ID   CAP9_ADE03              Reviewed;         138 AA.
AC   P68970; P03283;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 33.
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}; Synonyms=PIX;
OS   Human adenovirus B serotype 3 (HAdV-3) (Human adenovirus 3).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX   NCBI_TaxID=45659;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7262560; DOI=10.1016/0378-1119(81)90018-4;
RA   Engler J.A.;
RT   "The nucleotide sequence of the polypeptide IX gene of human adenovirus
RT   type 3.";
RL   Gene 13:387-394(1981).
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; J01962; AAA42510.1; -; Genomic_DNA.
DR   PIR; B03854; SXAD93.
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..138
FT                   /note="Hexon-interlacing protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
FT                   /id="PRO_0000221845"
FT   COILED          100..127
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
SQ   SEQUENCE   138 AA;  14107 MW;  B45EFBD6F7933EF2 CRC64;
     MSGSASFEGG VFSPYLTGRL PPWAGVRQNV MGSTVDGRPV QPANSSTLTY ATLSSSPLDA
     AAAAAATAAA NTILGMGYYG SIVANSSSSN NPSTLAEDKL LVLLAQLEAL TQRLGELSKQ
     VAQLREQTES AVATAKSK