ID   Q1H8W5_CHIKV            Unreviewed;      1248 AA.
AC   Q1H8W5;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE   AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
DE   Flags: Precursor;
OS   Chikungunya virus (CHIKV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=37124 {ECO:0000313|EMBL:CAJ90470.1, ECO:0000313|Proteomes:UP000139463};
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH   NCBI_TaxID=299627; Aedes furcifer (Mosquito).
OH   NCBI_TaxID=188700; Aedes polynesiensis (Polynesian tiger mosquito).
OH   NCBI_TaxID=9533; Cercopithecus.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9539; Macaca (macaques).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
OH   NCBI_TaxID=9554; Papio (baboons).
OH   NCBI_TaxID=9573; Presbytis.
RN   [1] {ECO:0000313|Proteomes:UP000105651, ECO:0000313|Proteomes:UP000139463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05-061 {ECO:0000313|EMBL:CAJ90481.1}, and 05-115
RC   {ECO:0000313|EMBL:CAJ90470.1};
RX   PubMed=16700631; DOI=10.1371/journal.pmed.0030263;
RA   Schuffenecker I., Iteman I., Michault A., Murri S., Frangeul L.,
RA   Vaney M.-C., Lavenir R., Pardigon N., Reynes J.-M., Pettinelli F.,
RA   Biscornet L., Diancourt L., Michel S., Duquerroy S., Guigon G.,
RA   Frenkiel M.-P., Brehin A.-C., Cubito N., Despres P., Kunst F., Rey F.R.,
RA   Zeller H., Brisse S.;
RT   "Genome microevolution of chikungunya viruses causing the Indian Ocean
RT   outbreak.";
RL   PLoS Med. 3:e263-e263(2006).
RN   [2] {ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC}
RP   X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 810-1200 AND 266-666,
RP   GLYCOSYLATION AT ASN-273; ASN-588 AND ASN-950, AND DISULFIDE BONDS.
RX   PubMed=21124458; DOI=10.1038/nature09555;
RA   Voss J.E., Vaney M.C., Duquerroy S., Vonrhein C., Girard-Blanc C.,
RA   Crublet E., Thompson A., Bricogne G., Rey F.A.;
RT   "Glycoprotein organization of Chikungunya virus particles revealed by X-ray
RT   crystallography.";
RL   Nature 468:709-712(2010).
RN   [3] {ECO:0007829|PDB:3J2W}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.00 ANGSTROMS) OF 810-1202; 332-667 AND
RP   332-666, AND DISULFIDE BONDS.
RX   PubMed=23577234; DOI=10.7554/eLife.00435;
RA   Sun S., Xiang Y., Akahata W., Holdaway H., Pal P., Zhang X., Diamond M.S.,
RA   Nabel G.J., Rossmann M.G.;
RT   "Structural analyses at pseudo atomic resolution of Chikungunya virus and
RT   antibodies show mechanisms of neutralization.";
RL   Elife 2:e00435-e00435(2013).
RN   [4] {ECO:0000313|EMBL:AGX45492.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L2 {ECO:0000313|EMBL:AGX45492.1}, and S7
RC   {ECO:0000313|EMBL:AGX45493.1};
RA   Wasonga C.O., Michuki G.N., Rumberia C.N., Musila L.A., Kimotho J.H.,
RA   Ongus J.R., Inoue S., Sang R.C.;
RT   "Chikungunya virus variants identified in human serum isolate from Comoros
RT   Island, 2005.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0007829|PDB:5ANY}
RP   STRUCTURE BY ELECTRON MICROSCOPY (16.90 ANGSTROMS) OF 810-1221 AND 332-685,
RP   AND DISULFIDE BONDS.
RX   PubMed=26553503; DOI=10.1016/J.CELL.2015.10.050;
RA   Fox J.M., Long F., Edeling M.A., Lin H., van Duijl-Richter M.K., Fong R.H.,
RA   Kahle K.M., Smit J.M., Jin J., Simmons G., Doranz B.J., Crowe J.E.,
RA   Fremont D.H., Rossmann M.G., Diamond M.S.;
RT   "Broadly Neutralizing Alphavirus Antibodies Bind an Epitope on E2 and
RT   Inhibit Entry and Egress.";
RL   Cell 163:1095-1107(2015).
RN   [6] {ECO:0000313|EMBL:AGX45492.1, ECO:0000313|Proteomes:UP000165736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2 {ECO:0000313|EMBL:AGX45492.1}, and S7
RC   {ECO:0000313|EMBL:AGX45493.1};
RX   PubMed=26347221; DOI=10.1007/s11262-015-1243-4;
RA   Wasonga C., Inoue S., Rumberia C., Michuki G., Kimotho J., Ongus J.R.,
RA   Sang R., Musila L.;
RT   "Genetic divergence of Chikungunya virus plaque variants from the Comoros
RT   Island (2005).";
RL   Virus Genes 51:323-328(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Autocatalytic release of the core protein from the N-terminus
CC         of the togavirus structural polyprotein by hydrolysis of a -Trp-|-
CC         Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000256|ARBA:ARBA00000840};
CC   -!- INTERACTION:
CC       Q1H8W5; Q1H8W5: -; NbExp=6; IntAct=EBI-15895793, EBI-15895793;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC       membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. Host cell membrane
CC       {ECO:0000256|ARBA:ARBA00004598}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004598}. Host cell membrane
CC       {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004402}. Host cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004385}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004563}.
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DR   EMBL; KF283986; AGX45492.1; -; Genomic_RNA.
DR   EMBL; KF283987; AGX45493.1; -; Genomic_RNA.
DR   EMBL; AM258990; CAJ90470.1; -; Genomic_RNA.
DR   EMBL; AM258995; CAJ90481.1; -; Genomic_RNA.
DR   PDB; 2XFB; EM; 9.00 A; A/D/F/H=810-1200, B/E/G/I=333-666.
DR   PDB; 2XFC; EM; 9.00 A; A/D/F/H=810-1248, B/E/G/I=326-748.
DR   PDB; 3J2W; EM; 5.00 A; A/B/C/D=810-1202, M/N/O/P=332-667.
DR   PDB; 3N40; X-ray; 2.17 A; F=808-1200, P=266-666.
DR   PDB; 3N41; X-ray; 3.01 A; A=262-325, B=326-685, F=803-808, F=810-1221.
DR   PDB; 3N42; X-ray; 3.00 A; A=262-325, B=326-685, F=803-1221.
DR   PDB; 3N43; X-ray; 2.58 A; A=262-325, B=326-685, F=803-1221.
DR   PDB; 3N44; X-ray; 2.35 A; A=262-325, B=326-685, F=810-1221.
DR   PDB; 5ANY; EM; 16.90 A; A/C/E/G=810-1221, B/D/F/H=332-685.
DR   PDBsum; 2XFB; -.
DR   PDBsum; 2XFC; -.
DR   PDBsum; 3J2W; -.
DR   PDBsum; 3N40; -.
DR   PDBsum; 3N41; -.
DR   PDBsum; 3N42; -.
DR   PDBsum; 3N43; -.
DR   PDBsum; 3N44; -.
DR   PDBsum; 5ANY; -.
DR   DIP; DIP-59506N; -.
DR   MEROPS; S03.001; -.
DR   Proteomes; UP000105651; Genome.
DR   Proteomes; UP000139463; Genome.
DR   Proteomes; UP000165736; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.2230; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.40.3200; Alphavirus E2 glycoprotein, A domain; 1.
DR   Gene3D; 2.60.40.4310; Alphavirus E2 glycoprotein, domain B; 1.
DR   Gene3D; 2.60.40.2400; Alphavirus E2 glycoprotein, domain C; 1.
DR   Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 3.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR002548; Alpha_E1_glycop.
DR   InterPro; IPR000936; Alpha_E2_glycop.
DR   InterPro; IPR002533; Alpha_E3_glycop.
DR   InterPro; IPR042304; Alphavir_E2_A.
DR   InterPro; IPR042305; Alphavir_E2_B.
DR   InterPro; IPR042306; Alphavir_E2_C.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR000930; Peptidase_S3.
DR   Pfam; PF01589; Alpha_E1_glycop; 1.
DR   Pfam; PF00943; Alpha_E2_glycop; 1.
DR   Pfam; PF01563; Alpha_E3_glycop; 1.
DR   Pfam; PF00944; Peptidase_S3; 1.
DR   PRINTS; PR00798; TOGAVIRIN.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
DR   PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|ARBA:ARBA00022510};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|ARBA:ARBA00022506};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   T=4 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022973};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW   Virion {ECO:0000256|ARBA:ARBA00022844};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   TRANSMEM        687..715
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        727..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        766..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        794..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1222..1245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..261
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000259|PROSITE:PS51690"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   CARBOHYD        588
FT                   /note="N-acetyl-D-glucosamine 1"
FT                   /evidence="ECO:0007829|PDB:3N40, ECO:0007829|PDB:3N42"
FT   CARBOHYD        588
FT                   /note="N-acetyl-D-glucosamine 2"
FT                   /evidence="ECO:0007829|PDB:3N43"
FT   CARBOHYD        588
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007829|PDB:3N40, ECO:0007829|PDB:3N42"
FT   CARBOHYD        925
FT                   /note="N-acetyl-D-glucosamine 2"
FT                   /evidence="ECO:0007829|PDB:3N43"
FT   CARBOHYD        950
FT                   /note="N-acetyl-D-glucosamine 3"
FT                   /evidence="ECO:0007829|PDB:3N41, ECO:0007829|PDB:3N44"
FT   CARBOHYD        950
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007829|PDB:3N41, ECO:0007829|PDB:3N44"
FT   DISULFID        269..278
FT                   /evidence="ECO:0007829|PDB:3N40, ECO:0007829|PDB:3N41"
FT   DISULFID        283..287
FT                   /evidence="ECO:0007829|PDB:3N40, ECO:0007829|PDB:3N41"
FT   DISULFID        286..318
FT                   /evidence="ECO:0007829|PDB:3N40, ECO:0007829|PDB:3N41"
FT   DISULFID        344..450
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        347..353
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        416..430
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        478..591
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        526..550
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        528..545
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        858..923
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        871..903
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        872..905
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        877..887
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        1068..1080
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        1110..1185
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        1115..1189
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
FT   DISULFID        1137..1179
FT                   /evidence="ECO:0007829|PDB:2XFB, ECO:0007829|PDB:2XFC"
SQ   SEQUENCE   1248 AA;  138310 MW;  5CCEA5A7D8F2CB19 CRC64;
     MEFIPTQTFY NRRYQPRPWT PRPTIQVIRP RPRPQRQAGQ LAQLISAVNK LTMRAVPQQK
     PRRNRKNKKQ KQKQQAPQNN TNQKKQPPKK KPAQKKKKPG RRERMCMKIE NDCIFEVKHE
     GKVTGYACLV GDKVMKPAHV KGTIDNADLA KLAFKRSSKY DLECAQIPVH MKSDASKFTH
     EKPEGYYNWH HGAVQYSGGR FTIPTGAGKP GDSGRPIFDN KGRVVAIVLG GANEGARTAL
     SVVTWNKDIV TKITPEGAEE WSLAIPVMCL LANTTFPCSQ PPCTPCCYEK EPEETLRMLE
     DNVMRPGYYQ LLQASLTCSP HRQRRSTKDN FNVYKATRPY LAHCPDCGEG HSCHSPVALE
     RIRNEATDGT LKIQVSLQIG IKTDDSHDWT KLRYMDNHMP ADAERAGLFV RTSAPCTITG
     TMGHFILARC PKGETLTVGF TDSRKISHSC THPFHHDPPV IGREKFHSRP QHGKELPCST
     YVQSTAATTE EIEVHMPPDT PDRTLMSQQS GNVKITVNGQ TVRYKCNCGG SNEGLTTTDK
     VINNCKVDQC HAAVTNHKKW QYNSPLVPRN AELGDRKGKI HIPFPLANVT CRVPKARNPT
     VTYGKNQVIM LLYPDHPTLL SYRNMGEEPN YQEEWVMHKK EVVLTVPTEG LEVTWGNNEP
     YKYWPQLSTN GTAHGHPHEI ILYYYELYPT MTVVVVSVAT FILLSMVGMA AGMCMCARRR
     CITPYELTPG ATVPFLLSLI CCIRTAKAAT YQEAAIYLWN EQQPLFWLQA LIPLAALIVL
     CNCLRLLPCC CKTLAFLAVM SVGAHTVSAY EHVTVIPNTV GVPYKTLVNR PGYSPMVLEM
     ELLSVTLEPT LSLDYITCEY KTVIPSPYVK CCGTAECKDK NLPDYSCKVF TGVYPFMWGG
     AYCFCDAENT QLSEAHVEKS ESCKTEFASA YRAHTASASA KLRVLYQGNN ITVTAYANGD
     HAVTVKDAKF IVGPMSSAWT PFDNKIVVYK GDVYNMDYPP FGAGRPGQFG DIQSRTPESK
     DVYANTQLVL QRPAAGTVHV PYSQAPSGFK YWLKERGASL QHTAPFGCQI ATNPVRAVNC
     AVGNMPISID IPEAAFTRVV DAPSLTDMSC EVPACTHSSD FGGVAIIKYA ASKKGKCAVH
     SMTNAVTIRE AEIEVEGNSQ LQISFSTALA SAEFRVQVCS TQVHCAAECH PPKDHIVNYP
     ASHTTLGVQD ISATAMSWVQ KITGGVGLVV AVAALILIVV LCVSFSRH
//