ID   CAPSD_HASV4             Reviewed;         771 AA.
AC   Q3ZN05;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   02-JUN-2021, entry version 35.
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-4 (HAstV-4).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Mamastrovirus.
OX   NCBI_TaxID=35300;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Barthel J., Rethwilm A., Rohayem J.;
RT   "Molecular characterization of human astrovirus type 4.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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; AY720891; AAW51879.1; -; Genomic_RNA.
DR   SMR; Q3ZN05; -.
DR   Proteomes; UP000009176; 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..771
FT                   /note="Capsid polyprotein VP90"
FT                   /id="PRO_0000320234"
FT   CHAIN           1..657
FT                   /note="Capsid polyprotein VP70"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419566"
FT   CHAIN           1..313
FT                   /note="Capsid protein VP34"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419567"
FT   CHAIN           394..648
FT                   /note="Capsid protein VP27"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419568"
FT   CHAIN           424..648
FT                   /note="Capsid protein VP25"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419569"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..692
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            313..314
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            393..394
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            423..424
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            648..649
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            657..658
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   771 AA;  85125 MW;  22913EC67E88AD7D CRC64;
     MASKSDKQVT VEVNNNGRSR SKSRARSQSR GRGRSVKITV NSNNKGRRQN GRNKYQSNQR
     VRKIVNKQLR KQGVTGPKPA ICQTATATLG TIGSNTTGAT EIEACILLNP VLVKDATGST
     QFGPVQALGA QYSMWKLKYL NVRLTSMVGA SAVDGTVVRI SLNPTSTPSS TSWSGLGARK
     HLDVTVGKNA VFKLKPSDLG GPRDGWWLTN TNDNASDTLG PSIEIHTLGQ TMSSYQNTQF
     TGGLFLVGLS SAWCFTGYAA NPNLVNLVKS TDKSVDVTFE GSAGTPLIMN VPEHSHFARM
     AVEHSSLSTT LSRAGGESSS DTVWQVLNTA VSAAELVTPP PFNWLVKGGW WFVKLIAGRA
     RTGARRFYVY PSYQDALSNK PALCTGGVST YTRQSNPVRT TLQFTQMNQP SLGRGATPAT
     LGRSIPEPGD QFKVIMTVGA LVQPNRSDTQ NWLFKTVTPP TGHDAARVGW NTQHYLTIQG
     FLLIDSLEWL TPNLQESQEP PLIPELGVYI GIHKKALVYF MQQYVNPHTN NKHQVSSIFL
     IKPTENFSVT NYMSYFFRES QSDQNVANLK IRPQTWQQTV NFQRGKWYLV TNTAIRNGPP
     PSGWVWDNIE LTNESIYYAD QVLAHFINPP PQNSKIYFEV HTTMPQSRAR SIGLEEDQTD
     NWQEPDEDLQ TSTEESDYET DSLEDESDDE DSNTCRELVI NTLVNQGISR ERATYIGMSA
     YPNVEWGSGE QSTSQHIQEI SSDDVGAGAH YSCVCERKQQ SLNQGSRGHA E