CAP3_ADEM1
ID CAP3_ADEM1 Reviewed; 494 AA.
AC O10438;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 12-AUG-2020, entry version 51.
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 Murine adenovirus A serotype 1 (MAdV-1) (Murine adenovirus 1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Murine mastadenovirus A.
OX NCBI_TaxID=10530;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Meissner J.D., Hirsch G.N., Larue E.A., Fulcher R.A., Spindler K.R.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; U95843; AAB53753.1; -; Genomic_DNA.
DR SMR; O10438; -.
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; Viral genome packaging; Viral release from host cell;
KW Virion.
FT CHAIN 1..494
FT /note="Pre-hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000221840"
FT CHAIN 1..483
FT /note="Hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000439412"
FT PROPEP 484..494
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000439413"
FT REGION 1..101
FT /note="Peripentonal hexon-tethering domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 132..245
FT /note="Binding to hexon-linking protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT SITE 483..484
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 268
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 439
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 456
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
SQ SEQUENCE 494 AA; 56016 MW; 83A6B9D6D61D8F8B CRC64;
MAALSPTVRA ALQSQAAGEE PWEQRFKRIM STTLKNPGAF RSQPWFTRRD AILEAVLPSR
TDPTHEKVLA VVNGLVQAKA VRADEGGAIY DALLQRVGRY NSSNVQSNLD HLVQDVREAV
AMKAQEERGS MGSLVALNGF LSTLPSTVNH GQSDYVGFVG ALRQLIAEVP QTLVYRTGPF
YYFQTSRQGL QTVNLTKAFQ NLSALWGVTT SAQTPMATAA LLTPNTRLLL LLVAPFTDSR
TVNGDTYLGH LLTLYREALR DARLDEITYS EIRDVARATG QDDSRALQST LNFLVSQQTK
RLPEDVFLTP QQTTVLRYLQ KAIELQHARE PHERADRLLD AVVADLEPSF YSKHRHFITK
LLDYFQRAAA LNPHYFMSIV KNKHWTPPPG FYTGDFELPE VVHDSFQWDD TEDGAWSRPL
AEQVNEEEPN TDYLAEYRSA FSDNREEKNQ KKEWESLVDM MARWKTHRQS ALDLDDEIEE
LSSTNPFKHL QPQF
