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Database: UniProt
Entry: A0A161CB96_9ADEN
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ID   A0A161CB96_9ADEN        Unreviewed;       920 AA.
AC   A0A161CB96;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Hexon protein {ECO:0000256|ARBA:ARBA00019716, ECO:0000256|RuleBase:RU361265};
DE            Short=CP-H {ECO:0000256|RuleBase:RU361265};
DE   AltName: Full=Protein II {ECO:0000256|ARBA:ARBA00032254, ECO:0000256|RuleBase:RU361265};
GN   ORFNames=CSPAdV-2_gp11 {ECO:0000313|EMBL:ALB78146.1};
OS   Chinstrap penguin adenovirus 2.
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Siadenovirus; Penguin siadenovirus A.
OX   NCBI_TaxID=1434088 {ECO:0000313|EMBL:ALB78146.1, ECO:0000313|Proteomes:UP000150550};
RN   [1] {ECO:0000313|EMBL:ALB78146.1, ECO:0000313|Proteomes:UP000150550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSPAdV_2 {ECO:0000313|EMBL:ALB78146.1};
RA   Lee S.-Y., Song J.-W.;
RT   "Analysis of complete genome sequence of novel adenoviruses in Antarctic
RT   penguin.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024662}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|RuleBase:RU361265}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. Virion
CC       {ECO:0000256|RuleBase:RU361265}. Host nucleus
CC       {ECO:0000256|RuleBase:RU361265}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000256|RuleBase:RU361265}.
CC   -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC       {ECO:0000256|ARBA:ARBA00008659, ECO:0000256|RuleBase:RU361265}.
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DR   EMBL; KP144329; ALB78146.1; -; Genomic_DNA.
DR   OrthoDB; 198at10239; -.
DR   Proteomes; UP000150550; Segment.
DR   GO; GO:0039623; C:T=25 icosahedral viral capsid; 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; 2.70.9.10; Adenovirus Type 2 Hexon, domain 4; 2.
DR   Gene3D; 3.90.39.10; Hexon Major Viral Coat Protein, domain 2; 1.
DR   Gene3D; 3.90.249.10; Hexon Major Viral Coat Protein, domain 3; 2.
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; IPR016112; VP_dsDNA_II.
DR   Pfam; PF01065; Adeno_hexon; 1.
DR   Pfam; PF03678; Adeno_hexon_C; 1.
DR   SUPFAM; SSF49749; Group II dsDNA viruses VP; 2.
PE   2: Evidence at transcript level;
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561,
KW   ECO:0000256|RuleBase:RU361265};
KW   Cytoplasmic inwards viral transport {ECO:0000256|ARBA:ARBA00023120};
KW   Host nucleus {ECO:0000256|RuleBase:RU361265};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Late protein {ECO:0000256|RuleBase:RU361265};
KW   Microtubular inwards viral transport {ECO:0000256|ARBA:ARBA00022952};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   T=25 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00023275,
KW   ECO:0000256|RuleBase:RU361265};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU361265};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   DOMAIN          7..592
FT                   /note="Adenovirus Pll hexon N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01065"
FT   DOMAIN          593..824
FT                   /note="Adenovirus Pll hexon C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03678"
FT   REGION          166..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  103226 MW;  16BE505A11771951 CRC64;
     MDISNGTPKL DIFHIAGQDA SEYLSENLVN FISSTESYFP INKKFRETVV APTKNVTTEQ
     SQRLQVRIVP TLTQDLENSF TARFTIAVGD GRVLDMGSTY FDIRGFLDRG HSFKPYGGTA
     YNSMAPRSAQ FNNIRKLTQT TTLSAQLSNI YTVSTSGNAC QAAKTKSDSF TNDKPSPHTG
     LLDSTFSPAT EGGIGRAVIM DDDAKETTCY GAYAKATNSN GQQIAAGQSV QKKFTNAGLR
     TGSGTSCTGA IAAEKFAVTY PDTRIVAYDD SDKLATRMGS RTNFIGFRDN FIGLMYYDNG
     AHSGSLATET GDINLVEQLQ DRNTEISYQY MLADLMSRQH YFSQWNQAVD DYDLNVRVLT
     NSGYEEGPPG YVFPSVGMGN YPSEPLFIGQ MVENSGGSTS TQTQNTSAVV GFGSVPTMEM
     NVNAYLQRCW LYANVAEYLP DEYKTKVTGT TETDPHTYAY MNAMLPNINV VDLFTNIGGR
     YSLDCMDNVN PFNHHRNRGL QYRSQLLGNG RYCNFHIQVP QKFFAVRNLL LTPGTYSYEW
     WFRKDPNVVL QSTMGNDLRK DGASIHYTSI NLFASFFPMD HATCSELILM LRNDQNDQSF
     MDYMGAKNNL YIVPPNQTNL QIEIPSRSWT AFRGWSFNRV KAAETPAVWS TYDVNFRYSG
     SIPYLDGTFY LSHTFNSMSI TFDSAISWPG NDRMLIPNYF EIKRRVDSEG YTTSQSNITK
     DFYLIQMSAN YNQGYHGYSF PADKTYRQYD FISNFDPMSI QVPQYGSEAY DLLSESFKQN
     VSNNVIINNS GFVPSRDTAI VAAQEGHPYP ANWPMPLIGE HAVEATRTIR KFLCDKYLWT
     IPFSSNFLNM GELTDLGQSL LYTESAHSLQ ITFDLDPMPE TTYVYMLYNV FDAVRVNQPN
     KNYLSAAYFR TPFATGTASA
//
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