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Q5XXP3

- POLS_CHIK3

UniProt

Q5XXP3 - POLS_CHIK3

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Protein

Structural polyprotein

Gene
N/A
Organism
Chikungunya virus (strain 37997) (CHIKV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. 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 icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity).By similarity
E3 protein's function is unknown.By similarity
E2 is responsible for 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 (By similarity).By similarity
6K is a 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 (By similarity).By similarity
E1 is a 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 (By similarity).By similarity

Catalytic activityi

Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391Charge relay systemPROSITE-ProRule annotation
Active sitei145 – 1451Charge relay systemPROSITE-ProRule annotation
Active sitei213 – 2131Charge relay systemPROSITE-ProRule annotation
Sitei261 – 2622Cleavage; by capsid proteinBy similarity
Sitei325 – 3262Cleavage; by host furinBy similarity
Sitei748 – 7492Cleavage; by host signal peptidaseBy similarity
Sitei809 – 8102Cleavage; by host signal peptidaseBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Structural polyprotein
Alternative name(s):
p130
Cleaved into the following 6 chains:
Alternative name(s):
Coat protein
Short name:
C
Alternative name(s):
E3/E2
Alternative name(s):
Spike glycoprotein E3
Alternative name(s):
Spike glycoprotein E2
Alternative name(s):
Spike glycoprotein E1
OrganismiChikungunya virus (strain 37997) (CHIKV)
Taxonomic identifieri371095 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Aedes furcifer (Mosquito) [TaxID: 299627]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]
Cercopithecus [TaxID: 9533]
Homo sapiens (Human) [TaxID: 9606]
Macaca (macaques) [TaxID: 9539]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Papio (baboons) [TaxID: 9554]
Presbytis [TaxID: 9573]
ProteomesiUP000008450: Genome

Subcellular locationi

Chain Capsid protein : Virion By similarity. Host cytoplasm By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 692692ExtracellularSequence AnalysisAdd
BLAST
Transmembranei693 – 71321HelicalSequence AnalysisAdd
BLAST
Topological domaini714 – 74835CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini749 – 76315ExtracellularSequence AnalysisAdd
BLAST
Transmembranei764 – 78421HelicalSequence AnalysisAdd
BLAST
Topological domaini785 – 79511CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei796 – 81621HelicalSequence AnalysisAdd
BLAST
Topological domaini817 – 1224408ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1225 – 124521HelicalSequence AnalysisAdd
BLAST
Topological domaini1246 – 12483CytoplasmicSequence Analysis

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. T=4 icosahedral viral capsid Source: UniProtKB-KW
  5. virion membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Membrane, T=4 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Capsid proteinBy similarityPRO_0000226225Add
BLAST
Chaini262 – 748487p62By similarityPRO_0000226226Add
BLAST
Chaini262 – 32564E3 proteinBy similarityPRO_0000226227Add
BLAST
Signal peptidei262 – 27514Not cleavedSequence AnalysisAdd
BLAST
Chaini326 – 748423E2 envelope glycoproteinBy similarityPRO_0000226228Add
BLAST
Chaini749 – 809616K proteinBy similarityPRO_0000226229Add
BLAST
Chaini810 – 1248439E1 envelope glycoproteinBy similarityPRO_0000226230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi113 ↔ 128By similarity
Glycosylationi273 – 2731N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi588 – 5881N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi670 – 6701N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi721 – 7211S-palmitoyl cysteine; by hostBy similarity
Lipidationi741 – 7411S-palmitoyl cysteine; by hostBy similarity
Lipidationi742 – 7421S-palmitoyl cysteine; by hostBy similarity
Disulfide bondi858 ↔ 923By similarity
Disulfide bondi871 ↔ 903By similarity
Disulfide bondi872 ↔ 905By similarity
Disulfide bondi877 ↔ 887By similarity
Glycosylationi950 – 9501N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi1068 ↔ 1080By similarity
Disulfide bondi1110 ↔ 1185By similarity
Disulfide bondi1115 ↔ 1189By similarity
Disulfide bondi1137 ↔ 1179By similarity
Lipidationi1242 – 12421S-stearoyl cysteine; by hostBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking p62 signal peptide. The remaining polyprotein is then targeted to the endoplasmic reticulum, where host signal peptidase cleaves it into p62, 6K and E1 proteins. p62 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle (By similarity).By similarity
E2 is 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. 6K protein is also palmitoylated. E1 is stearoylated (By similarity).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

p62 and E1 form a heterodimer shortly after synthesis. Processing of p62 into E2 and E3 results in a heterodimer of E2 and E1. Spike at virion surface are constituted of three E2-E1 heterodimers. After target cell attachment and endocytosis, E1 change conformation to form homotrimers (By similarity).By similarity

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J2Welectron microscopy5.00E/F/G/H1203-1248[»]
I/J/K/L113-261[»]
M/N/O/P332-666[»]
Q/R/S/T668-748[»]
ProteinModelPortaliQ5XXP3.
SMRiQ5XXP3. Positions 113-261, 810-1199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 261149Peptidase S3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 107107Intrinsically disordered, in contact with genomic RNA in nucleocapsidSequence AnalysisAdd
BLAST
Regioni88 – 10013Ribosome-bindingBy similarityAdd
BLAST
Regioni721 – 74121Transient transmembrane before p62-6K protein processingSequence AnalysisAdd
BLAST
Regioni893 – 91018E1 fusion peptide loopBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase S3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 3 hits.
InterProiIPR002548. Alpha_E1_glycop.
IPR000936. Alpha_E2_glycop.
IPR002533. Alpha_E3_glycop.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014756. Ig_E-set.
IPR000930. Peptidase_S3.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF01589. Alpha_E1_glycop. 1 hit.
PF00943. Alpha_E2_glycop. 1 hit.
PF01563. Alpha_E3_glycop. 1 hit.
PF00944. Peptidase_S3. 1 hit.
[Graphical view]
PRINTSiPR00798. TOGAVIRIN.
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51690. ALPHAVIRUS_CP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5XXP3-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MEFIPTQTFY NRRYQPRPWA PRPTIQVIRP RPRPQRQAGQ LAQLISAVNK
60 70 80 90 100
LTMRAVPQQK PRRNRKNKKQ RQKKQAPQND PKQKKQPPQK KPAQKKKKPG
110 120 130 140 150
RRERMCMKIE NDCIFEVKHE GKVMGYACLV GDKVMKPAHV KGTIDNADLA
160 170 180 190 200
KLAFKRSSKY DLECAQIPVH MKSDASKFTH EKPEGYYNWH HGAVQYSGGR
210 220 230 240 250
FTIPTGAGKP GDSGRPIFDN KGRVVAIVLG GANEGARTAL SVVTWNKDIV
260 270 280 290 300
TKITPEGAEE WSLALPVLCL LANTTFPCSQ PPCTPCCYEK EPESTLRMLE
310 320 330 340 350
DNVMRPGYYQ LLKASLTCSP HRQRRSTKDN FNVYKATRPY LAHCPDCGEG
360 370 380 390 400
HSCHSPIALE RIRNEATDGT LKIQVSLQIG IKTDDSHDWT KLRYMDSHTP
410 420 430 440 450
ADAERAGLLV RTSAPCTITG TMGHFILARC PKGETLTVGF TDSRKISHTC
460 470 480 490 500
THPFHHEPPV IGRERFHSRP QHGKELPCST YVQSTAATAE EIEVHMPPDT
510 520 530 540 550
PDRTLMTQQS GNVKITVNGQ TVRYKCNCGG SNEGLTTTDK VINNCKIDQC
560 570 580 590 600
HAAVTNHKNW QYNSPLVPRN AELGDRKGKI HIPFPLANVT CRVPKARNPT
610 620 630 640 650
VTYGKNQVTM LLYPDHPTLL SYRNMGQEPN YHEEWVTHKK EVTLTVPTEG
660 670 680 690 700
LEVTWGNNEP YKYWPQMSTN GTAHGHPHEI ILYYYELYPT MTVVIVSVAS
710 720 730 740 750
FVLLSMVGTA VGMCVCARRR CITPYELTPG ATVPFLLSLL CCVRTTKAAT
760 770 780 790 800
YYEAAAYLWN EQQPLFWLQA LIPLAALIVL CNCLKLLPCC CKTLAFLAVM
810 820 830 840 850
SIGAHTVSAY EHVTVIPNTV GVPYKTLVNR PGYSPMVLEM ELQSVTLEPT
860 870 880 890 900
LSLDYITCEY KTVIPSPYVK CCGTAECKDK SLPDYSCKVF TGVYPFMWGG
910 920 930 940 950
AYCFCDAENT QLSEAHVEKS ESCKTEFASA YRAHTASASA KLRVLYQGNN
960 970 980 990 1000
ITVAAYANGD HAVTVKDAKF VVGPMSSAWT PFDNKIVVYK GDVYNMDYPP
1010 1020 1030 1040 1050
FGAGRPGQFG DIQSRTPESK DVYANTQLVL QRPAAGTVHV PYSQAPSGFK
1060 1070 1080 1090 1100
YWLKERGASL QHTAPFGCQI ATNPVRAVNC AVGNIPISID IPDAAFTRVV
1110 1120 1130 1140 1150
DAPSVTDMSC EVPACTHSSD FGGVAIIKYT ASKKGKCAVH SMTNAVTIRE
1160 1170 1180 1190 1200
ADVEVEGNSQ LQISFSTALA SAEFRVQVCS TQVHCAAACH PPKDHIVNYP
1210 1220 1230 1240
ASHTTLGVQD ISTTAMSWVQ KITGGVGLIV AVAALILIVV LCVSFSRH
Length:1,248
Mass (Da):138,071
Last modified:November 23, 2004 - v1
Checksum:iA19160F7E5ED521E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY726732 Genomic RNA. Translation: AAU43881.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY726732 Genomic RNA. Translation: AAU43881.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J2W electron microscopy 5.00 E/F/G/H 1203-1248 [» ]
I/J/K/L 113-261 [» ]
M/N/O/P 332-666 [» ]
Q/R/S/T 668-748 [» ]
ProteinModelPortali Q5XXP3.
SMRi Q5XXP3. Positions 113-261, 810-1199.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.350. 1 hit.
2.60.98.10. 3 hits.
InterProi IPR002548. Alpha_E1_glycop.
IPR000936. Alpha_E2_glycop.
IPR002533. Alpha_E3_glycop.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014756. Ig_E-set.
IPR000930. Peptidase_S3.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF01589. Alpha_E1_glycop. 1 hit.
PF00943. Alpha_E2_glycop. 1 hit.
PF01563. Alpha_E3_glycop. 1 hit.
PF00944. Peptidase_S3. 1 hit.
[Graphical view ]
PRINTSi PR00798. TOGAVIRIN.
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS51690. ALPHAVIRUS_CP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Differential infectivities of O'Nyong-Nyong and Chikungunya virus isolates in Anopheles gambiae and Aedes aegypti mosquitoes."
    Vanlandingham D.L., Hong C., Klingler K., Tsetsarkin K., McElroy K.L., Powers A.M., Lehane M.J., Higgs S.
    Am. J. Trop. Med. Hyg. 72:616-621(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLS_CHIK3
AccessioniPrimary (citable) accession number: Q5XXP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 23, 2004
Last modified: October 29, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Structural polyprotein is translated from a subgenomic RNA synthesized during togavirus replication.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3