CAP9_ADE12
ID CAP9_ADE12 Reviewed; 144 AA.
AC P03284;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 75.
DE RecName: Full=Hexon-interlacing protein {ECO:0000255|HAMAP-Rule:MF_04050};
DE AltName: Full=Protein IX {ECO:0000255|HAMAP-Rule:MF_04050};
GN Name=IX {ECO:0000255|HAMAP-Rule:MF_04050};
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 [GENOMIC DNA].
RX PubMed=7326748; DOI=10.1016/0092-8674(81)90366-4;
RA Bos J.L., Polder L.J., Bernards R., Schrier P.I., van den Elsen P.J.,
RA van der Eb A.J., van Ormondt H.;
RT "The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two tumor antigens
RT starting at different AUG triplets.";
RL Cell 27:121-131(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6275367; DOI=10.1093/nar/9.23.6571;
RA Kimura T., Sawada Y., Shinawawa M., Shimizu Y., Shiroki K., Shimojo H.,
RA Sugisaki H., Takanami M., Uemizu Y., Fujinaga K.;
RT "Nucleotide sequence of the transforming early region E1b of adenovirus
RT type 12 DNA: structure and gene organization, and comparison with those of
RT adenovirus type 5 DNA.";
RL Nucleic Acids Res. 9:6571-6589(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kimura T.;
RT "Structure and sequence analysis of the transforming region E1B of human
RT adenovirus type 12.";
RL Sapporo Igaku Zasshi 52:253-267(1983).
RN [4]
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).
CC -!- FUNCTION: Structural component of the virion that acts as a cement
CC protein on the capsid exterior and forms triskelion structures
CC consisting of three molecules that stabilize three hexon trimers at the
CC center of each icosahedral facet and fixes the peripentonal hexons.
CC Dispensable for assembly. During virus entry, recruits the anterograde
CC motor kinesin-1 to the capsid docked at the nuclear pore complex
CC thereby subjecting the docked capsid to a pulling force. The resulting
CC tension leads to capsid disruption, dispersion of capsid fragments
CC toward cell periphery and eventually viral DNA entry into the host
CC nucleus. {ECO:0000255|HAMAP-Rule:MF_04050}.
CC -!- SUBUNIT: Homotrimer. Interacts with hexon protein; this interaction
CC tethers the hexons together. Self-interacts with adjacent proteins.
CC Interacts with kinesin light chain KLC1; this interaction leads to
CC capsid disruption at the nuclear pore complex during virus entry into
CC host cell. {ECO:0000255|HAMAP-Rule:MF_04050}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04050}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04050}. Note=Located in the canyons
CC between the hexons on the outer surface of the capsid. Forms a sort of
CC hairnet on the outer side of the virion. Present in 240 copies per
CC virion. {ECO:0000255|HAMAP-Rule:MF_04050}.
CC -!- INDUCTION: Expressed in the intermediate phase of the viral replicative
CC cycle. {ECO:0000255|HAMAP-Rule:MF_04050}.
CC -!- DOMAIN: Three N-terminal domains of hexon-interlacing protein form
CC triskelions between hexon capsomers. {ECO:0000255|HAMAP-Rule:MF_04050}.
CC -!- MISCELLANEOUS: This protein is only encoded by mastadenoviruses, and
CC may therefore play a role in mammals tropism. {ECO:0000255|HAMAP-
CC Rule:MF_04050}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon-interlacing protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000305}.
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DR EMBL; V00004; CAA23411.1; -; Genomic_DNA.
DR EMBL; M55003; AAA42500.1; -; Genomic_DNA.
DR EMBL; X73487; CAA51880.1; -; Genomic_DNA.
DR PIR; A90814; SXAD12.
DR RefSeq; NP_040913.1; NC_001460.1.
DR PRIDE; P03284; -.
DR GeneID; 1460846; -.
DR KEGG; vg:1460846; -.
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 GO; GO:0031423; F:hexon binding; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04050; ADV_CAP9; 1.
DR InterPro; IPR005641; Hexon_assoc_IX.
DR Pfam; PF03955; Adeno_PIX; 1.
PE 3: Inferred from homology;
KW Capsid decoration protein; Capsid protein; Coiled coil; Host nucleus;
KW Host-virus interaction; Virion; Virus entry into host cell.
FT CHAIN 1..144
FT /note="Hexon-interlacing protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
FT /id="PRO_0000221848"
FT COILED 106..133
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
SQ SEQUENCE 144 AA; 15017 MW; EFC24A73CA978D82 CRC64;
MNGTTQNNAA LFDGGVFSPY LTSRLPYWAG VRQNVVGSTV DGRPVAPANS STLTYATIGP
SPLDTAAAAA ASAAASTARS MAADFSFYNH LASNAVTRTA VREDILTVML AKLETLTAQL
EELSQKVEEL ADATTHTPAQ PVTQ
