1..570
FT /note="Hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000421130"
FT PROPEP 571..585
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT /id="PRO_0000421129"
FT REGION 1..106
FT /note="Peripentonal hexon-tethering domain"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..251
FT /note="Binding to hexon-linking protein"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT REGION 438..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 570..571
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 225
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 274
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 310
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 444
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 449
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 450
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 452
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 469
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 473
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 490
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 494
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 515
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
SQ SEQUENCE 585 AA; 65253 MW; 430113688C473F1D CRC64;
MMQDATDPAV RAALQSQPSG LNSTDDWRQV MDRIMSLTAR NPDAFRQQPQ ANRLSAILEA
VVPARANPTH EKVLAIVNAL AENRAIRPDE AGLVYDALLQ RVARYNSGNV QTNLDRLVGD
VREAVAQRER AQQQGNLGSM VALNAFLSTQ PANVPRGQED YTNFVSALRL MVTETPQSEV
YQSGPDYFFQ TSRQGLQTVN LSQAFKNLQG LWGVRAPTGD RATVSSLLTP NSRLLLLLIA
PFTDSGSVSR DTYLGHLLTL YREAIGQAHV DEHTFQEITS VSRALGQEDT GSLEATLNYL
LTNRRQKIPS LHSLNSEEER ILRYVQQSVS LNLMRDGVTP SVALDMTARN MEPGMYASNR
PFINRLMDYL HRAAAVNPEY FTNAILNPHW LPPPGFYTGG FEVPEGNDGF LWDDIDDSVF
SPQPQTLLEL QQREQAEAAL RKESFRRPSS LSDLGAAAPR SDASSPFPSL IGSLTSTRTT
RPRLLGEEEY LNNSLLQPQR EKNLPPAFPN NGIESLVDKM SRWKTYAQEH RDVPGPRPPT
RRQRHDRQRG LVWEDDDSAD DSSVLDLGGS GNPFAHLRPR LGRMF
