CAPSD_HASV1
ID CAPSD_HASV1 Reviewed; 786 AA.
AC O12792; O12498; Q67725;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 02-JUN-2021, entry version 64.
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-1 (HAstV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=12456;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8293952; DOI=10.1111/j.1574-6968.1993.tb06542.x;
RA Willcocks M.M., Carter M.J.;
RT "Identification and sequence determination of the capsid protein gene of
RT human astrovirus serotype 1.";
RL FEMS Microbiol. Lett. 114:1-7(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8021608; DOI=10.1099/0022-1317-75-7-1785;
RA Willcocks M.M., Brown T.D., Madeley C.R., Carter M.J.;
RT "The complete sequence of a human astrovirus.";
RL J. Gen. Virol. 75:1785-1788(1994).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=22743104; DOI=10.1016/j.jmb.2012.06.029;
RA Dryden K.A., Tihova M., Nowotny N., Matsui S.M., Mendez E., Yeager M.;
RT "Immature and mature human astrovirus: structure, conformational changes,
RT and similarities to hepatitis E virus.";
RL J. Mol. Biol. 422:650-658(2012).
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 (PubMed:22743104). Plays a role in the attachment to target
CC host cell. This attachment induces virion internalization through
CC clathrin-dependent endocytosis (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:22743104}.
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 (Probable).
CC {ECO:0000305|PubMed:22743104}.
CC -!- SIMILARITY: Belongs to the astroviridae capsid polyprotein family.
CC {ECO:0000305}.
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DR EMBL; S68561; AAC60723.1; -; Genomic_RNA.
DR EMBL; Z25771; CAA81032.1; -; Genomic_RNA.
DR SMR; O12792; -.
DR PRIDE; O12792; -.
DR Proteomes; UP000001650; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IDA: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 1: Evidence at protein level;
KW Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW Reference proteome; T=3 icosahedral capsid protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..786
FT /note="Capsid polyprotein VP90"
FT /id="PRO_0000320231"
FT CHAIN 1..657
FT /note="Capsid polyprotein VP70"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419554"
FT CHAIN 1..313
FT /note="Capsid protein VP34"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419555"
FT CHAIN 394..648
FT /note="Capsid protein VP27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419556"
FT CHAIN 424..648
FT /note="Capsid protein VP25"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419557"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..668
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 26..40
FT /note="Basic and 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 786 AA; 85539 MW; E412F643B2B5A4A0 CRC64;
MASKSNKQVT VEVSNNGRSR SKSRARSQSR GRDKSVKITV NSRNRARRQP GRDKRQSSQR
VRNIVNKQLR KQGVTGPKPA ICQRATATLG TVGSNTSGTT EIEACILLNP VLVKDATGST
QFGPVQALGA QYSMWKLKYL NVKLTSMVGA SAVNGTVSGV SLNPTTTPTS TSWSGLGARK
HLDVTVGKNA TFKLKPSDLG GPRDGWWLTN TNDNASDTLG PSIEIHTLGR TMSSYKNEQF
TGGLFLVELA SEWCFTGYAA NPNLVNLVKS TDNQVSVTFE GSAGSPLIMN VPEGSHFART
VLARSTTPTT LARAGERTTS DTVWQVLNTA VSAAELVTPP PFNWLVKGGW WFVKLIAGRT
RTGSRSFYVY PSYQDALSNK PALCTGSTPG GMRTRNPVTT TLQFTQMNQP SLGHGEAPAA
FGRSIPAPGE EFKVVLTFGA PMSPNANNKQ TWVNKPLDAP SGHYNVKIAK DVDHYLTMQG
FTSIASVDWY TIDFQPSEAP APIQGLQVLV NSSKKADVYA IKQFVTAQTN NKHQVTSLFL
VKVTTGFQVN NYLSYFYRAS ATGDATTNLL VRGDTYTAGI SFTQGGWYLL TNTSIVDGAM
PPGWVWNNVE LKTNTAYHMD KGLVHLIMPL PESTQMCYEM LTSIPRSRAS GHGYESDNTE
YLDAPDSADQ FKEDIETDTD IESTEDEDEA DRFDIIDTSD EEDENETDRV TLLSTLVNQG
MTMTRATRIA RRAFPTLSDR IKRGVYMDLL VSGASPGNAW SHACEEARKA AGEINPCTSG
SRGHAE
