CAPSD_HASV2
ID CAPSD_HASV2 Reviewed; 796 AA.
AC Q82446;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 54.
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-2 (HAstV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=12701;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8497068; DOI=10.1128/jvi.67.6.3611-3614.1993;
RA Monroe S.S., Jiang B., Stine S.E., Koopmans M., Glass R.I.;
RT "Subgenomic RNA sequence of human astrovirus supports classification of
RT Astroviridae as a new family of RNA viruses.";
RL J. Virol. 67:3611-3614(1993).
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; L06802; AAA62427.1; -; mRNA.
DR PIR; A45695; A45695.
DR PDB; 5KOU; X-ray; 1.87 A; A/B/C/D=429-644.
DR PDB; 5KOV; X-ray; 3.25 A; A/B/G/H/M/N/S/T=429-644.
DR PDBsum; 5KOU; -.
DR PDBsum; 5KOV; -.
DR SMR; Q82446; -.
DR PRIDE; Q82446; -.
DR ABCD; Q82446; 1 sequenced antibody.
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 1: Evidence at protein level;
KW 3D-structure; Capsid protein;
KW 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..796
FT /note="Capsid polyprotein VP90"
FT /id="PRO_0000320232"
FT CHAIN 1..659
FT /note="Capsid polyprotein VP70"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419558"
FT CHAIN 1..313
FT /note="Capsid protein VP34"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419559"
FT CHAIN 395..650
FT /note="Capsid protein VP27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419560"
FT CHAIN 423..650
FT /note="Capsid protein VP25"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419561"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..718
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 644..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..699
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..717
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 394..395
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 422..423
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 650..651
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 659..660
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:5KOU"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 482..492
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 515..530
FT /evidence="ECO:0007829|PDB:5KOU"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 534..547
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 589..601
FT /evidence="ECO:0007829|PDB:5KOU"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:5KOU"
FT STRAND 637..643
FT /evidence="ECO:0007829|PDB:5KOU"
SQ SEQUENCE 796 AA; 87839 MW; 36DD1A65203C444C CRC64;
MASKSDKQVT VEVNNNGRNR SKSRARSQSR GRGRSVKITV NSHNKGRRQN GRNKYQSNQR
VRKIVNKQLR KQGVTGPKPA ICQRATATLG TIGTNTTGAT EIEACILLNP VLVKDATGST
QFGPVQALGA QYSMWKLKYL NVKLTSMVGA SAVNGTVLRI SLNPTSTPSS TSWSGLGARK
HMDVTVGRNA VFKLRPSDLG GPRDGWWLTN TNDNASDTLG PSIEIHTLGK TMSSYKNEQF
TGGLFLVELA SEWCFTGYAA NPNLVNLVKS TDHEVNVTFE GSKGTPLIMN VAEHSHFARM
AEQHSSISTT FSRAGGDATS DTVWQVLNTA VSAAELVAPP PFNWLIKGGW WFVKLIAGRT
RTGTKQFYVY PSYQDALSNK PALCTGGVTG GVLRTTPVTT LQFTQMNQPS LGHGEHTATI
GSIVQDPSGE LRVLLTVGSI MSPNSADRQV WLNKTLTAPG TNSNDNLVKI AHDLGHYLIM
QGFMHIKTVE WYTPDFQPSR DPTPIAGMSV MVNITKKADV YFMKQFKNSY TNNRHQITSI
FLIKPLADFK VQCYMSYFKR ESHDNDGVAN LTVRSMTSPE TIRFQVGEWY LLTSTTLKEN
NLPEGWVWDR VELKSDTPYY ADQALTYFIT PPPVDSQILF EGNTTLPRIS SPPDNPSGRY
MESHQQDCDS SDDEDDCENV SEETETEDEE DEDEDDEADR FDLHSPYSSE PEDSDENNRV
TLLSTLINQG MTVERATRIT KRAFPTCAEK LKRSVYMDLL ASGASPSSAW SNACDEARNV
GSNQLAKLSG DRGHAE
