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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
