ID   CAPSD_HEVME             Reviewed;         659 AA.
AC   Q03500;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   29-SEP-2021, entry version 67.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Protein ORF2;
DE            Short=pORF2;
DE   Flags: Precursor;
GN   ORFNames=ORF2;
OS   Hepatitis E virus genotype 2 (isolate Human/Mexico) (HEV-2).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX   NCBI_TaxID=31768;
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=9031; Gallus gallus (Chicken).
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 RNA].
RX   PubMed=1448913; DOI=10.1016/0042-6822(92)90230-m;
RA   Huang C.C., Nguyen D., Fernandez J., Yun K.Y., Fry K.E., Bradley D.W.,
RA   Tam A.W., Reyes G.R.;
RT   "Molecular cloning and sequencing of the Mexico isolate of hepatitis E
RT   virus (HEV).";
RL   Virology 191:550-558(1992).
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; M74506; AAA45732.1; -; Genomic_RNA.
DR   PIR; B44212; B44212.
DR   SMR; Q03500; -.
DR   Proteomes; UP000007245; 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; 2.
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..659
FT                   /note="Capsid protein"
FT                   /id="PRO_0000036996"
FT   REGION          19..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..393
FT                   /note="particle formation"
FT                   /evidence="ECO:0000250"
FT   REGION          584..609
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   659 AA;  70641 MW;  CF75E75EFD8FBE2C CRC64;
     MRPRPLLLLF LLFLPMLPAP PTGQPSGRRR GRRSGGTGGG FWGDRVDSQP FAIPYIHPTN
     PFAPDVAAAS GSGPRLRQPA RPLGSTWRDQ AQRPSAASRR RPATAGAAAL TAVAPAHDTS
     PVPDVDSRGA ILRRQYNLST SPLTSSVASG TNLVLYAAPL NPPLPLQDGT NTHIMATEAS
     NYAQYRVARA TIRYRPLVPN AVGGYAISIS FWPQTTTTPT SVDMNSITST DVRILVQPGI
     ASELVIPSER LHYRNQGWRS VETSGVAEEE ATSGLVMLCI HGSPVNSYTN TPYTGALGLL
     DFALELEFRN LTTCNTNTRV SRYSSTARHS ARGADGTAEL TTTAATRFMK DLHFTGLNGV
     GEVGRGIALT LLNLADTLLG GLPTELISSA GGQLFYSRPV VSANGEPTVK LYTSVENAQQ
     DKGVAIPHDI DLGDSRVVIQ DYDNQHEQDR PTPSPAPSRP FSVLRANDVL WLSLTAAEYD
     QSTYGSSTGP VYISDSVTLV NVATGAQAVA RSLDWSKVTL DGRPLPTVEQ YSKTFFVLPL
     RGKLSFWEAG TTKAGYPYNY NTTASDQILI ENAAGHRVAI STYTTRLGAG PVAISAAAVL
     APRSALALLE DTFDYPGRAH TFDDFCPECR ALGLQGCAFQ STVAELQRLK VKVGKTREL