CAP3_ADE12
ID CAP3_ADE12 Reviewed; 582 AA.
AC P36712;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 23-FEB-2022, entry version 70.
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 A serotype 12 (HAdV-12) (Human adenovirus 12).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=28282;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994;
RA Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT functional analysis.";
RL J. Virol. 68:379-389(1994).
RN [2]
RP PROTEIN SEQUENCE OF 566-576.
RC STRAIN=Huie;
RX PubMed=8438575; DOI=10.1006/viro.1993.1131;
RA Freimuth P., Anderson C.W.;
RT "Human adenovirus serotype 12 virion precursors pMu and pVI are cleaved at
RT amino-terminal and carboxy-terminal sites that conform to the adenovirus 2
RT endoproteinase cleavage consensus sequence.";
RL Virology 193:348-355(1993).
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; X73487; CAA51886.1; -; Genomic_DNA.
DR PIR; S33937; S33937.
DR RefSeq; NP_040919.1; NC_001460.1.
DR SMR; P36712; -.
DR GeneID; 1460848; -.
DR KEGG; vg:1460848; -.
DR Proteomes; UP000004993; Genome.
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 1: Evidence at protein level;
KW Capsid decoration protein; Capsid protein; Direct protein sequencing;
KW Host nucleus; Late protein; Phosphoprotein; Viral genome packaging;
KW Viral release from host cell; Virion.
FT CHAIN 1..582
FT /note="Pre-hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000221836"
FT CHAIN 1..565
FT /note="Hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000421388"
FT PROPEP 566..582
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT /id="PRO_0000421387"
FT REGION 1..114
FT /note="Peripentonal hexon-tethering domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 146..259
FT /note="Binding to hexon-linking protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 437..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 565..566
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03279, ECO:0000255|HAMAP-
FT Rule:MF_04047"
FT MOD_RES 233
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 282
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 458
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 465
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 482
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT MOD_RES 503
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
SQ SEQUENCE 582 AA; 64787 MW; 8341875AE9A267F1 CRC64;
MQRPAIIAER APNLDPAVLA AMQSQPSGVT ASDDWTAAMD RIMALTARSP DAFRQQPQAN
RFSAILEAVV PSRTNPTHEK VLTIVNALLD SKAIRKDEAG LIYNALLERV ARYNSTNVQA
NLDRMGTDVK EALAQRERFH RDGNLGSLVA LNAFLSTQPA NVPRGQEDYT NFISALRLMV
TEVPQSEVYQ SGPDYFFQTS RQGLQTVNLT QAFKNLQGLW GVRAPVGDRS TLSSLLTPNS
RLLLLLIAPF TNTNSLSRDS YLGHLVTLYR EAIGQAQVDE QTYQEITSVS RALGQEDTGS
LEATLNFLLT NRRQQVPPQY TLNAEEERIL RYVQQSVSLY LMREGATPSA ALDMTARNME
PSFYASNRAF INRLMDYLHR AAAMNGEYFT NAILNPHWLP PPGFYTGEFD LPEGNDGFLW
DDVTDSLFSP AVIGHHGKKE AGDEGPLLDS RASSPFPSLT SLPASVNSGR TTRPRLTGES
EYLNDPILFP VRDKNFPNNG IESLVDKMSR WKTYAQERRE WEERQPRPVR PPRQRWQRRK
KGAHAGDEGS DDSADDSSVL DLGGSGNPFA HLRPQGCIGS LY
