CAPSD_HEVBU
ID CAPSD_HEVBU Reviewed; 660 AA.
AC P29326;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 29-SEP-2021, entry version 80.
DE RecName: Full=Secreted protein ORF2;
DE AltName: Full=Protein ORF2;
DE Short=pORF2;
GN ORFNames=ORF2;
OS Hepatitis E virus genotype 1 (isolate Human/Burma) (HEV-1).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX NCBI_TaxID=31767;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1926770; DOI=10.1016/0042-6822(91)90760-9;
RA Tam A.W., Smith M.M., Guerra M.E., Huang C.-C., Bradley D.W., Fry K.E.,
RA Reyes G.R.;
RT "Hepatitis E virus (HEV): molecular cloning and sequencing of the full-
RT length viral genome.";
RL Virology 185:120-131(1991).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CAPSID SHELL, AND SUBUNIT (ISOFORM
RP CAPSID PROTEIN ORF2).
RX PubMed=10603315; DOI=10.1006/viro.1999.0005;
RA Xing L., Kato K., Li T., Takeda N., Miyamura T., Hammar L., Cheng R.H.;
RT "Recombinant hepatitis E capsid protein self-assembles into a dual-domain T
RT = 1 particle presenting native virus epitopes.";
RL Virology 265:35-45(1999).
RN [3]
RP FUNCTION (ISOFORM CAPSID PROTEIN ORF2), AND RNA-BINDING (ISOFORM CAPSID
RP PROTEIN ORF2).
RX PubMed=14671114; DOI=10.1128/jvi.78.1.320-328.2004;
RA Surjit M., Jameel S., Lal S.K.;
RT "The ORF2 protein of hepatitis E virus binds the 5' region of viral RNA.";
RL J. Virol. 78:320-328(2004).
RN [4]
RP FUNCTION (ISOFORM CAPSID PROTEIN ORF2), REGION OF DIMERIZATION (ISOFORM
RP CAPSID PROTEIN ORF2), AND MUTAGENESIS OF ALA-597; VAL-598; ALA-599; LEU-601
RP AND ALA-602.
RX PubMed=15557331; DOI=10.1074/jbc.m410361200;
RA Li S.-W., Zhang J., He Z.-Q., Gu Y., Liu R.-S., Lin J., Chen Y.-X.,
RA Ng M.H., Xia N.-S.;
RT "Mutational analysis of essential interactions involved in the assembly of
RT hepatitis E virus capsid.";
RL J. Biol. Chem. 280:3400-3406(2005).
CC -!- FUNCTION: [Isoform Secreted protein ORF2]: Plays a role in the
CC inhibition of host antibody-mediated neutralization without blocking
CC viral cell entry. {ECO:0000250|UniProtKB:Q81871}.
CC -!- FUNCTION: [Isoform Capsid protein ORF2]: Forms an icosahedral capsid
CC with a T=1 symmetry and a 34 nm diameter. The capsid is composed of 60
CC copies linked to each other. Binds to the 5' end of the genomic RNA to
CC mediate genome encapsidation (PubMed:14671114, PubMed:15557331). Binds
CC to heparin surface proteoglycans (HSPGs) to mediate viral entry.
CC Additionally, the interactions with host ASGR1 and ASGR2 facilitate
CC viral infection of hepatocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q81871, ECO:0000269|PubMed:14671114,
CC ECO:0000269|PubMed:15557331}.
CC -!- SUBUNIT: [Isoform Secreted protein ORF2]: Homodimers.
CC {ECO:0000250|UniProtKB:Q68985}.
CC -!- SUBUNIT: [Isoform Capsid protein ORF2]: Self-assembles to form the
CC capsid. The capsid is dominated by dimers that define the 30
CC morphological units. Interacts with phosphorylated protein ORF3 (By
CC similarity). Interacts with host TMEM134. Interacts with host ASGR1 and
CC ASGR2; these interactions facilitate infection of host hepatocytes (By
CC similarity). {ECO:0000250|UniProtKB:Q81871}.
CC -!- SUBCELLULAR LOCATION: [Isoform Secreted protein ORF2]: Secreted
CC {ECO:0000250|UniProtKB:Q81871}.
CC -!- SUBCELLULAR LOCATION: [Isoform Capsid protein ORF2]: Virion
CC {ECO:0000250|UniProtKB:Q81871}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q81871}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q81871}. Host Golgi apparatus
CC {ECO:0000250|UniProtKB:Q81871}. Host cell surface
CC {ECO:0000250|UniProtKB:Q68985}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Secreted protein ORF2;
CC IsoId=P29326-1; Sequence=Displayed;
CC Name=Capsid protein ORF2;
CC IsoId=P29326-2; Sequence=VSP_059885;
CC -!- PTM: [Isoform Secreted protein ORF2]: Exists as a glycosylated dimer.
CC {ECO:0000250|UniProtKB:Q81871}.
CC -!- SIMILARITY: Belongs to the hepevirus capsid protein family.
CC {ECO:0000305}.
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DR EMBL; M73218; AAA45736.1; -; Genomic_RNA.
DR PIR; C40778; VHWWH2.
DR PDB; 2ZZQ; X-ray; 3.81 A; A=112-608.
DR PDBsum; 2ZZQ; -.
DR SMR; P29326; -.
DR ABCD; P29326; 1 sequenced antibody.
DR Proteomes; UP000007243; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; 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 GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; Alternative initiation; Capsid protein; Glycoprotein;
KW Host cytoplasm; Host endoplasmic reticulum; Host Golgi apparatus;
KW Host-virus interaction; RNA-binding; Secreted;
KW T=1 icosahedral capsid protein; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Virion;
KW Virus entry into host cell.
FT CHAIN 1..660
FT /note="Secreted protein ORF2"
FT /id="PRO_0000445485"
FT REGION 18..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..394
FT /note="particle formation"
FT REGION 585..610
FT /note="Oligomerization"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q81871"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q81871"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q81871"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform Capsid protein ORF2)"
FT /id="VSP_059885"
FT MUTAGEN 597
FT /note="A->E: Complete loss of dimeric interactions."
FT /evidence="ECO:0000269|PubMed:15557331"
FT MUTAGEN 598
FT /note="V->E: Complete loss of dimeric interactions."
FT /evidence="ECO:0000269|PubMed:15557331"
FT MUTAGEN 599
FT /note="A->E: Complete loss of dimeric interactions."
FT /evidence="ECO:0000269|PubMed:15557331"
FT MUTAGEN 600
FT /note="V->E: Decreased amount of dimeric form."
FT MUTAGEN 601
FT /note="L->E: Complete loss of dimeric interactions."
FT /evidence="ECO:0000269|PubMed:15557331"
FT MUTAGEN 602
FT /note="A->E: Complete loss of dimeric interactions."
FT /evidence="ECO:0000269|PubMed:15557331"
SQ SEQUENCE 660 AA; 70978 MW; 5832A013CCC4A61C CRC64;
MRPRPILLLL LMFLPMLPAP PPGQPSGRRR GRRSGGSGGG FWGDRVDSQP FAIPYIHPTN
PFAPDVTAAA GAGPRVRQPA RPLGSAWRDQ AQRPAVASRR RPTTAGAAPL TAVAPAHDTP
PVPDVDSRGA ILRRQYNLST SPLTSSVATG TNLVLYAAPL SPLLPLQDGT NTHIMATEAS
NYAQYRVARA TIRYRPLVPN AVGGYAISIS FWPQTTTTPT SVDMNSITST DVRILVQPGI
ASELVIPSER LHYRNQGWRS VETSGVAEEE ATSGLVMLCI HGSLVNSYTN TPYTGALGLL
DFALELEFRN LTPGNTNTRV SRYSSTARHR LRRGADGTAE LTTTAATRFM KDLYFTSTNG
VGEIGRGIAL TLFNLADTLL GGLPTELISS AGGQLFYSRP VVSANGEPTV KLYTSVENAQ
QDKGIAIPHD IDLGESRVVI QDYDNQHEQD RPTPSPAPSR PFSVLRANDV LWLSLTAAEY
DQSTYGSSTG PVYVSDSVTL VNVATGAQAV ARSLDWTKVT LDGRPLSTIQ QYSKTFFVLP
LRGKLSFWEA GTTKAGYPYN YNTTASDQLL VENAAGHRVA ISTYTTSLGA GPVSISAVAV
LAPHSALALL EDTLDYPARA HTFDDFCPEC RPLGLQGCAF QSTVAELQRL KMKVGKTREL
