Q5XXP3 · POLS_CHIK3
- ProteinStructural polyprotein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1248 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Capsid protein
Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity).
The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity).
Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (By similarity).
Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles (By similarity).
The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (By similarity).
In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (By similarity).
This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (By similarity).
The uncoating might be triggered by the interaction of capsid proteins with ribosomes (By similarity).
Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity).
Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (By similarity).
Degrades host cyclic GMP-AMP synthase (CGAS) thereby inhibiting the cGAS-STING pathway (By similarity).
The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity).
Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (By similarity).
Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles (By similarity).
The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (By similarity).
In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (By similarity).
This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (By similarity).
The uncoating might be triggered by the interaction of capsid proteins with ribosomes (By similarity).
Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity).
Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (By similarity).
Degrades host cyclic GMP-AMP synthase (CGAS) thereby inhibiting the cGAS-STING pathway (By similarity).
Assembly protein E3
Provides the signal sequence for the translocation of the precursor of protein E3/E2 to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with spike glycoprotein E1 and mediates pH protection of the latter during the transport via the secretory pathway. After virion release from the host cell, the assembly protein E3 is gradually released in the extracellular space.
Spike glycoprotein E2
Plays a role in viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane.
6K protein
Constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins.
Spike glycoprotein E1
Class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group.
Miscellaneous
Structural polyprotein: Translated from a subgenomic RNA synthesized during togavirus replication.
Catalytic activity
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 139 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 161 | Charge relay system | ||||
Sequence: D | ||||||
Site | 187 | Involved in dimerization of the capsid protein | ||||
Sequence: Y | ||||||
Active site | 213 | Charge relay system | ||||
Sequence: S | ||||||
Site | 220 | Involved in dimerization of the capsid protein | ||||
Sequence: N | ||||||
Site | 261-262 | Cleavage; by autolysis | ||||
Sequence: WS | ||||||
Site | 325-326 | Cleavage; by host furin | ||||
Sequence: RS | ||||||
Site | 748-749 | Cleavage; by host signal peptidase | ||||
Sequence: AA | ||||||
Site | 809-810 | Cleavage; by host signal peptidase | ||||
Sequence: AY |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Cellular Component | host cell nucleus | |
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Cellular Component | T=4 icosahedral viral capsid | |
Cellular Component | virion membrane | |
Molecular Function | RNA binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | structural molecule activity | |
Biological Process | fusion of virus membrane with host endosome membrane | |
Biological Process | proteolysis | |
Biological Process | symbiont entry into host cell | |
Biological Process | symbiont-mediated suppression of host toll-like receptor signaling pathway | |
Biological Process | virion attachment to host cell |
Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameStructural polyprotein
- Alternative names
- Cleaved into 6 chains
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Alsuviricetes > Martellivirales > Togaviridae > Alphavirus > Chikungunya virus
- Virus hosts
Accessions
- Primary accessionQ5XXP3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Capsid protein
Note: Shuttles between the cytoplasm and the nucleus.
Spike glycoprotein E2
Virion membrane ; Single-pass type I membrane protein
Host cell membrane ; Single-pass type I membrane protein
6K protein
Host cell membrane ; Multi-pass membrane protein
Virion membrane ; Multi-pass membrane protein
Spike glycoprotein E1
Virion membrane ; Single-pass type I membrane protein
Host cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-692 | Extracellular | ||||
Sequence: MEFIPTQTFYNRRYQPRPWAPRPTIQVIRPRPRPQRQAGQLAQLISAVNKLTMRAVPQQKPRRNRKNKKQRQKKQAPQNDPKQKKQPPQKKPAQKKKKPGRRERMCMKIENDCIFEVKHEGKVMGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWNKDIVTKITPEGAEEWSLALPVLCLLANTTFPCSQPPCTPCCYEKEPESTLRMLEDNVMRPGYYQLLKASLTCSPHRQRRSTKDNFNVYKATRPYLAHCPDCGEGHSCHSPIALERIRNEATDGTLKIQVSLQIGIKTDDSHDWTKLRYMDSHTPADAERAGLLVRTSAPCTITGTMGHFILARCPKGETLTVGFTDSRKISHTCTHPFHHEPPVIGRERFHSRPQHGKELPCSTYVQSTAATAEEIEVHMPPDTPDRTLMTQQSGNVKITVNGQTVRYKCNCGGSNEGLTTTDKVINNCKIDQCHAAVTNHKNWQYNSPLVPRNAELGDRKGKIHIPFPLANVTCRVPKARNPTVTYGKNQVTMLLYPDHPTLLSYRNMGQEPNYHEEWVTHKKEVTLTVPTEGLEVTWGNNEPYKYWPQMSTNGTAHGHPHEIILYYYELYPTMT | ||||||
Transmembrane | 693-713 | Helical | ||||
Sequence: VVIVSVASFVLLSMVGTAVGM | ||||||
Topological domain | 714-748 | Cytoplasmic | ||||
Sequence: CVCARRRCITPYELTPGATVPFLLSLLCCVRTTKA | ||||||
Topological domain | 749-763 | Extracellular | ||||
Sequence: ATYYEAAAYLWNEQQ | ||||||
Transmembrane | 764-784 | Helical | ||||
Sequence: PLFWLQALIPLAALIVLCNCL | ||||||
Topological domain | 785-795 | Cytoplasmic | ||||
Sequence: KLLPCCCKTLA | ||||||
Transmembrane | 796-816 | Helical | ||||
Sequence: FLAVMSIGAHTVSAYEHVTVI | ||||||
Topological domain | 817-1224 | Extracellular | ||||
Sequence: PNTVGVPYKTLVNRPGYSPMVLEMELQSVTLEPTLSLDYITCEYKTVIPSPYVKCCGTAECKDKSLPDYSCKVFTGVYPFMWGGAYCFCDAENTQLSEAHVEKSESCKTEFASAYRAHTASASAKLRVLYQGNNITVAAYANGDHAVTVKDAKFVVGPMSSAWTPFDNKIVVYKGDVYNMDYPPFGAGRPGQFGDIQSRTPESKDVYANTQLVLQRPAAGTVHVPYSQAPSGFKYWLKERGASLQHTAPFGCQIATNPVRAVNCAVGNIPISIDIPDAAFTRVVDAPSVTDMSCEVPACTHSSDFGGVAIIKYTASKKGKCAVHSMTNAVTIREADVEVEGNSQLQISFSTALASAEFRVQVCSTQVHCAAACHPPKDHIVNYPASHTTLGVQDISTTAMSWVQKITG | ||||||
Transmembrane | 1225-1245 | Helical | ||||
Sequence: GVGLIVAVAALILIVVLCVSF | ||||||
Topological domain | 1246-1248 | Cytoplasmic | ||||
Sequence: SRH |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000226225 | 1-261 | Capsid protein | |||
Sequence: MEFIPTQTFYNRRYQPRPWAPRPTIQVIRPRPRPQRQAGQLAQLISAVNKLTMRAVPQQKPRRNRKNKKQRQKKQAPQNDPKQKKQPPQKKPAQKKKKPGRRERMCMKIENDCIFEVKHEGKVMGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWNKDIVTKITPEGAEEW | ||||||
Disulfide bond | 113↔128 | |||||
Sequence: CIFEVKHEGKVMGYAC | ||||||
Chain | PRO_0000226227 | 262-325 | Assembly protein E3 | |||
Sequence: SLALPVLCLLANTTFPCSQPPCTPCCYEKEPESTLRMLEDNVMRPGYYQLLKASLTCSPHRQRR | ||||||
Chain | PRO_0000226226 | 262-748 | Precursor of protein E3/E2 | |||
Sequence: SLALPVLCLLANTTFPCSQPPCTPCCYEKEPESTLRMLEDNVMRPGYYQLLKASLTCSPHRQRRSTKDNFNVYKATRPYLAHCPDCGEGHSCHSPIALERIRNEATDGTLKIQVSLQIGIKTDDSHDWTKLRYMDSHTPADAERAGLLVRTSAPCTITGTMGHFILARCPKGETLTVGFTDSRKISHTCTHPFHHEPPVIGRERFHSRPQHGKELPCSTYVQSTAATAEEIEVHMPPDTPDRTLMTQQSGNVKITVNGQTVRYKCNCGGSNEGLTTTDKVINNCKIDQCHAAVTNHKNWQYNSPLVPRNAELGDRKGKIHIPFPLANVTCRVPKARNPTVTYGKNQVTMLLYPDHPTLLSYRNMGQEPNYHEEWVTHKKEVTLTVPTEGLEVTWGNNEPYKYWPQMSTNGTAHGHPHEIILYYYELYPTMTVVIVSVASFVLLSMVGTAVGMCVCARRRCITPYELTPGATVPFLLSLLCCVRTTKA | ||||||
Glycosylation | 273 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000226228 | 326-748 | Spike glycoprotein E2 | |||
Sequence: STKDNFNVYKATRPYLAHCPDCGEGHSCHSPIALERIRNEATDGTLKIQVSLQIGIKTDDSHDWTKLRYMDSHTPADAERAGLLVRTSAPCTITGTMGHFILARCPKGETLTVGFTDSRKISHTCTHPFHHEPPVIGRERFHSRPQHGKELPCSTYVQSTAATAEEIEVHMPPDTPDRTLMTQQSGNVKITVNGQTVRYKCNCGGSNEGLTTTDKVINNCKIDQCHAAVTNHKNWQYNSPLVPRNAELGDRKGKIHIPFPLANVTCRVPKARNPTVTYGKNQVTMLLYPDHPTLLSYRNMGQEPNYHEEWVTHKKEVTLTVPTEGLEVTWGNNEPYKYWPQMSTNGTAHGHPHEIILYYYELYPTMTVVIVSVASFVLLSMVGTAVGMCVCARRRCITPYELTPGATVPFLLSLLCCVRTTKA | ||||||
Glycosylation | 588 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 670 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Lipidation | 721 | S-palmitoyl cysteine; by host | ||||
Sequence: C | ||||||
Lipidation | 741 | S-palmitoyl cysteine; by host | ||||
Sequence: C | ||||||
Lipidation | 742 | S-palmitoyl cysteine; by host | ||||
Sequence: C | ||||||
Chain | PRO_0000226229 | 749-809 | 6K protein | |||
Sequence: ATYYEAAAYLWNEQQPLFWLQALIPLAALIVLCNCLKLLPCCCKTLAFLAVMSIGAHTVSA | ||||||
Chain | PRO_0000226230 | 810-1248 | Spike glycoprotein E1 | |||
Sequence: YEHVTVIPNTVGVPYKTLVNRPGYSPMVLEMELQSVTLEPTLSLDYITCEYKTVIPSPYVKCCGTAECKDKSLPDYSCKVFTGVYPFMWGGAYCFCDAENTQLSEAHVEKSESCKTEFASAYRAHTASASAKLRVLYQGNNITVAAYANGDHAVTVKDAKFVVGPMSSAWTPFDNKIVVYKGDVYNMDYPPFGAGRPGQFGDIQSRTPESKDVYANTQLVLQRPAAGTVHVPYSQAPSGFKYWLKERGASLQHTAPFGCQIATNPVRAVNCAVGNIPISIDIPDAAFTRVVDAPSVTDMSCEVPACTHSSDFGGVAIIKYTASKKGKCAVHSMTNAVTIREADVEVEGNSQLQISFSTALASAEFRVQVCSTQVHCAAACHPPKDHIVNYPASHTTLGVQDISTTAMSWVQKITGGVGLIVAVAALILIVVLCVSFSRH | ||||||
Disulfide bond | 858↔923 | |||||
Sequence: CEYKTVIPSPYVKCCGTAECKDKSLPDYSCKVFTGVYPFMWGGAYCFCDAENTQLSEAHVEKSESC | ||||||
Disulfide bond | 871↔903 | |||||
Sequence: CCGTAECKDKSLPDYSCKVFTGVYPFMWGGAYC | ||||||
Disulfide bond | 872↔905 | |||||
Sequence: CGTAECKDKSLPDYSCKVFTGVYPFMWGGAYCFC | ||||||
Disulfide bond | 877↔887 | |||||
Sequence: CKDKSLPDYSC | ||||||
Glycosylation | 950 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 1068↔1080 | |||||
Sequence: CQIATNPVRAVNC | ||||||
Disulfide bond | 1110↔1185 | |||||
Sequence: CEVPACTHSSDFGGVAIIKYTASKKGKCAVHSMTNAVTIREADVEVEGNSQLQISFSTALASAEFRVQVCSTQVHC | ||||||
Disulfide bond | 1115↔1189 | |||||
Sequence: CTHSSDFGGVAIIKYTASKKGKCAVHSMTNAVTIREADVEVEGNSQLQISFSTALASAEFRVQVCSTQVHCAAAC | ||||||
Disulfide bond | 1137↔1179 | |||||
Sequence: CAVHSMTNAVTIREADVEVEGNSQLQISFSTALASAEFRVQVC | ||||||
Lipidation | 1242 | S-stearoyl cysteine; by host | ||||
Sequence: C |
Post-translational modification
Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (By similarity).
The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle (By similarity).
The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle (By similarity).
Spike glycoprotein E2
Palmitoylated via thioester bonds. These palmitoylations may induce disruption of the C-terminus transmembrane. This would result in the reorientation of E2 C-terminus from lumenal to cytoplasmic side.
Spike glycoprotein E1
N-glycosylated.
Spike glycoprotein E2
N-glycosylated.
Assembly protein E3
N-glycosylated.
6K protein
Palmitoylated via thioester bonds.
Keywords
- PTM
Interaction
Subunit
Capsid protein
Homodimer (By similarity).
Homomultimer (Probable). Interacts with host karyopherin KPNA4; this interaction allows the nuclear import of the viral capsid protein (By similarity).
Interacts with spike glycoprotein E2 (By similarity).
Interacts with host IRAK1; the interaction leads to inhibition of IRAK1-dependent signaling (By similarity).
Homomultimer (Probable). Interacts with host karyopherin KPNA4; this interaction allows the nuclear import of the viral capsid protein (By similarity).
Interacts with spike glycoprotein E2 (By similarity).
Interacts with host IRAK1; the interaction leads to inhibition of IRAK1-dependent signaling (By similarity).
Precursor of protein E3/E2
The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity).
Spike glycoprotein E1
The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity).
Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity).
Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity).
After target cell attachment and endocytosis, E1 change conformation to form homotrimers (By similarity).
Interacts with 6K protein (By similarity).
Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity).
Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity).
After target cell attachment and endocytosis, E1 change conformation to form homotrimers (By similarity).
Interacts with 6K protein (By similarity).
Spike glycoprotein E2
Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity).
Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity).
Interacts with 6K protein (By similarity).
Interacts with host MXRA8; this interaction mediates virus entry (By similarity).
Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity).
Interacts with 6K protein (By similarity).
Interacts with host MXRA8; this interaction mediates virus entry (By similarity).
6K protein
Interacts with spike glycoprotein E1 (By similarity).
Interacts with spike glycoprotein E2 (By similarity).
Interacts with spike glycoprotein E2 (By similarity).
Family & Domains
Features
Showing features for region, motif, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 14-104 | Disordered | ||||
Sequence: YQPRPWAPRPTIQVIRPRPRPQRQAGQLAQLISAVNKLTMRAVPQQKPRRNRKNKKQRQKKQAPQNDPKQKKQPPQKKPAQKKKKPGRRER | ||||||
Region | 36-68 | Host transcription inhibition | ||||
Sequence: RQAGQLAQLISAVNKLTMRAVPQQKPRRNRKNK | ||||||
Motif | 61-99 | Nuclear localization signal | ||||
Sequence: PRRNRKNKKQRQKKQAPQNDPKQKKQPPQKKPAQKKKKP | ||||||
Compositional bias | 73-87 | Basic and acidic residues | ||||
Sequence: KKQAPQNDPKQKKQP | ||||||
Region | 84-114 | Binding to the viral RNA | ||||
Sequence: KKQPPQKKPAQKKKKPGRRERMCMKIENDCI | ||||||
Compositional bias | 88-102 | Basic residues | ||||
Sequence: PQKKPAQKKKKPGRR | ||||||
Region | 99-113 | Ribosome-binding | ||||
Sequence: PGRRERMCMKIENDC | ||||||
Domain | 113-261 | Peptidase S3 | ||||
Sequence: CIFEVKHEGKVMGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWNKDIVTKITPEGAEEW | ||||||
Motif | 144-154 | Nuclear export signal | ||||
Sequence: IDNADLAKLAF | ||||||
Region | 183-193 | Dimerization of the capsid protein | ||||
Sequence: PEGYYNWHHGA | ||||||
Region | 219-223 | Dimerization of the capsid protein | ||||
Sequence: DNKGR | ||||||
Region | 262-274 | Functions as an uncleaved signal peptide for the precursor of protein E3/E2 | ||||
Sequence: SLALPVLCLLANT | ||||||
Region | 721-741 | Transient transmembrane before p62-6K protein processing | ||||
Sequence: CITPYELTPGATVPFLLSLLC | ||||||
Region | 893-910 | E1 fusion peptide loop | ||||
Sequence: VYPFMWGGAYCFCDAENT |
Domain
Capsid protein
The N-terminus contains a nuclear localization signal and a CRM1-mediated nuclear export signal (By similarity).
The C-terminus functions as a protease during translation to cleave itself from the translating structural polyprotein (By similarity).
The C-terminus functions as a protease during translation to cleave itself from the translating structural polyprotein (By similarity).
Structural polyprotein: As soon as the capsid protein has been autocleaved, an internal uncleaved signal peptide directs the remaining polyprotein to the endoplasmic reticulum.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,248
- Mass (Da)138,071
- Last updated2004-11-23 v1
- ChecksumA19160F7E5ED521E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 73-87 | Basic and acidic residues | ||||
Sequence: KKQAPQNDPKQKKQP | ||||||
Compositional bias | 88-102 | Basic residues | ||||
Sequence: PQKKPAQKKKKPGRR |
Keywords
- Technical term