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Database: UniProt
Entry: Q0QFR3_WEEV
LinkDB: Q0QFR3_WEEV
Original site: Q0QFR3_WEEV 
ID   Q0QFR3_WEEV             Unreviewed;      1236 AA.
AC   Q0QFR3;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   22-FEB-2023, entry version 84.
DE   RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE   AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
OS   Western equine encephalitis virus (WEEV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=11039 {ECO:0000313|EMBL:ABD57958.1};
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=7164; Anopheles.
OH   NCBI_TaxID=7177; Culex tarsalis (Encephalitis mosquito).
OH   NCBI_TaxID=30427; Haemorhous mexicanus (House finch) (Carpodacus mexicanus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=48086; Lepus americanus (Snowshoe hare).
OH   NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH   NCBI_TaxID=48849; Passer domesticus (House sparrow) (Fringilla domestica).
OH   NCBI_TaxID=34999; Thamnophis.
OH   NCBI_TaxID=37591; Urocitellus richardsonii (Richardson's ground squirrel) (Spermophilus richardsonii).
RN   [1] {ECO:0000313|EMBL:ABD57958.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mn520 {ECO:0000313|EMBL:ABD57958.1};
RX   PubMed=16847131; DOI=10.1099/vir.0.81815-0;
RA   Nagata L.P., Hu W.G., Parker M., Chau D., Rayner G.A., Schmaltz F.L.,
RA   Wong J.P.;
RT   "Infectivity variation and genetic diversity among strains of Western
RT   equine encephalitis virus.";
RL   J. Gen. Virol. 87:2353-2361(2006).
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   -!- 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; DQ393793; ABD57958.1; -; Genomic_RNA.
DR   MEROPS; S03.001; -.
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: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   4: Predicted;
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        684..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        759..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1206..1232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..259
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000259|PROSITE:PS51690"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..99
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
SQ   SEQUENCE   1236 AA;  136152 MW;  F0685F9FA1931F22 CRC64;
     MFPYPQLNFP PVYPTNPMAY RDPNPPRRRW RPFRPPLAAQ IEDLRRSIAN LTFKQRSPNP
     PPGPPPKKKK SAPKPKPTQP KKKKQQAKRT KRKPKPGKRQ RMCMKLESDK TFPIMLNGQV
     NGYACVVGGR LMKPLHVEGK IDNEQLAAVK LKKASMYDLE YGDVPQNMKS DTLQYTSDKP
     PGFYNWHHGA VQYENGRFTV PRGVGGKGDS GRPILDNRGR VVAIVLGGAN EGTRTALSVV
     TWNQKGVTIR DTPEGSEPWS LVTALCVLSN VTFPCDKPPV CYSLAPERTL DVLEENVDNP
     NYDTLLENVL KCPSRRPKRS ITDDFTLTSP YLGFCPYCRH STPCFSPIKI ENVWDESDDG
     SIRIQVSAQF GYNQAGTADV TKFRYMSFDH DHDIKEDSME KIAISTSGPC RRLGHKGYFL
     LAQCPPGDSV TVSITSGASE NSCTVEKKIR RKFVGREEYL FPPVHGKLVK CHVYDHLKET
     SAGYITMHRP GPHAYKSYLE EASGEVYIKP PSGKNVTYEC KCGDYSTGIV STRTKMNGCT
     RAKQCIAYKS DQTKWVFNSP DLIRHTDHSV QGKLHIPFRL TPTVCPVPLA HTPTVTKWFK
     GITLHLTATR PTLLTTRKLG LRADATAEWI TGTTSRNFSV GREGLEYVWG NHEPVRVWAQ
     ESAPGDPHGW PHEIIIHYYH RHPVYTVIVL CGVALAILVG TASSAACIAK ARRDCLTPYA
     LAPNATVPTA LAVLCCIRPT NAETFGETLN HLWFNNQPFL WAQLCIPLAA LVILFRCFSC
     CMPFLLVAGV CLGKVDAFEH ATTVPNVPGI PYKALAERAG YAPLNLEITV VSSELTPSTN
     KEYVTCKFRT VIPSPQVKCC GSLECKASSK ADYTCRVFGG VYPFMWGGAQ CFCDSENTQL
     SEAYVEFAPD CTIDHAVALK VHTAALKVGL RIVYGNTTAH LDTFVNGVTP GSSRDLKVIA
     GPISAAFSPF DHKVVIRKGL VYNYDFPEYG AMKPGAFGDI QASSLDATDI VARTDIRLLK
     PSVKNIHVPY TQAVSGYEMW KNNSGRPLQE TAPFGCKIEV EPLRASNCAY GHIPISIDIP
     DAAFVRSSES PTILEVSCTV ADCIYSADFG GSLTLQCKAD REGHCPVHSH STTAVLKEAT
     THVTAVGSIT LHFSTSSPQA NFLVSLCGKK STCNAECKPP ADHIIGEPHK VDQEFQAAVS
     KTSWNWLLAL FGGASSLIVV GLIVLVCSSM LINTRR
//
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