ID   CAP9_ADET1              Reviewed;         122 AA.
AC   P04376;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   10-FEB-2021, entry version 58.
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   Tree shrew adenovirus serotype 1 (TSAdV-1) (Tupaia adenovirus 1).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Tree shrew mastadenovirus A.
OX   NCBI_TaxID=47680;
OH   NCBI_TaxID=9393; Tupaiidae (tree shrews).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3159623; DOI=10.1016/0378-1119(85)90296-3;
RA   Flugel R.M., Bannert H., Suhai S., Darai G.;
RT   "The nucleotide sequence of the early region of the Tupaia adenovirus DNA
RT   corresponding to the oncogenic region E1b of human adenovirus 7.";
RL   Gene 34:73-80(1985).
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}.
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DR   EMBL; M10054; AAA42532.1; -; Genomic_DNA.
DR   PIR; A03856; SXAD9T.
DR   SMR; P04376; -.
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..122
FT                   /note="Hexon-interlacing protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
FT                   /id="PRO_0000221854"
FT   COILED          72..106
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
SQ   SEQUENCE   122 AA;  13491 MW;  D888D25170BB9E2B CRC64;
     MSSNDNSGIV NTCFLTTRLP AWAGVRQDEV GSDVNGLPII PSNSMQIRSR AATTDAATEP
     STRQGLNLLR SVTELNESID ELQQKMTELE KRLKIMEEKI EEIKLALANP LIENPHDGNF
     IV