ID   CAPSD_HASV5             Reviewed;         783 AA.
AC   Q4TWH7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   02-JUN-2021, entry version 36.
DE   RecName: Full=Capsid polyprotein VP90;
DE   Contains:
DE     RecName: Full=Capsid polyprotein VP70;
DE   Contains:
DE     RecName: Full=Capsid protein VP34;
DE   Contains:
DE     RecName: Full=Capsid protein VP27;
DE   Contains:
DE     RecName: Full=Capsid protein VP25;
GN   ORFNames=ORF2;
OS   Human astrovirus-5 (HAstV-5).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Mamastrovirus.
OX   NCBI_TaxID=35741;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16421636; DOI=10.1007/s00705-005-0704-9;
RA   Silva P.A., Cardoso D.D., Schreier E.;
RT   "Molecular characterization of human astroviruses isolated in Brazil,
RT   including the complete sequences of astrovirus genotypes 4 and 5.";
RL   Arch. Virol. 151:1405-1417(2006).
CC   -!- FUNCTION: The capsid polyprotein VP90 self-assembles and undergoes a
CC       proteolytic cleavage by host caspases to yield the VP70 virions. This
CC       immature virion is composed of 180 VP70 subunits with 90 dimeric spikes
CC       and displays a T=3 icosahedral symmetry. The mature virion is obtained
CC       by further cleavages resulting in three structural proteins VP25, VP27
CC       and VP34. This forms contains only 30 spikes located on the icosahedral
CC       2-fold axes. Plays a role in the attachment to target host cell. This
CC       attachment induces virion internalization through clathrin-dependent
CC       endocytosis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90
CC       acidic C-terminal domain is eliminated from the immature virion by host
CC       caspases during viral maturation giving rise to virions composed of
CC       VP70. Further tryptic cleavages occur resulting in the three structural
CC       proteins VP34, VP27 and VP25 and confering infectivity (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the astroviridae capsid polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; DQ028633; AAY46274.1; -; Genomic_RNA.
DR   SMR; Q4TWH7; -.
DR   PRIDE; Q4TWH7; -.
DR   Proteomes; UP000008628; Genome.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; ISS:UniProtKB.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; ISS:UniProtKB.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR022027; Astro_capsid_p.
DR   InterPro; IPR004337; Capsid_astroviral.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF03115; Astro_capsid_N; 1.
DR   Pfam; PF12226; Astro_capsid_p; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   T=3 icosahedral capsid protein; Viral penetration into host cytoplasm;
KW   Virion; Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..783
FT                   /note="Capsid polyprotein VP90"
FT                   /id="PRO_0000320235"
FT   CHAIN           1..654
FT                   /note="Capsid polyprotein VP70"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419570"
FT   CHAIN           1..312
FT                   /note="Capsid protein VP34"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419571"
FT   CHAIN           393..645
FT                   /note="Capsid protein VP27"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419572"
FT   CHAIN           423..645
FT                   /note="Capsid protein VP25"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419573"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            312..313
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            392..393
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            422..423
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            645..646
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            654..655
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   783 AA;  86018 MW;  5B5972AC587C6BFF CRC64;
     MASKPSKQVT VEVNNGRSRS RSRPRSQSRG RDKSVKITVN SRNKGRRQNG RNKHQSNQRV
     RNIVNKQLRK QGVTGPKPAI CQRATATLGT VGSNTSGTTE IEACILLNPV LVKDATGSTQ
     FGPVQALGAQ YSMWKLKYLN VKLTSMVGSS AVNGTVVRVS LNPTSTPSST SWSGLGARKH
     LDVTVGKNAV FKLKPADLGG PRDGWWLTNT NDNASDTLGP SIEIHTLGRT MSSYQNQQFT
     GGLFLVELAS EWCFTGYAAN PNLVNLMKST DKQVNVTFNG SAGEPLVMSV PATSHFVRAV
     VARSTLPTSL ARAGERTTSD TVWQVLNTAV SAAELVTPPP FNWLVKGGWW FVKLIAGRTR
     NGTRSFYVYP SYQDALSNKP AICTGGLPSG LRAASAVATT LQFTQMNQPS LGHGENTATL
     GRSIATAGDR LKVILTVGQP VTPNENNKQT WVGKTNTPTE EVVKIGVNTQ NYNVMNGFTM
     ISSIDWYDEE MQPLEVPVPM SELLVMKGIN KKADVYAAQQ YKNSISNNKH QITSVYLVRV
     KENFQVTNHL SYFFREKVDT TATELMKIRP QTYYTTVNFV QNNWYLLTST VLHTGSLPSG
     WVWMNQELMN NENYIVDQGM KHLMTTPPVS SQLYFEMLTS LPQAMAEHFD QGDQAVVAHD
     SPGQALFSAE ETDSDFESTE DETDEVDRFD LHLSSESDDD DVENNRVTLL STLINQGMSV
     ERATRITSNA FPTRAARLRR SVYNDLLVSG LGPDAAWSHA CEQARKVGDN HDLQASGSRG
     HAE