ID   CAPSD_HASV3             Reviewed;         794 AA.
AC   Q9WFZ0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 46.
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-3 (HAstV-3).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Mamastrovirus.
OX   NCBI_TaxID=35740;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Monroe S.S., Stine S.E.;
RL   Submitted (DEC-1998) 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; AF117209; AAD17224.1; -; Genomic_RNA.
DR   SMR; Q9WFZ0; -.
DR   PRIDE; Q9WFZ0; -.
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..794
FT                   /note="Capsid polyprotein VP90"
FT                   /id="PRO_0000320233"
FT   CHAIN           1..661
FT                   /note="Capsid polyprotein VP70"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419562"
FT   CHAIN           1..315
FT                   /note="Capsid protein VP34"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419563"
FT   CHAIN           396..649
FT                   /note="Capsid protein VP27"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419564"
FT   CHAIN           426..649
FT                   /note="Capsid protein VP25"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419565"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..697
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..715
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            315..316
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            395..396
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            425..426
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            649..650
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            661..662
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   794 AA;  87096 MW;  B0EEFF372FAEDEE2 CRC64;
     MASKSDKQVT VEVKNNNNGR NRSRSRARSQ SRGRGKSVKI TVNSRSRGRR QNGRDKYQSN
     QRVRNIVTKQ LRKQGVTGPK PAICQRATAT LGTIGSNTSG TTEIEACILL NPVLVKDATG
     STQFGPVQAL GAQYSMWKLK YLNVKLTSMV GASAVNGTVV RVSLNPTSTP SSTSWSGLGA
     RKHLDVTVGK NAVFKLKPAD LGGPRDGWWL TNTNDNASDT LGPSVEIHTL GMTMSSYKNE
     QFTGGLFLVE LASEWCFTGY AANPNLVNLE KSTDKQVNVT FEGSNGTPLI MKVPEASHFA
     RTAVARSSLP TTLARAGQNT TSDTVWQVLN TAVSAAELVT PPPFNWLVKG GWWFVKLIAG
     RARTGTRSFY VYPSYQDALS NKPALCTGSA PSGMRSRAAV MTTLQFTQMN QPSLGHGEMT
     ATLGRAIPSP GDTFNVVLTI GQPLAPNTLT KQSWLNKTTV SPQNHHVVKI AKDVNNYTTM
     QGFTPISSVD WYTTDFQPSE EPTPIPGLQV LVNSSKKADV YAIQQYLNNQ TNNKVQLTSI
     FLVKVTTSFQ VNNYLSYFYR SYGTGTTVEN LKVRSDTTAQ DVNFPVGWYL MTNTAIFNAP
     APPGWIWQNV ELLNDTAYLI DQGMMHLIMP PPANTQLLFE MRTSVTGSRS MISSEEPDTH
     EPGDEWCDAL DASDSRVFLE ETDYEDEEDE DEDDEADRFD LHSSYGSEPE DDDENNRVTL
     LSTLINQGMT VERATRITKR AFPTSADKTK RSVYMDLLAS GLSPGNAWSH ACEEARIMGT
     NQMPNVSGDR GHAE