http://togogenome.org/gene/2697049:GU280_gp04 ^@ http://purl.uniprot.org/uniprot/P0DTC4 ^@ Molecule Processing|||Natural Variation|||Region|||Secondary Structure ^@ Chain|||Helix|||Motif|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Envelope small membrane protein|||Helical|||In strain: Beta/B.1.351.|||In strain: Eta/B.1.525.|||In strain: Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||Intravirion|||PDZ-binding; required for interaction with human MPP5|||Virion surface ^@ http://purl.uniprot.org/annotation/PRO_0000449651 http://togogenome.org/gene/2697049:GU280_gp06 ^@ http://purl.uniprot.org/uniprot/P0DTC6 ^@ Experimental Information|||Molecule Processing|||Natural Variation ^@ Chain|||Mutagenesis Site|||Sequence Variant ^@ Complete loss of Golgi localization.|||Complete loss of binding to the NUP98-RAE1 complex and IFN antagonistic function.|||Does not affect repression of reporter protein expression.|||In strain: Eta/B.1.525.|||In strain: Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4.|||Loss of interaction with human NUP98-RAE1 complex which suppresses the down-regulation of protein expression of newly transcribed genes in the host cell.|||Loss of interaction with human NUP98-RAE1 complex which suppresses the mRNA accumulation in the nucleus, the down-regulation of protein expression of newly transcribed genes in the host cell and blockade on nuclear import on a broad range of host factors.|||ORF6 protein|||Retains interaction with human NUP98-RAE1 complex. Increases down-regulation of protein expression of newly transcribed genes in host cell. ^@ http://purl.uniprot.org/annotation/PRO_0000449653 http://togogenome.org/gene/2697049:GU280_gp10 ^@ http://purl.uniprot.org/uniprot/P0DTC9 ^@ Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn ^@ Basic and acidic residues|||CoV N CTD|||CoV N NTD|||Complete loss of RNA-binding.|||In strain: Alpha/B.1.1.7, Gamma/P.1, Zeta/P.2, Theta/P.3, Lambda/C.37, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Alpha/B.1.1.7.|||In strain: Beta/B.1.351, Epsilon/B.1.429, Eta/B.1.525 and Mu/B.1.621.|||In strain: Delta/B.1.617.2, Kappa/B.1.617.1.|||In strain: Delta/B.1.617.2.|||In strain: Eta/B.1.525.|||In strain: Gamma/P.1.|||In strain: Lambda/C.37, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Lambda/C.37.|||In strain: Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.2, Omicron/BA.2.12.1, Omicron BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.4.|||In strain: Zeta/P.2.|||No effect on RNA-binding.|||No effect on phosphorylation.|||No effect on virus replication ex vivo.|||Nuclear localization signal|||Nucleoprotein|||Partial increase of pathogenesis and fitness in vivo. No effect on virus replication ex vivo.|||Partial loss of RNA-binding.|||Partial loss of phosphorylation.|||Phosphoserine; by host|||Phosphoserine; by host GSK3-alpha and GSK3-beta|||Polar residues|||Significant decrease of RNA binding capacity.|||Significant increase of RNA-binding. ^@ http://purl.uniprot.org/annotation/PRO_0000449656 http://togogenome.org/gene/2697049:GU280_gp09 ^@ http://purl.uniprot.org/uniprot/P0DTC8 ^@ Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn ^@ Complete loss of IL17RA binding.|||Complete loss of N-glycosylation and of secretion.|||Complete loss of dimerization.|||Complete loss of hIL-17RA binding.|||Complete loss of hIL-17RC binding.|||In strain: B.1.1.7.|||In strain: Delta/B.1.617.2.|||In strain: Gamma/P.1.|||In strain: Iota/B.1.526.|||In strain: Mu/B.1.621.|||In strain: Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Theta/P.3.|||Interchain|||N-linked (GlcNAc...) (complex) asparagine; by host|||ORF8 protein|||Partial loss of hIL-17RC binding.|||SARS ORF8 Ig-like ^@ http://purl.uniprot.org/annotation/PRO_0000449655 http://togogenome.org/gene/2697049:GU280_gp11 ^@ http://purl.uniprot.org/uniprot/A0A663DJA2 ^@ Molecule Processing ^@ Chain ^@ Putative ORF10 protein ^@ http://purl.uniprot.org/annotation/PRO_0000455520 http://togogenome.org/gene/2697049:GU280_gp02 ^@ http://purl.uniprot.org/uniprot/P0DTC2 ^@ Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ About 50% stronger entry efficiency in Vero E6 cells while 30% weaker entry efficiency in hACE2-expressing BHK cells.|||BetaCoV S1-CTD|||BetaCoV S1-NTD|||Binding to host endocytosis trafficking protein SNX27|||Binding to host plasma membrane localising/FERM domain proteins|||Complete loss of COPI binding and increase in cell fusion.|||Complete loss of O-glycosylation by host GALNT1.|||Complete loss of cleavage by host furin.|||Cytoplasmic|||Decreased HLA binding to NF9 epitope. Increased binding affinity to human ACE2.|||Diacidic ER export motif (host COPII)|||Extracellular|||Helical|||Improved COPI binding, reduced cell fusion and reduced levels of S1/S2 cleavage.|||In strain: 19B/501T.|||In strain: 19B/501Y, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: 19B/501Y.|||In strain: 20A.EU1.|||In strain: 20A.EU2, Iota/B.1.526, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: A23.1, Omicron/BA.2.75.|||In strain: A23.1.|||In strain: Alpha/B.1.1.7, Beta/B.1.351, Gamma/P.1, Delta/B.1.617.2, Epsilon/B.1.427/B.1.429, Eta/B.1.525, Theta/P.3, Iota/B.1.526, Kappa/B.1.617.1, Lambda/C.37, B.1.1.318, Zeta/P.2, Mu/B.1.621, 20A.EU1, 20A.EU2, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5; common variant; binds to hACE2 more efficiently; produces more infectious particles when cultured in primary human epithelial cells; does not significantly shift SARS-CoV-2 neutralization properties.|||In strain: Alpha/B.1.1.7, Beta/B.1.351, Gamma/P.1, Theta/P.3, Mu/B.1.621, 19B/501Y, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5; May enhance affinity to human ACE2 receptor.|||In strain: Alpha/B.1.1.7, Eta/B.1.525, 19B/501T, Omicron/BA.1, Omicron/BA.4, Omicron/BA.5; May compensate for reduced infectivity of RBD escape mutants.|||In strain: Alpha/B.1.1.7, Eta/B.1.525, B.1.1.318.|||In strain: Alpha/B.1.1.7, Theta/P.3, Mu/B.1.621, B.1.1.318, A23.1, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Alpha/B.1.1.7.|||In strain: B.1.1.298.|||In strain: B.1.1.318.|||In strain: Beta/B.1.351, Eta/B.1.525, Theta/P.3, Iota/B.1.526, B.1.1.318, Gamma/P.1, Zeta/P.2 and Mu/B.1.621; May enhance affinity to human ACE2 receptor.|||In strain: Beta/B.1.351, Gamma/P.1, 19B/501Y.|||In strain: Beta/B.1.351, Gamma/P.1, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5; May enhance affinity to human ACE2 receptor.|||In strain: Beta/B.1.351, Iota/B.1.526.|||In strain: Beta/B.1.351.|||In strain: Delta/B.1.617.2, Epsilon/B.1.427/B.1.429, Kappa/B.1.617.1, Lambda/C.37, 19B/501Y, Omicron/BA.4, Omicron/BA.5; Contributes to cellular immunity evasion and increases infectivity.|||In strain: Delta/B.1.617.2, Kappa/B.1.617.1.|||In strain: Delta/B.1.617.2, Mu/B.1.621.|||In strain: Delta/B.1.617.2, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Delta/B.1.617.2, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Delta/B.1.617.2.|||In strain: Epsilon/B.1.427/B.1.429; may change signal peptide cleavage to position 16-17.|||In strain: Epsilon/B.1.427/B.1.429; when coupled with S13I induces resistance to NTD antibodies by changing disulfid bond in positions 15-136 to 136-152.|||In strain: Eta/B.1.525, Omicron/BA.1.|||In strain: Eta/B.1.525.|||In strain: Gamma/P.1, 19B/501T, 19B/501Y, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Gamma/P.1, Theta/P.3, Zeta/P.2.|||In strain: Gamma/P.1.|||In strain: Iota/B.1.526, Mu/B.1.621, B.1.1.318, Omicron/BA.1.|||In strain: Iota/B.1.526.|||In strain: Kappa/B.1.617.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Kappa/B.1.617.1.|||In strain: Lambda/C.37.|||In strain: Mu/B.1.621.|||In strain: Omicron/BA.1, Omicron/BA.2 Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.1, Omicron/BA.2 Omicron/BA.2.12.1.|||In strain: Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.1, Omicron/BA.2.75.|||In strain: Omicron/BA.1.|||In strain: Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.2.12.1.|||In strain: Omicron/BA.2.75.|||In strain: Omicron/BA.4, Omicron/BA.5.|||In strain: Theta/P.3.|||Increase of pseudotyped VSV particle production ex vivo. Increase of viral load in hamster upper respiratory tract. Produces more infectious particles when cultured in primary human epithelial cells; increases replication and transmissibility in hamsters and ferrets.|||Increased binding affinity to human ACE2.|||Increased incorporation of cleaved spike into virions.|||Increased resistance to human covalescent sera neutralization.|||Increased resistance to neutralizing antibodies and human covalescent sera neutralization.|||Increased resistance to neutralizing antibodies.|||Increased resistance to neutralizing antibodies. Decreases HLA binding to NF9 epitope. Increased binding affinity to human ACE2.|||KxHxx, ER retrieval signal (COPI)|||N-linked (GlcNAc...) (complex) asparagine; by host|||N-linked (GlcNAc...) (high mannose) asparagine; by host|||N-linked (GlcNAc...) (hybrid) asparagine; by host|||No effect on O-glycosylation by host GALNT1.|||O-linked (GalNAc) threonine; by host|||O-linked (GlcNAc...) threonine; by host GALNT1|||O-linked (HexNAc...) serine; by host|||Optimized cleavage by host furin.|||Partial improvement of cleavage by host furin.|||Partial loss of O-glycoslyation by host GALNT1.|||Partial loss of biliverdin affinity.|||Reduced host ACE2-binding affinity in vitro.|||Reduced viral infectivity.|||S-palmitoyl cysteine; by host ZDHHC20|||S-palmitoyl cysteine; by host ZDHHC20; partial|||Spike glycoprotein|||Spike protein S1|||Spike protein S2|||Spike protein S2'|||Stabilization in prefusion state (in vaccine Ad26.COV2.S/Janssen Pharmaceutical).|||Stabilization in prefusion state (in vaccine BNT162b2/Pfizer-Biontech, vaccine mRNA-1273/Moderna, vaccine Ad26.COV2.S/Janssen Pharmaceutical). ^@ http://purl.uniprot.org/annotation/PRO_0000449646|||http://purl.uniprot.org/annotation/PRO_0000449647|||http://purl.uniprot.org/annotation/PRO_0000449648|||http://purl.uniprot.org/annotation/PRO_0000449649 http://togogenome.org/gene/2697049:GU280_gp03 ^@ http://purl.uniprot.org/uniprot/P0DTC3 ^@ Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane ^@ CoV 3a-like viroporin CD|||CoV 3a-like viroporin TM|||Cytoplasmic|||Extracellular|||Helical|||In strain: Beta/B.1.351, Epsilon/B.1.429, Iota/B.1.526 and Mu/B.1621.|||In strain: Beta/B.1.351.|||In strain: Delta/B.1.617.2 and Kappa/B.1.617.1.|||In strain: Gamma/P.1.|||In strain: Iota/B.1.526.|||In strain: Mu/B.1.621.|||In strain: Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||No effect on ion permeability.|||O-linked (GalNAc...) threonine; by host|||ORF3a protein|||Partial loss of Ca(2+) and NMDG(+) permeability.|||Partial loss of Ca(2+) and NMDG(+) permeability. Increased localization at host plasma membrane. ^@ http://purl.uniprot.org/annotation/PRO_0000449650 http://togogenome.org/gene/2697049:GU280_gp01 ^@ http://purl.uniprot.org/uniprot/P0DTC1|||http://purl.uniprot.org/uniprot/P0DTD1 ^@ Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Repeat|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger ^@ (+)RNA virus helicase ATP-binding|||(+)RNA virus helicase C-terminal|||2'-O-methyltransferase nsp16|||3C-like proteinase nsp5|||AV-Nsp11N/CoV-Nsp15M|||Acidic residues|||BetaCoV Nsp1 C-terminal|||C4-type|||CV ZBD|||CoV Nsp1 globular|||CoV Nsp2 C-terminal|||CoV Nsp2 N-terminal|||CoV Nsp2 middle|||CoV Nsp3 Y3|||Complete loss of 3C-like proteinase nsp5 cleavage.|||Complete loss of NSP15 endonuclease activity.|||Complete loss of PL-pro activity.|||Complete loss of RNA guanylyltransferase activity.|||Complete loss of ribosome binding and cellular translation inhibition.|||Cytoplasmic|||DPUP|||ExoN|||ExoN/MTase coactivator|||For 3CL-PRO activity|||For PL-PRO activity|||For uridylate-specific endoribonuclease nsp15 activity|||G2M|||Guanine-N7 methyltransferase nsp14|||Helical|||Helicase nsp13|||Host translation inhibitor nsp1|||In strain: Alpha/B.1.1.7, Beta/B.1.351, Gamma/P.1, Delta/B.1.617.2 Iota/B.1.526, Kappa/B.1.617.1, Lambda/C.7, Epsilon/B.1.427/B.1.429, Theta/P.3, Zeta/P.2, Mu/B.1.621, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Alpha/B.1.1.7, Beta/B.1.351, Gamma/P.1, Eta/B.1.525, Iota/B.1.526 and Lambda/C.37.|||In strain: Alpha/B.1.1.7.|||In strain: Beta/B.1.351.|||In strain: Delta/B.1.617.2, Omicron/BA.2.75.|||In strain: Delta/B.1.617.2.|||In strain: Epsilon/B.1.427/B.1.429.|||In strain: Eta/B.1.525.|||In strain: Gamma/P.1.|||In strain: Iota/B.1.526, Beta/B.1.351 and Epsilon/B.1.427/B.1.429.|||In strain: Iota/B.1.526, Lambda/C.37 and Theta/P.3.|||In strain: Iota/B.1.526.|||In strain: Kappa/B.1.617.1.|||In strain: Lambda/C.37, Mu/B.1.621, Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Lambda/C.37.|||In strain: Mu/B.1.621.|||In strain: Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.1.|||In strain: Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75.|||In strain: Omicron/BA.2.75.|||In strain: Omicron/BA.4.|||In strain: Theta/P.3 and Zeta/P.2.|||In strain: Theta/P.3.|||In strain: Zeta/P.2.|||In strain:Omicron/BA.1.|||Increased cleavage of ubiquitin in vitro; no effect on ISG15 cleavage in vitro.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Lumenal|||Macro 1|||Macro 2|||Macro 3|||N7-MTase|||NendoU|||NiRAN|||Nidovirus-type SAM-dependent 2'-O-MTase|||Non-structural protein 10|||Non-structural protein 11|||Non-structural protein 2|||Non-structural protein 4|||Non-structural protein 6|||Non-structural protein 7|||Non-structural protein 8|||Nsp12 Interface|||Nsp12 RNA-dependent RNA polymerase|||Nsp15 N-terminal oligomerization|||Nsp4C|||Nsp9 ssRNA-binding|||Nucleic acid-binding|||Nucleophile; for 3CL-PRO activity|||Papain-like protease nsp3|||Partial loss of ISG15 cleavage in vitro.|||Partial loss of ubiquitin cleavage in vitro; no effect on ISG15 cleavage in vitro.|||Peptidase C16|||Peptidase C30|||Polar residues|||Proton acceptor; for uridylate-specific endoribonuclease nsp15 activity|||Proton donor; for uridylate-specific endoribonuclease nsp15 activity|||RNA-capping enzyme subunit nsp9|||RNA-directed RNA polymerase nsp12|||RdRp Nsp7 cofactor|||RdRp Nsp8 cofactor|||RdRp catalytic|||Reduced inhibition by GRL-0617.|||Reduces RdRp inhibition by remdesivir.|||Replicase polyprotein 1a|||Replicase polyprotein 1ab|||Ubiquitin-like 1|||Ubiquitin-like 2|||Unable to remove host IFIH1 (MDA5) ISGylation.|||Uridylate-specific endoribonuclease nsp15 ^@ http://purl.uniprot.org/annotation/PRO_0000449618|||http://purl.uniprot.org/annotation/PRO_0000449619|||http://purl.uniprot.org/annotation/PRO_0000449620|||http://purl.uniprot.org/annotation/PRO_0000449621|||http://purl.uniprot.org/annotation/PRO_0000449622|||http://purl.uniprot.org/annotation/PRO_0000449623|||http://purl.uniprot.org/annotation/PRO_0000449624|||http://purl.uniprot.org/annotation/PRO_0000449625|||http://purl.uniprot.org/annotation/PRO_0000449626|||http://purl.uniprot.org/annotation/PRO_0000449627|||http://purl.uniprot.org/annotation/PRO_0000449628|||http://purl.uniprot.org/annotation/PRO_0000449629|||http://purl.uniprot.org/annotation/PRO_0000449630|||http://purl.uniprot.org/annotation/PRO_0000449631|||http://purl.uniprot.org/annotation/PRO_0000449632|||http://purl.uniprot.org/annotation/PRO_0000449633|||http://purl.uniprot.org/annotation/PRO_0000449634|||http://purl.uniprot.org/annotation/PRO_0000449635|||http://purl.uniprot.org/annotation/PRO_0000449636|||http://purl.uniprot.org/annotation/PRO_0000449637|||http://purl.uniprot.org/annotation/PRO_0000449638|||http://purl.uniprot.org/annotation/PRO_0000449639|||http://purl.uniprot.org/annotation/PRO_0000449640|||http://purl.uniprot.org/annotation/PRO_0000449641|||http://purl.uniprot.org/annotation/PRO_0000449642|||http://purl.uniprot.org/annotation/PRO_0000449643|||http://purl.uniprot.org/annotation/PRO_0000449644|||http://purl.uniprot.org/annotation/PRO_0000449645 http://togogenome.org/gene/2697049:GU280_gp07 ^@ http://purl.uniprot.org/uniprot/P0DTC7 ^@ Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane ^@ Complete loss of ubiquitination. Partial loss of interferon pathway inhibition.|||Di-lysine motif|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In strain: Alpha/B.1.1.7.|||In strain: Delta/B.1.617.2 and Kappa/B.1.617.1 .|||In strain; Delta/B.1.617.2.|||No effect on ubiquitination.|||ORF7a protein|||X4e ^@ http://purl.uniprot.org/annotation/PRO_0000449654 http://togogenome.org/gene/2697049:GU280_gp08 ^@ http://purl.uniprot.org/uniprot/P0DTD8 ^@ Molecule Processing|||Natural Variation|||Region ^@ Chain|||Sequence Variant|||Transmembrane ^@ Helical|||In strain: Omicron/BA.4.|||ORF7b protein ^@ http://purl.uniprot.org/annotation/PRO_0000449799 http://togogenome.org/gene/2697049:GU280_gp05 ^@ http://purl.uniprot.org/uniprot/P0DTC5 ^@ Modification|||Molecule Processing|||Natural Variation|||Region ^@ Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Helical|||In strain: Eta/B.1.525 and Delta/B.1.617.2.|||In strain: Omicron/BA.1, Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5.|||In strain: Omicron/BA.1.|||In strain: Omicron/BA.5.|||Intravirion|||Membrane protein|||N-linked (GlcNAc...) asparagine; by host|||Virion surface ^@ http://purl.uniprot.org/annotation/PRO_0000449652