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: 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 -!- 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 -!- SUBCELLULAR LOCATION: Virion. Host nucleus. Note=Surrounds the border CC of each facet on the capsid exterior. Present in around 60 copies per CC 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 # Revision 1.4 2019/11/20 //