CAP9_ADE02
ID CAP9_ADE02 Reviewed; 140 AA.
AC P03282;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 70.
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 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6985473; DOI=10.1016/s0092-8674(80)80044-4;
RA Alestroem P., Akusjaervi G., Perricaudet M., Mathews M.B., Klessig D.F.,
RA Pettersson U.;
RT "The gene for polypeptide IX of adenovirus type 2 and its unspliced
RT messenger RNA.";
RL Cell 19:671-681(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7142161; DOI=10.1016/s0021-9258(18)33473-2;
RA Gingeras T.R., Sciaky D., Gelinas R.E., Bing-Dong J., Yen C.E., Kelly M.M.,
RA Bullock P.A., Parsons B.L., O'Neill K.E., Roberts R.J.;
RT "Nucleotide sequences from the adenovirus-2 genome.";
RL J. Biol. Chem. 257:13475-13491(1982).
RN [3]
RP PROTEIN SEQUENCE OF 126-140, AND PHOSPHORYLATION AT SER-135.
RX PubMed=22939182; DOI=10.1016/j.virol.2012.08.012;
RA Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J.,
RA Pettersson U.;
RT "The phosphoproteome of the adenovirus type 2 virion.";
RL Virology 433:253-261(2012).
RN [4]
RP FUNCTION, AND INTERACTION WITH KLC1.
RX PubMed=21925109; DOI=10.1016/j.chom.2011.08.010;
RA Strunze S., Engelke M.F., Wang I.H., Puntener D., Boucke K., Schleich S.,
RA Way M., Schoenenberger P., Burckhardt C.J., Greber U.F.;
RT "Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore
RT complex promote virus infection.";
RL Cell Host Microbe 10:210-223(2011).
RN [5]
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).
CC -!- FUNCTION: Structural component of the virion that forms triskelion
CC structures consisting of three molecules that stabilize three hexon
CC trimers at the center of each icosahedral facet and fixes the
CC peripentonal hexons (By similarity). Dispensable for assembly. During
CC virus entry, recruits the anterograde motor kinesin-1 to the capsid
CC docked at the nuclear pore complex thereby subjecting the docked capsid
CC to a pulling force (PubMed:21925109). The resulting tension leads to
CC capsid disruption, dispersion of capsid fragments toward cell periphery
CC and eventually viral DNA entry into the host nucleus (PubMed:21925109).
CC {ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000269|PubMed:21925109}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with hexon protein; this
CC interaction tethers the hexons together (By similarity). Self-interacts
CC with adjacent proteins (By similarity). Interacts with kinesin light
CC chain KLC1; this interaction leads to capsid disruption at the nuclear
CC pore complex during virus entry into host cell (PubMed:21925109).
CC {ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000269|PubMed:21925109}.
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}.
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; J01917; AAA92204.1; -; Genomic_DNA.
DR PIR; C03853; SXAD92.
DR RefSeq; AP_000164.1; AC_000007.1.
DR RefSeq; NP_040514.1; NC_001405.1.
DR SMR; P03282; -.
DR DIP; DIP-29897N; -.
DR iPTMnet; P03282; -.
DR GeneID; 2653012; -.
DR KEGG; vg:2653012; -.
DR Proteomes; UP000008167; 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:0019061; P:uncoating of virus; IDA:UniProtKB.
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 Capsid decoration protein; Capsid protein; Coiled coil;
KW Direct protein sequencing; Host nucleus; Host-virus interaction;
KW Phosphoprotein; Reference proteome; 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_0000221844"
FT COILED 100..127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04050"
FT MOD_RES 135
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:22939182"
SQ SEQUENCE 140 AA; 14428 MW; DB4640E5CBB616EB CRC64;
MSANSFDGSI VSSYLTTRMP PWAGVRQNVM GSSIDGRPVL PANSTTLTYE TVSGTPLETA
ASAAASAAAA TARGIVTDFA FLSPLASSAA SRSSARDDKL TALLAQLDSL TRELNVVSQQ
LLDLRQQVSA LKASSPPNAV
