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 24-JAN-2024, entry version 85. 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; Human mastadenovirus C. 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}. 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; 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 EMDB; EMD-24881; -. DR EMDB; EMD-7034; -. DR SMR; P12537; -. DR IntAct; P12537; 5. 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; Pre-hexon-linking protein IIIa; 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 //