CAPSD_HEVRH
ID CAPSD_HEVRH Reviewed; 485 AA.
AC Q00270;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 29-SEP-2021, entry version 56.
DE RecName: Full=Capsid protein;
DE AltName: Full=Protein ORF2;
DE Short=pORF2;
DE Flags: Fragment;
GN ORFNames=ORF2;
OS Hepatitis E virus (isolate Rhesus/HT-4) (HEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX NCBI_TaxID=31766;
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=1584074; DOI=10.1111/j.1348-0421.1992.tb01643.x;
RA Uchida T., Suzuki K., Hayashi N., Iida F., Hara T., Oo S.S., Wang C.-K.,
RA Shikata T., Ichikawa M., Rikihisa T., Mizuno K., Win K.M.;
RT "Hepatitis E virus: cDNA cloning and expression.";
RL Microbiol. Immunol. 36:67-79(1992).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10355765; DOI=10.1099/0022-1317-80-5-1185;
RA Torresi J., Li F., Locarnini S.A., Anderson D.A.;
RT "Only the non-glycosylated fraction of hepatitis E virus capsid (open
RT reading frame 2) protein is stable in mammalian cells.";
RL J. Gen. Virol. 80:1185-1188(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; D90274; BAA20910.1; -; Genomic_RNA.
DR SMR; Q00270; -.
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:0019028; C: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 1: Evidence at protein level;
KW Capsid protein; Host cytoplasm; RNA-binding; Virion.
FT CHAIN <1..>485
FT /note="Capsid protein"
FT /id="PRO_0000100140"
FT REGION 236..262
FT /note="particle formation"
FT /evidence="ECO:0000250"
FT REGION 453..478
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 485
SQ SEQUENCE 485 AA; 52318 MW; 5A4FD9273AC74F94 CRC64;
RRQYNLSTSP LTSSVATGTN LVLYAAPLSP LLPLQDGTNT HIMATEASNY AQYRVVRATI
RYRPLVPNAV GGYAISISFW PQTTTTPTSV DMNSITSTDV RILVQPGIAS ELVIPSERLH
YRNQGWRSVE TSGVAEEEAT SGLVMLCIHG SPVNSYTNTP YTGALGLLDF ALELEFRNLT
PGNTNTRVSR YSSTARHRLR RGADGTAELT TTAATRFMKD LYFTSTNGVG EIGRGIALTL
FNLADTLLGG LPTELISSAG GQLFYSRPVV SAHGEPTVKL YTSVENAQQD KGIAIPHDID
LGESRVVIQD YDNQHEQDRP TPSPAPSRPF SVLRANDVLW LSLTAAEYDQ STYGSSTAPV
YVSDSVTLVN VATGAQAVAR SLDWTKVTLD GRPLSTIQQY PKTFFVLPLR GKLSFWEAGT
TKAGYPYNYN TTASDQLLVE NAAGHRVAIS TYTTSLGAGP VSISAVAVLA PHSALALLED
TLDYP