CAPSD_HEVHY
ID CAPSD_HEVHY Reviewed; 660 AA.
AC Q68985;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 74.
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/India/Hyderabad) (HEV-1).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX NCBI_TaxID=512346;
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 RNA].
RX PubMed=8567900; DOI=10.1128/jcm.33.10.2653-2659.1995;
RA Panda S.K., Nanda S.K., Zafrullah M., Ansari I.H., Ozdener M.H., Jameel S.;
RT "An Indian strain of hepatitis E virus (HEV): cloning, sequence, and
RT expression of structural region and antibody responses in sera from
RT individuals from an area of high-level HEV endemicity.";
RL J. Clin. Microbiol. 33:2653-2659(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone pSGI-HEV;
RX PubMed=10666275; DOI=10.1128/jvi.74.5.2430-2437.2000;
RA Panda S.K., Ansari I.H., Durgapal H., Agrawal S., Jameel S.;
RT "The in vitro-synthesized RNA from a cDNA clone of hepatitis E virus is
RT infectious.";
RL J. Virol. 74:2430-2437(2000).
RN [3]
RP SUBUNIT (ISOFORM SECRETED PROTEIN ORF2), GLYCOSYLATION (ISOFORM SECRETED
RP PROTEIN ORF2), AND SUBCELLULAR LOCATION (ISOFORM CAPSID PROTEIN ORF2).
RX PubMed=8523527; DOI=10.1128/jvi.70.1.207-216.1996;
RA Jameel S., Zafrullah M., Ozdener M.H., Panda S.K.;
RT "Expression in animal cells and characterization of the hepatitis E virus
RT structural proteins.";
RL J. Virol. 70:207-216(1996).
RN [4]
RP GLYCOSYLATION AT ASN-137 AND ASN-562 (ISOFORM SECRETED PROTEIN ORF2),
RP MUTAGENESIS OF ASN-137; ASN-310 AND ASN-562, AND SUBCELLULAR LOCATION
RP (ISOFORM CAPSID PROTEIN ORF2).
RX PubMed=10196303; DOI=10.1128/jvi.73.5.4074-4082.1999;
RA Zafrullah M., Ozdener M.H., Kumar R., Panda S.K., Jameel S.;
RT "Mutational analysis of glycosylation, membrane translocation, and cell
RT surface expression of the hepatitis E virus ORF2 protein.";
RL J. Virol. 73:4074-4082(1999).
RN [5]
RP SUBUNIT (ISOFORM CAPSID PROTEIN ORF2), AND REGION OF OLIGOMERIZATION
RP (ISOFORM CAPSID PROTEIN ORF2).
RX PubMed=12488605; DOI=10.1155/s1110724301000262;
RA Xiaofang L., Zafrullah M., Ahmad F., Jameel S.;
RT "A C-terminal hydrophobic region is required for homo-oligomerization of
RT the Hepatitis E virus capsid (ORF2) protein.";
RL J. Biomed. Biotechnol. 1:122-128(2001).
RN [6]
RP INTERACTION WITH PROTEIN ORF3 (ISOFORM CAPSID PROTEIN ORF2), AND
RP SUBCELLULAR LOCATION (ISOFORM CAPSID PROTEIN ORF2).
RX PubMed=11934888; DOI=10.1074/jbc.m200185200;
RA Tyagi S., Korkaya H., Zafrullah M., Jameel S., Lal S.K.;
RT "The phosphorylated form of the ORF3 protein of hepatitis E virus interacts
RT with its non-glycosylated form of the major capsid protein, ORF2.";
RL J. Biol. Chem. 277:22759-22767(2002).
RN [7]
RP SUBCELLULAR LOCATION (ISOFORM CAPSID PROTEIN ORF2).
RC STRAIN=Infectious clone pSGI-HEV;
RX PubMed=17229684; DOI=10.1128/jvi.02039-06;
RA Surjit M., Jameel S., Lal S.K.;
RT "Cytoplasmic localization of the ORF2 protein of hepatitis E virus is
RT dependent on its ability to undergo retrotranslocation from the endoplasmic
RT reticulum.";
RL J. Virol. 81:3339-3345(2007).
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 (By similarity). Binds to heparin surface
CC proteoglycans (HSPGs) to mediate viral entry. Additionally, the
CC interactions with host ASGR1 and ASGR2 facilitate viral infection of
CC hepatocytes (By similarity). {ECO:0000250|UniProtKB:P29326,
CC ECO:0000250|UniProtKB:Q81871}.
CC -!- SUBUNIT: [Isoform Secreted protein ORF2]: Homodimers (By similarity).
CC {ECO:0000250|UniProtKB:Q81871}.
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 (PubMed:8523527, PubMed:12488605). Interacts with
CC phosphorylated protein ORF3 (PubMed:11934888). Interacts with host
CC TMEM134. Interacts with host ASGR1 and ASGR2; these interactions
CC facilitate infection of host hepatocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q81871, ECO:0000269|PubMed:11934888,
CC ECO:0000269|PubMed:12488605, ECO:0000269|PubMed:8523527}.
CC -!- INTERACTION:
CC Q68985; Q9WC28: ORF1; NbExp=2; IntAct=EBI-11180197, EBI-11179420;
CC Q68985; Q68985: ORF2; NbExp=24; IntAct=EBI-11180197, EBI-11180197;
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:0000269|PubMed:11934888, ECO:0000269|PubMed:17229684,
CC ECO:0000269|PubMed:8523527}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q81871}. Host Golgi apparatus
CC {ECO:0000250|UniProtKB:Q81871}. Host cell surface
CC {ECO:0000269|PubMed:10196303, ECO:0000269|PubMed:17229684,
CC ECO:0000269|PubMed:8523527}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Secreted protein ORF2;
CC IsoId=Q68985-1; Sequence=Displayed;
CC Name=Capsid protein ORF2;
CC IsoId=Q68985-2; Sequence=VSP_059887;
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}.
CC -!- CAUTION: Asn-310 was considered to be a major site of N-glycosylation
CC by host but the surrounding motif does not correspond to the N-{P}-
CC [ST]-{P} pattern. {ECO:0000269|PubMed:10196303}.
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DR EMBL; U22532; AAA97366.1; -; Genomic_RNA.
DR EMBL; AF076239; AAC27936.1; -; Genomic_RNA.
DR SMR; Q68985; -.
DR IntAct; Q68985; 2.
DR iPTMnet; Q68985; -.
DR Proteomes; UP000007244; 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: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 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 Alternative initiation; Capsid protein; Glycoprotein; Host cytoplasm;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host-virus interaction;
KW RNA-binding; Secreted; T=1 icosahedral capsid protein;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Virion; Virus entry into host cell.
FT CHAIN 1..660
FT /note="Secreted protein ORF2"
FT /id="PRO_0000445487"
FT REGION 20..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 /evidence="ECO:0000250"
FT REGION 585..610
FT /note="Oligomerization"
FT /evidence="ECO:0000269|PubMed:12488605"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:10196303"
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:0000269|PubMed:10196303"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform Capsid protein ORF2)"
FT /id="VSP_059887"
FT MUTAGEN 137
FT /note="N->A: Slight loss of glycosylation; when associated
FT with A-562."
FT /evidence="ECO:0000269|PubMed:10196303"
FT MUTAGEN 310
FT /note="N->A: Complete loss of glycosylation when associated
FT with A-137 or A-562."
FT /evidence="ECO:0000269|PubMed:10196303"
FT MUTAGEN 562
FT /note="N->A: Slight loss of glycosylation; when associated
FT with A-137."
FT /evidence="ECO:0000269|PubMed:10196303"
SQ SEQUENCE 660 AA; 70937 MW; 948556F804382EB3 CRC64;
MGPRPILLLF LMFLPMLLAP PPGQPSGRRR GRRSGGSGGG FWGDRVDSQP FAIPYIHPTN
PFAPNVTAAA GAGPRVRQPV RPLGSAWRDQ AQRPAAASRR RPTTAGAAPL TAVAPAHDTP
PVPDVDSRGA ILRRQYNLST SPLTSSVATG TNLVLYAAPL SPLLPLQDGT NTHIMATEAS
NYAQYRVARA TIRYRPLVPN AVGGYAISIS FWPQTTPTPT SVDMNSITST DVRILVQPGI
ASELVIPSER LHYRNQGWRS VETSGVAEEE ATSGLVMLCI HGSPVNSYTN TPYTGALGLL
DFALELEFRN LTPGNTNTRV SRYSSTARHR LRRGADGTAE LTTTAATRFM KDLYFTSTNG
VGEIGRGIAL TLFNLADTLL GGLPTELISS AGGQLFYSRP VVSANGEPTV KLYTSVENAQ
QDKGIAIPND IDLGESRVVI QDYDNQHEQD RPTPSPAPSR PFSVLRANDV LWLSLTAAEY
DQSTYGSSTG PVYVSDSVTL VNVATGAQAV ARSLDWTKVT LDGRPLSTIQ QYSKIFFVLP
LRGKLSFWEA GTTRPGYPYN YNTTASDQLL VENAAGHRVA ISTYTTSLGA GPVSISAVAV
LGPHSALALL EDTLDYPARA HTFDDFCPEC RPLGLQGCAF QSTVAELQRL KMKVGKTREL
