CAP3_ADECR
ID CAP3_ADECR Reviewed; 563 AA.
AC Q96684;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 23-FEB-2022, entry version 57.
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 Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine adenovirus 1
OS (strain RI261)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX NCBI_TaxID=69151;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9129661; DOI=10.1099/0022-1317-78-4-873;
RA Morrison M.D., Onions D.E., Nicolson L.;
RT "Complete DNA sequence of canine adenovirus type 1.";
RL J. Gen. Virol. 78:873-878(1997).
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}.
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; Y07760; CAA69060.1; -; Genomic_DNA.
DR RefSeq; NP_044192.1; NC_001734.1.
DR SMR; Q96684; -.
DR GeneID; 1488925; -.
DR KEGG; vg:1488925; -.
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..563
FT /note="Pre-hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000221838"
FT CHAIN 1..548
FT /note="Hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000421392"
FT PROPEP 549..563
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT /id="PRO_0000421391"
FT REGION 1..117
FT /note="Peripentonal hexon-tethering domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 148..261
FT /note="Binding to hexon-linking protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 449..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 548..549
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 235
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 284
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 452
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"
FT MOD_RES 475
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 486
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
SQ SEQUENCE 563 AA; 63313 MW; AB343256C1318F4B CRC64;
MRKRRTLTAP SHFNSMSAAL NPMKMAAMQS QPTVDDSWAA SISRIMSLTA GDRHKFSSQP
FANRLDAILE AVVPSRKDPT HEKVLTIVNA LIENGAIRRD EGAGVYDALL HRVSKYNSIN
TQSNLERLAG DVREAVAQQV RIAAGNLGSL TALNSFLARL PANVERGQDN YTGFLSALKL
LVSEVPNTEV YQSGPHYFLQ SSRNGTQTVN LTNAFENLKP LWGVKAPTME RLSISALLTP
NTRLLLLLVS PFTDSVSISR DSYLGYLLTL YREALGRNHL DERTLEEVTE VSKAMGNENI
NNLQATLNFL LTNRQKKIPK DYSLTPEEER IVRFIQQAVS LRMMQENLSP TEALDVTAAN
MEPSFYANNR DFINKLMDYF HRAAAIAPDY FLGAVMNPRW LPPEGFFTGV FDFPERDNYI
WDGLDSSLDL TRQDAMRFLE EKFIDDDQRT ESRSVSRVPT PASSRRSSVA MASDSLIRPM
NNDKNSLREI EVLADKLARW KTYKRESEEA RESLPVIVRP KKYSSAISSD ESDDGMSKPD
KFLKFEGSGN PFAHLRPKLG RCL
