AC MF_04047; DC Protein; auto TR HAMAP; MF_04047; -; 1; level=0 XX Names: ADV_CAP3 XX ID CAP3 DE RecName: Full=Pre-hexon-linking protein IIIa; DE AltName: Full=Capsid vertex-specific component IIIa; DE Short=CVSC; DE AltName: Full=Protein IIIa; DE AltName: Full=pIIIa; DE Contains: DE RecName: Full=Hexon-linking protein IIIa; XX CC -!- FUNCTION: [Hexon-linking protein IIIa]: Structural component of the CC virion that acts as a cement protein on the capsid interior and which CC mediates the interactions between the hexons, including the CC peripentonal hexons, and reaches all the way to the penton vertices. CC Two hexon linking proteins IIIa, one from each facet, stabilize the CC unique edge interface between a pair of facets. As the virus enters the CC host cell, hexon linking proteins IIIa are shed concomitant with virion CC acidification in the endosome. During virus assembly, seems to play a CC role in the serotype specificity of the packaging of viral DNA via its CC interaction with packaging protein 3. CC -!- SUBUNIT: [Hexon-linking protein IIIa]: Interacts with hexon proteins; CC this interaction tethers the peripentonal hexons to hexons situated in CC the facet. Interacts with the penton protein (via N-terminus). CC Interacts with packaging protein 3; this interaction is required to CC promote correct genome packaging. Interacts with hexon-linking protein CC VIII. CC -!- SUBCELLULAR LOCATION: [Hexon-linking protein IIIa]: Virion. Host CC nucleus. Note=Located on the inner side of the capsid shell. 5 copies CC cement the gaps between the penton base and peripenton hexons around CC each 5-fold axis. Present in 60 copies per virion. CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle. CC -!- PTM: Cleaved near the C-terminus by the viral protease during virion CC maturation to form the mature protein. 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. CC -!- SIMILARITY: Belongs to the adenoviridae hexon-linking protein IIIa CC family. XX DR Pfam; PF02455; Hex_IIIa; 1; trigger=no XX KW Capsid decoration protein KW Capsid protein KW Host nucleus KW Late protein KW Phosphoprotein KW Viral genome packaging KW Virion KW Viral release from host cell XX GO GO:0042025; C:host cell nucleus GO GO:0019028; C:viral capsid GO GO:0098021; C:viral capsid, decoration XX FT From: CAP3_ADE05 (P12537) FT CHAIN Nter..Cter FT /note="Pre-hexon-linking protein IIIa" FT CHAIN Nter..570 FT /note="Hexon-linking protein IIIa" FT PROPEP 571..Cter FT REGION Nter..106 FT /note="Peripentonal hexon-tethering domain" FT REGION 138..251 FT /note="Binding to hexon-linking protein" FT SITE 570..571 FT /note="Cleavage; by viral protease" FT MOD_RES 225 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 274 FT /note="Phosphothreonine; by host" FT Condition: T FT MOD_RES 310 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 444 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 449 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 450 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 452 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 469 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 473 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 490 FT /note="Phosphotyrosine; by host" FT Condition: Y FT MOD_RES 494 FT /note="Phosphoserine; by host" FT Condition: S FT MOD_RES 515 FT /note="Phosphoserine; by host" FT Condition: S XX Size: 494-615; Related: None; Template: P12537; Scope: Viruses; Adenoviridae Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Version: 6 # Last updated date: 2025-07-02 # Created date: 2017-02-13 //