CAPSH_ADE09
ID CAPSH_ADE09 Reviewed; 943 AA.
AC P36853; Q5TJ04;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 3.
DT 23-FEB-2022, entry version 103.
DE RecName: Full=Hexon protein {ECO:0000255|HAMAP-Rule:MF_04051};
DE Short=CP-H {ECO:0000255|HAMAP-Rule:MF_04051};
DE AltName: Full=Protein II {ECO:0000255|HAMAP-Rule:MF_04051};
GN Name=L3 {ECO:0000255|HAMAP-Rule:MF_04051};
OS Human adenovirus D serotype 9 (HAdV-9) (Human adenovirus 9).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus D.
OX NCBI_TaxID=10527;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate ATCC VR-1086 / Hicks / V-209-003-014;
RA Buettner W.H., Veres-Molnar S.K.;
RT "Adenovirus type 9, complete sequence.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-621.
RC STRAIN=Isolate ATCC VR-1086 / Hicks / V-209-003-014, and Isolate N-62;
RX PubMed=7491756; DOI=10.1006/viro.1995.0004;
RA Eiz B., Adrian T., Pring-Akerblom P.;
RT "Immunological adenovirus variant strains of subgenus D: comparison of the
RT hexon and fiber sequences.";
RL Virology 213:313-320(1995).
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. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC -!- SUBUNIT: Homotrimer. Interacts with the capsid vertex protein; this
CC interaction binds the peripentonal hexons to the neighboring penton
CC base. Interacts with the hexon-linking protein; this interaction
CC tethers the hexons surrounding the penton to those situated in the
CC 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. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04051}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04051}. Note=Forms the capsid
CC icosahedric shell. Present in 720 copies per virion, assembled in 240
CC trimers. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04051}.
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. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04051, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52721.1; Type=Erroneous initiation; Note=Extended N-terminus.;
CC Sequence=CAA52728.1; Type=Erroneous initiation; Note=Extended N-terminus.;
CC Sequence=CAI05969.1; Type=Erroneous initiation; Note=Extended N-terminus.;
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DR EMBL; AJ854486; CAI05969.1; ALT_INIT; Genomic_DNA.
DR EMBL; X74664; CAA52728.1; ALT_INIT; Genomic_DNA.
DR EMBL; X74657; CAA52721.1; ALT_INIT; Genomic_DNA.
DR PIR; S37279; S37279.
DR SMR; P36853; -.
DR Proteomes; UP000118285; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039623; C:T=25 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.249.10; -; 3.
DR Gene3D; 3.90.39.10; -; 1.
DR HAMAP; MF_04051; ADV_CAPSH; 1.
DR InterPro; IPR016108; Adenovirus_Pll_hexon_C.
DR InterPro; IPR016107; Adenovirus_Pll_hexon_N.
DR InterPro; IPR044942; Adenovirus_Pll_hexon_sub2.
DR InterPro; IPR016110; Adenovirus_Pll_hexon_sub3.
DR InterPro; IPR037542; ADV_hexon.
DR InterPro; IPR016112; VP_dsDNA_II.
DR Pfam; PF01065; Adeno_hexon; 1.
DR Pfam; PF03678; Adeno_hexon_C; 1.
DR SUPFAM; SSF49749; SSF49749; 2.
PE 3: Inferred from homology;
KW Acetylation; Capsid protein; Cytoplasmic inwards viral transport;
KW Host nucleus; Host-virus interaction; Late protein;
KW Microtubular inwards viral transport; Phosphoprotein;
KW T=25 icosahedral capsid protein; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT CHAIN 2..943
FT /note="Hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT /id="PRO_0000439756"
FT SITE 768
FT /note="Involved in interaction with pre-protein VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT MOD_RES 2
FT /note="N-acetylalanine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT MOD_RES 931
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT CONFLICT 155
FT /note="A -> R (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..235
FT /note="GQAK -> PVKPN (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="L -> M (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="G -> E (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="N -> H (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 477..478
FT /note="KY -> ND (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="V -> I (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="A -> T (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> H (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="R -> A (in Ref. 2; CAA52728/CAA52721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 943 AA; 106055 MW; AF4BD6628B6114D5 CRC64;
MATPSMMPQW AYMHIAGQDA SEYLSPGLVQ FARATDTYFS LGNKFRNPTV APTHDVTTDR
SQRLTLRFVP VDREDTTYSY KARFTLAVGD NRVLDMASTY FDIRGVLDRG PSFKPYSGTA
YNSLAPKGAP NSSQWLAKDT NAGDQALKTH THGVAAMGGT DITAKGLQIG VDTTENKNEP
IYANEIYQPE PQVGEENLQD VENFYGGRAL KKETKMKPCY GSFARPTNEK GGQAKFLTDG
DGQLTKNHDI TMNFFDTPGG TVGQDTELEA DIVMYAENVH LETPDTHVVY KPGTSDESSE
ANLVQQSMPN RPNYIGFRDN FVGLMYYNST GNMGVLAGQA SQLNAVVDLQ DRNTELSYQL
LLDSLGDRTR YFSMWNSAVD SYDPDVRIIE NHGVEDELPN YCFPLDGAGT NATYQGVKVK
NGQDGDVNAD WEKDPNLASR NQICKGNIFA MEINLQANLW KSFLYSNVAL YLPDSYKYTP
ANVTLPANTN TYEYMNGRVV APSLVDAYIN IGARWSLDPM DNVNPFNHHR NAGLRYRSML
LGNGRYVPFH IQVPQKFFAI KNLLLLPGSY TYEWNFRKDV NMILQSSLGN DLRVDGASVR
FDSVNLYATF FPMAHNTAST LEAMLRNDTN DQSFNDYLSA ANMLYPIPAK ATNVPISIPS
RNWAAFRGWS FTRLKTKETP SLGSGFDPYF VYSGSIPYLD GTFYLNHTFK KVSIMFDSSV
SWPGNDRLLT PNEFEIKRSV DGEGYNVAQC NMTKDWFLVQ MLSHYNIGYQ GFHVPEGYKD
RMYSFFRNFQ PMSRQVVDEI NYKDYKAVTL PFQHNNSGFT GYLAPTMRQG QPYPANFPYP
LIGQTAVPSV TQKKFLCDRV MWRIPFSSNF MSMGALTDLG QNMLYANSAH ALDMTFEVDP
MDEPTLLYLL FEVFDVVRVH QPHRGVIEAV YLRTPFSAGN ATT
