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CAP9_ADE05
ID   CAP9_ADE05              Reviewed;         140 AA.
AC   P03281;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 85.
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 C serotype 5 (HAdV-5) (Human adenovirus 5).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus.
OX   NCBI_TaxID=28285;
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=6250944; DOI=10.1016/0378-1119(80)90140-7;
RA   Maat J., van Beveren C.P., van Ormondt H.;
RT   "The nucleotide sequence of adenovirus type 5 early region E1: the region
RT   between map positions 8.0 (HindIII site) and 11.8 (SmaI site).";
RL   Gene 10:27-38(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA   Chroboczek J., Bieber F., Jacrot B.;
RT   "The sequence of the genome of adenovirus type 5 and its comparison with
RT   the genome of adenovirus type 2.";
RL   Virology 186:280-285(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=23142869; DOI=10.1038/nmeth.2227;
RA   Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT   "De novo derivation of proteomes from transcriptomes for transcript and
RT   protein identification.";
RL   Nat. Methods 9:1207-1211(2012).
RN   [5]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE,
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEXON PROTEIN, AND DOMAIN.
RX   PubMed=20798312; DOI=10.1126/science.1187433;
RA   Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.;
RT   "Atomic structure of human adenovirus by cryo-EM reveals interactions among
RT   protein networks.";
RL   Science 329:1038-1043(2010).
RN   [6]
RP   REVIEW.
RX   PubMed=22754652; DOI=10.3390/v4050847;
RA   San Martin C.;
RT   "Latest insights on adenovirus structure and assembly.";
RL   Viruses 4:847-877(2012).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), INTERACTION WITH THE HEXON PROTEIN,
RP   FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=25071205; DOI=10.1073/pnas.1408462111;
RA   Reddy V.S., Nemerow G.R.;
RT   "Structures and organization of adenovirus cement proteins provide insights
RT   into the role of capsid maturation in virus entry and infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11715-11720(2014).
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, ECO:0000269|PubMed:20798312,
CC       ECO:0000269|PubMed:25071205}.
CC   -!- SUBUNIT: Homotrimer. Interacts with hexon protein; this interaction
CC       tethers the hexons together (PubMed:20798312, PubMed:25071205). Self-
CC       interacts with adjacent proteins (PubMed:20798312, PubMed:25071205).
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 (By similarity). {ECO:0000250|UniProtKB:P03282,
CC       ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000269|PubMed:20798312,
CC       ECO:0000269|PubMed:25071205}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04050,
CC       ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}. Host nucleus
CC       {ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000305|PubMed:20798312}.
CC       Note=Located in the canyons between the hexons on the outer surface of
CC       the capsid. Forms a sort of hairnet on the outer side of the virion.
CC       Present in 240 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04050,
CC       ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}.
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       ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}.
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; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X02996; CAA26746.1; -; Genomic_DNA.
DR   PIR; A03853; SXAD95.
DR   RefSeq; AP_000200.1; AC_000008.1.
DR   PDB; 6B1T; EM; 3.20 A; Q/R/S/T=1-140.
DR   PDB; 6CGV; X-ray; 3.80 A; P/Q/R/S=1-140.
DR   PDB; 7S78; EM; 3.72 A; P/Q/R/S=1-140.
DR   PDBsum; 6B1T; -.
DR   PDBsum; 6CGV; -.
DR   PDBsum; 7S78; -.
DR   SMR; P03281; -.
DR   DIP; DIP-29895N; -.
DR   IntAct; P03281; 2.
DR   MINT; P03281; -.
DR   EvolutionaryTrace; P03281; -.
DR   Proteomes; UP000004992; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0098021; C:viral capsid, decoration; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Capsid decoration protein; Capsid protein; Coiled coil;
KW   Host nucleus; Host-virus interaction; Virion; Virus entry into host cell.
FT   CHAIN           1..140
FT                   /note="Hexon-interlacing protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
FT                   /id="PRO_0000221846"
FT   COILED          100..127
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
SQ   SEQUENCE   140 AA;  14458 MW;  DAFD4045CAB616FB CRC64;
     MSTNSFDGSI VSSYLTTRMP PWAGVRQNVM GSSIDGRPVL PANSTTLTYE TVSGTPLETA
     ASAAASAAAA TARGIVTDFA FLSPLASSAA SRSSARDDKL TALLAQLDSL TRELNVVSQQ
     LLDLRQQVSA LKASSPPNAV
 
 
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