CAPSD_HASV8
ID CAPSD_HASV8 Reviewed; 782 AA.
AC Q9IFX1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 57.
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-8 (HAstV-8).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=43358;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11086120; DOI=10.1099/0022-1317-81-12-2891;
RA Mendez-Toss M., Romero-Guido P., Munguia M.E., Mendez E., Arias C.F.;
RT "Molecular analysis of a serotype 8 human astrovirus genome.";
RL J. Gen. Virol. 81:2891-2897(2000).
RN [2]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=15280469; DOI=10.1128/jvi.78.16.8601-8608.2004;
RA Mendez E., Salas-Ocampo E., Arias C.F.;
RT "Caspases mediate processing of the capsid precursor and cell release of
RT human astroviruses.";
RL J. Virol. 78:8601-8608(2004).
RN [3]
RP CLEAVAGE BY HOST CASPASES.
RX PubMed=20347468; DOI=10.1016/j.virol.2010.02.028;
RA Banos-Lara Mdel R., Mendez E.;
RT "Role of individual caspases induced by astrovirus on the processing of its
RT structural protein and its release from the cell through a non-lytic
RT mechanism.";
RL Virology 401:322-332(2010).
RN [4]
RP FUNCTION.
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).
RN [5]
RP FUNCTION.
RX PubMed=24335315; DOI=10.1128/jvi.02908-13;
RA Mendez E., Munoz-Yanez C., Sanchez-San Martin C., Aguirre-Crespo G.,
RA Banos-Lara Mdel R., Gutierrez M., Espinosa R., Acevedo Y., Arias C.F.,
RA Lopez S.;
RT "Characterization of human astrovirus cell entry.";
RL J. Virol. 88:2452-2460(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 415-646, AND FUNCTION.
RX PubMed=21768348; DOI=10.1073/pnas.1104834108;
RA Dong J., Dong L., Mendez E., Tao Y.;
RT "Crystal structure of the human astrovirus capsid spike.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12681-12686(2011).
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. {ECO:0000269|PubMed:21768348, ECO:0000269|PubMed:22743104,
CC ECO:0000269|PubMed:24335315}.
CC -!- INTERACTION:
CC Q9IFX1; Q9IFX1: ORF2; NbExp=2; IntAct=EBI-15936945, EBI-15936945;
CC -!- SUBCELLULAR LOCATION: Virion.
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:15280469, ECO:0000305|PubMed:20347468}.
CC -!- SIMILARITY: Belongs to the astroviridae capsid polyprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF85964.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF260508; AAF85964.1; ALT_INIT; Genomic_RNA.
DR PDB; 3QSQ; X-ray; 1.80 A; A=415-646.
DR PDB; 5IBV; X-ray; 2.15 A; A=71-415.
DR PDB; 7RK1; X-ray; 2.05 A; A/B=429-647.
DR PDB; 7RK2; X-ray; 2.65 A; A/B=429-647.
DR PDBsum; 3QSQ; -.
DR PDBsum; 5IBV; -.
DR PDBsum; 7RK1; -.
DR PDBsum; 7RK2; -.
DR SMR; Q9IFX1; -.
DR DIP; DIP-59696N; -.
DR PRIDE; Q9IFX1; -.
DR ABCD; Q9IFX1; 2 sequenced antibodies.
DR Proteomes; UP000008629; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IDA: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..782
FT /note="Capsid polyprotein VP90"
FT /id="PRO_0000320238"
FT CHAIN 1..658
FT /note="Capsid polyprotein VP70"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419582"
FT CHAIN 1..313
FT /note="Capsid protein VP34"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419583"
FT CHAIN 394..648
FT /note="Capsid protein VP27"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419584"
FT CHAIN 424..648
FT /note="Capsid protein VP25"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419585"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..702
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 662..683
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 658..659
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT STRAND 80..93
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:5IBV"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:5IBV"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 132..148
FT /evidence="ECO:0007829|PDB:5IBV"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:5IBV"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:5IBV"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:5IBV"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:5IBV"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 242..258
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:5IBV"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5IBV"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 318..328
FT /evidence="ECO:0007829|PDB:5IBV"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:5IBV"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 362..372
FT /evidence="ECO:0007829|PDB:5IBV"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:5IBV"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 480..491
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 513..529
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 532..545
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 547..554
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:7RK1"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 576..582
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 587..599
FT /evidence="ECO:0007829|PDB:3QSQ"
FT TURN 621..625
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:3QSQ"
FT STRAND 635..643
FT /evidence="ECO:0007829|PDB:3QSQ"
SQ SEQUENCE 782 AA; 85731 MW; E97276C37CDB0FE0 CRC64;
MASKSDKQVT VEVNNNGRSR SKSRARSQSR GRGRSVKITV NSHNKGRRQN GRNKYQSNQR
VRKIVNKQLR KQGVTGPKPA ICQTATATLG TIGSNTTGAT EIEACILLNP VLVKDATGST
QFGPVQALGA QYSMWKLKYL NVRLTSMVGA SAVNGTVVRI SLNPTSTPSS TSWSGLGARK
HLDVTVGKNA VFKLKPSDLG GPRDGWWLTN TNDNASDTLG PSIEIHTLGQ TMSSYQNTQF
TGGLFLVELS SAWCFTGYAA NPNLVNLVKS TDKSVNVTFE GSAGTPLIMN VPEHSHFART
AVEHSSLSTS LSRAGGESSS DTVWQVLNTA VSAAELVTPP PFNWLVKGGW WFVKLIAGRA
RTGARRFYVY LSYQDALSNK PALCTGGVPA SARQSNPVRT TLQFTQMNQP SLGHGATPMT
FGRSIPEPGE QFRVLLTVGP PMAPNTANSQ NWVNKTIVPP ENQYTVKIGI DLEHYTTMQG
FTPVESVSWY TADFQPSDEP SPIPGLYARV NNTKKADVYG VQQFKSSHTN NRHQITSVFL
VRVTTSFQVI NYTSYFIRGA ESGSNVSNLK IRDQTYHTPL QFTQGKWYLL TSTVMHDGPT
SSGWVWMNQE LTNNIAYRVD PGMMYLITPP PAASQLYFEL HTVLPQARSE EPETYVDAPL
PEEPPIEEEE TDSDFESTED ENDEVDRFDL HPSSESDDDD VENDRATLLS TLLNQGISVE
RATRITNGAF PTRAARVRRS VYNDLLVSGL SPGAAWSHAC EQARRAGDNH DLQLSGSRDH
AE
