CAPSH_ADE31
ID CAPSH_ADE31 Reviewed; 468 AA.
AC P36855;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 29-SEP-2021, entry version 86.
DE RecName: Full=Hexon protein;
DE Short=CP-H;
DE AltName: Full=Protein II;
DE Flags: Fragment;
GN ORFNames=L3;
OS Human adenovirus A serotype 31 (HAdV-31) (Human adenovirus 31).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=10529;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VRL 15/62;
RX PubMed=8023012; DOI=10.1016/s0923-2516(07)80004-5;
RA Pring-Akerblom P., Adrian T.;
RT "Type- and group-specific polymerase chain reaction for adenovirus
RT detection.";
RL Res. Virol. 145:25-35(1994).
CC -!- FUNCTION: Major capsid protein that self-associates to form 240 hexon
CC trimers, each in the shape of a hexagon, building most of the pseudo
CC T=25 capsid. Assembled into trimeric units with the help of the
CC chaperone shutoff protein. Transported by pre-protein VI to the nucleus
CC where it associates with other structural proteins to form an empty
CC capsid. Might be involved, through its interaction with host dyneins,
CC in the intracellular microtubule-dependent transport of incoming viral
CC capsid to the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with the capsid vertex
CC protein; this interaction binds the peripentonal hexons to the
CC neighboring penton base. Interacts with the hexon-linking protein; this
CC interaction tethers the hexons surrounding the penton to those situated
CC in the central plate of the facet. Interacts with the hexon-interlacing
CC protein; this interaction lashes the hexons together. Interacts with
CC host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved
CC in intracellular microtubule-dependent transport of incoming viral
CC capsid. Interacts with the shutoff protein; this interaction allows
CC folding and formation of hexons trimers. Interacts with pre-protein VI;
CC this interaction probably allows nuclear import of hexon trimers and
CC possibly pre-capsid assembly (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host nucleus {ECO:0000250}.
CC Note=Forms the capsid icosahedric shell. Present in 720 copies per
CC virion, assembled in 240 trimers (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC are produced by alternative splicing and alternative polyadenylation of
CC the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC present in the N-terminus of all these mRNAs and is recognized by the
CC viral shutoff protein to provide expression although conventional
CC translation via ribosome scanning from the cap has been shut off in the
CC host cell (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC {ECO:0000305}.
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DR EMBL; X74661; CAA52725.1; -; Genomic_DNA.
DR PIR; S37217; S37217.
DR SMR; P36855; -.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039623; C:T=25 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.90.249.10; -; 1.
DR InterPro; IPR016107; Adenovirus_Pll_hexon_N.
DR InterPro; IPR016110; Adenovirus_Pll_hexon_sub3.
DR InterPro; IPR016112; VP_dsDNA_II.
DR Pfam; PF01065; Adeno_hexon; 1.
DR SUPFAM; SSF49749; SSF49749; 1.
PE 2: Evidence at transcript level;
KW Capsid protein; Cytoplasmic inwards viral transport; Host nucleus;
KW Host-virus interaction; Late protein; Microtubular inwards viral transport;
KW T=25 icosahedral capsid protein; Virion; Virus entry into host cell.
FT CHAIN <1..>468
FT /note="Hexon protein"
FT /id="PRO_0000221823"
FT NON_TER 1
FT NON_TER 468
SQ SEQUENCE 468 AA; 52100 MW; 8727BFA49179CE68 CRC64;
FDIRGVLDGP SFKPYSGSAY NSLAPKAAPN ASQWLTTNNG NKTHTFAQAP YIGDSISKDG
IQVGTNTANP QQAVYADKTY QPEPQVGESQ WNASVSNNAK AAGRVLKSTT PMYPCYGSYA
RATNEKGGQS KNNDGVEMRF FASSANDNQN DPTVVMYSED VNLEAPDTHI VYKPAVTADT
ISSELLHGQQ AAPNRPNYIA FRDNFYWALY YNSTGNMGVL AGQASQLNAV VDLQDRNTEL
SYQLMLDALG DRSRYFSMWN SAVDSYDPDV RIIENHGVED ELPNYCFPLG AVGVVNSYKG
VKQNDGNGWV KDDSVADTND IAKGNIFAME INLQANLWRS FLYSNVGLYL PDDLKYTPGN
IKLPENKNTY EYMNGRVTVP GLVDTYVNIG ARWYPDVMDN INPFNHHRNA GLRYRSMLLG
NGRFVPFHIQ VPQKFFAIKN LLLLPGSYTY EWNFRKDVNM ILQSTLGN