CAPSD_HASV6
ID CAPSD_HASV6 Reviewed; 778 AA.
AC Q67815;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 62.
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-6 (HAstV-6).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=37130;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8119358; DOI=10.1017/s0950268800057551;
RA Lee T.W., Kurtz J.B.;
RT "Prevalence of human astrovirus serotypes in the Oxford region 1976-92,
RT with evidence for two new serotypes.";
RL Epidemiol. Infect. 112:187-193(1994).
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; Z46658; CAA86616.1; -; Genomic_RNA.
DR SMR; Q67815; -.
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.
DR PROSITE; PS00018; EF_HAND_1; 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..778
FT /note="Capsid polyprotein VP90"
FT /id="PRO_0000320236"
FT CHAIN 1..655
FT /note="Capsid polyprotein VP70"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419574"
FT CHAIN 1..313
FT /note="Capsid protein VP34"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419575"
FT CHAIN 394..646
FT /note="Capsid protein VP27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419576"
FT CHAIN 424..646
FT /note="Capsid protein VP25"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419577"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..689
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..47
FT /note="Polar 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 646..647
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 655..656
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 778 AA; 85264 MW; CD9D5017A8AF8935 CRC64;
MASKSDKQVT VEVNNTGRGR SKSRARSQSR GRGRSVKITV NSQNKGRRQN GRNKRQSNQR
VRNIVNKQLR KQGVTGPKPA ICQKATATLG TIGSNTSGTT EIEACILLNP VLVEDATGST
QFGPVQALGA QYSMWKLKYL NVRLTSMVGA SAVNGTVVRV SLNPTSTPSS TSWSGLGARK
HLDVTVGKNA IFKLKPSDLG GPRDGWWLTN TNDNASDTLG PSVEIHTLGR TMSSYQNQQF
TGGLFLVELA SEWCFTGYAA NPNLVNLVKS TDKQVNVTFE GSAGTPLVMN VPAASHFART
VAQRSTLPTS MARAGENTAS DTVWQVLNTA VSAAELVTPP PFNWLVKGGW WFVKLIAGRV
RNGNRSFYVY ASYQDALSNK PALCTGSTSG SMRTRPAVMT TLQFTQMNQP SLGHGETPAT
LGRSIPTSGE TLKVLLTVGN PISPNETNKQ TWVNKTIEPP GAVVRIGRDT QHYCTLNGFT
LITKVDWFTE EFQPSEEPAP VQGLMVLGDN HKKADVYAAQ QYKNPITNDK QEVTSVFLVR
VNEGFQVTNH LSYFYRNSVN TDAVENIKIR SATRHTTVRF YQGSWYLLTS TVLHTGPPVS
GWLWMNQELQ NDQAYIIDQG IMHLITPPPV SSQIYFEMAT LVPQTRSGGG ETGLELVMGL
SDDEYPISHV NDEEETEYET ESDEDETDEV DRFDLCCTSD SEDDIENNRV TLLSTLINQG
VTVDRATMIT NRAFPTPNYK PRREPSNDLL APSDCLATAR SHACNETCQL SGSRGHAE
