CAPSD_HEVCT
ID CAPSD_HEVCT Reviewed; 672 AA.
AC Q9IVZ8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 29-SEP-2021, entry version 64.
DE RecName: Full=Capsid protein;
DE AltName: Full=Protein ORF2;
DE Short=pORF2;
DE Flags: Precursor;
GN ORFNames=ORF2;
OS Hepatitis E virus genotype 4 (isolate Human/China/T1) (HEV-4) (Hepatitis E
OS virus genotype 4 (isolate Human/China/Ct1)).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX NCBI_TaxID=509627;
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=10859372; DOI=10.1099/0022-1317-81-7-1675;
RA Wang Y., Zhang H., Ling R., Li H., Harrison T.J.;
RT "The complete sequence of hepatitis E virus genotype 4 reveals an
RT alternative strategy for translation of open reading frames 2 and 3.";
RL J. Gen. Virol. 81:1675-1686(2000).
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 -!- INTERACTION:
CC Q9IVZ8; Q9IVZ8: ORF2; NbExp=3; IntAct=EBI-15794984, EBI-15794984;
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AJ272108; CAB83210.1; -; Genomic_RNA.
DR PDB; 3HAG; X-ray; 3.50 A; A=124-620.
DR PDBsum; 3HAG; -.
DR SMR; Q9IVZ8; -.
DR DIP; DIP-48927N; -.
DR ABCD; Q9IVZ8; 1 sequenced antibody.
DR EvolutionaryTrace; Q9IVZ8; -.
DR Proteomes; UP000007242; 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:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Capsid protein; Host cytoplasm; RNA-binding; Signal;
KW T=1 icosahedral capsid protein; Virion.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..672
FT /note="Capsid protein"
FT /id="PRO_0000334537"
FT REGION 76..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..406
FT /note="particle formation"
FT /evidence="ECO:0000250"
FT REGION 597..622
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 194..208
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:3HAG"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 307..320
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 447..456
FT /evidence="ECO:0007829|PDB:3HAG"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 482..493
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 504..513
FT /evidence="ECO:0007829|PDB:3HAG"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:3HAG"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:3HAG"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 551..555
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 558..564
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:3HAG"
FT STRAND 607..613
FT /evidence="ECO:0007829|PDB:3HAG"
SQ SEQUENCE 672 AA; 72316 MW; EA2DDFF295375AAD CRC64;
MNNMFFCSVH GDATMRSRAL LFLLFVLLPM LPAPPAGQPS GRRRGQAGCG GGFWGDRVDS
QPFALPYIHP TNPFASDIPA AAGTGARPRQ PIRPLGSAWR DQSQRPAAST RRRPAPAGAS
PLTAVAPAPD TAPVPDADSR GAILRRQYNL STSPLTSTIA TGTNFVLYAA PLSPLLPLQD
GTNTHIMATE ASNYAQYRVV RATIRYRPLV PNAVGGYAIS ISFWPQTTTT PTSVDMNSIT
STDVRILVQP GIASELVTPS ERLHYRNQGW RSVETSGVAE EEATSGLVML CIHGSPVNSY
TNTPYTGALG LLDFALELEF RNLTPGNTNT RVSRYSSSAR HKLRRGPDGT AELTTTAATR
FMKDLHFTGT NGVGEVGRGI ALTLFNLADT LLGGLPTELI SSAGGQLFYS RPVVSANGEL
TVKLYTSVEN AQQDKGVAIP HDIDLGESRV VIQDYDNQHE QDRPTPSPAP SRPFSVLRAN
DVLWLSLTAA EYDQTTYGSS TNPMYVSDTV TFVNVATGAQ GVSRSLDWSK VTLDGRPLTT
IQQYSKTFYV LPLRGKLSFW EAGTTKAGYP YNYNTTASDQ ILIENAAGHR VCISTYTTNL
GSGPVSVSAV GVLAPHSALA ALEDTADYPA RAHTFDDFCP ECRALGLQGC AFQSTVGELQ
RLKMKVGKTR EY
