ID   CAPSD_HEVUS             Reviewed;         660 AA.
AC   Q9YLQ9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   29-SEP-2021, entry version 59.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Protein ORF2;
DE            Short=pORF2;
DE   Flags: Precursor;
GN   ORFNames=ORF2;
OS   Hepatitis E virus genotype 3 (isolate Human/United States/US2) (HEV-3).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX   NCBI_TaxID=509615;
OH   NCBI_TaxID=69079; Bandicota bengalensis (lesser bandicoot rat).
OH   NCBI_TaxID=9481; Callithrix.
OH   NCBI_TaxID=9536; Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey).
OH   NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9539; Macaca (macaques).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
OH   NCBI_TaxID=9520; Saimiri (squirrel monkeys).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10092008; DOI=10.1099/0022-1317-80-3-681;
RA   Erker J.C., Desai S.M., Schlauder G.G., Dawson G.J., Mushahwar I.K.;
RT   "A hepatitis E virus variant from the United States: molecular
RT   characterization and transmission in cynomolgus macaques.";
RL   J. Gen. Virol. 80:681-690(1999).
CC   -!- FUNCTION: Major viral capsid protein that encapsidates the viral
CC       genome. Binds to the 5' end of the genomic RNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimers. Homooligomer. Self-assembles to form the capsid.
CC       The capsid is dominated by dimers that define the 30 morphological
CC       units. The unglycosylated form interacts with the phosphorylated ORF3
CC       protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC       {ECO:0000250}. Host cell surface {ECO:0000250}. Note=Initially
CC       cotranslationally translocated into the ER from where it is
CC       retrotranslocated to the cytoplasm. A fraction is also observed on the
CC       cell surface (By similarity). {ECO:0000250}.
CC   -!- PTM: Glycosylated when overexpressed in mammalian cells. In vivo, the
CC       glycosylated form is probably much less stable than the non-
CC       glycosylated form, which is present in the cytosol and represents the
CC       major product accumulated in the cell. May be present initially as a
CC       glycosylated protein in the ER, and may become unglycosylated and
CC       retrotranslocated to the cytoplasm by the endoplasmic reticulum-
CC       associated degradation (ERAD) system. The non-glycosylated form may
CC       therefore be the authentic intermediate in HEV capsid assembly (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hepevirus capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF060669; AAD15816.1; -; Genomic_DNA.
DR   SMR; Q9YLQ9; -.
DR   Proteomes; UP000007247; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR004261; SP2.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF03014; SP2; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host cytoplasm; RNA-binding; Signal;
KW   T=1 icosahedral capsid protein; Virion.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..660
FT                   /note="Capsid protein"
FT                   /id="PRO_0000334535"
FT   REGION          19..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..394
FT                   /note="particle formation"
FT                   /evidence="ECO:0000250"
FT   REGION          585..610
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   660 AA;  70965 MW;  977416EED6C046BE CRC64;
     MRPRAVLLLL FVLLPMLPAP PAGQPSGRRR GRRSGGAGGG FWGDRVDSQP FALPYIHPTN
     PFAADVVSQP GAGTRPRQPP RPLGSAWRDQ SQRPSAAPRR RSAPAGAAPL TAVSPAPDTA
     PVPDVDSRGA ILRRQYNLST SPLTSSVASG TNLVLYAAPL NPLLPLQDGT NTHIMATEAS
     NYAQYRVVRA TIRYRPLVPN AVGGYAISIS FWPQTTTTPT SVDMNSITST DVRILVQPGI
     ASELVIPSER LHYRNQGWRS VETTGVAEEE ATSGLVMLCI HGSPVNSYTN TPYTGALGLL
     DFALELEFRN LTPGNTNTRV SRYTSTARHR LRRGADGTAE LTTTAATRFM KDLHFAGTNG
     VGEVGRGIAL TLFNLADTLL GGLPTELISS AGGQLFYSRP VVSANGEPTV KLYTSVENAQ
     QDKGITIPHD IDLGDSRVVI QDYDNQHEQD RPTPSPAPSR PFSVLRANDV LWLSLTAAEY
     DQTTYGSSTN PMYVSDTVTL VNVATGAQAV ARSLDWSKVT LDGRPLTTIQ QYSKTFYVLP
     LRGKLSFWEA GTTKAGYPYN YNTTASDQIL IENAAGHRVA ISTYTTSLGA GPTSISAVGV
     LAPHSALAVL EDTIDYPARA HTFDDFCPEC RTLGLQGCAF QSTIAELQRL KMKVGKTRES