ID C7EPG2_WEEV Unreviewed; 1236 AA.
AC C7EPG2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 22-FEB-2023, entry version 71.
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:ACT75286.1, ECO:0000313|Proteomes:UP000167234};
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:ACT75286.1, ECO:0000313|Proteomes:UP000167234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71V1658 {ECO:0000313|EMBL:ACT75286.1};
RX PubMed=19403754; DOI=10.1099/vir.0.008656-0;
RA Logue C.H., Bosio C.F., Welte T., Keene K.M., Ledermann J.P., Phillips A.,
RA Sheahan B.J., Pierro D.J., Marlenee N., Brault A.C., Bosio C.M.,
RA Singh A.J., Powers A.M., Olson K.E.;
RT "Virulence variation among isolates of western equine encephalitis virus in
RT an outbred mouse model.";
RL J. Gen. Virol. 90:1848-1858(2009).
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; GQ287645; ACT75286.1; -; Genomic_RNA.
DR MEROPS; S03.001; -.
DR Proteomes; UP000167234; 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: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..102
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; 136280 MW; B43953F9EE865BD1 CRC64;
MFPYPQLNFP PVYPTNPMAY RDPNPPRRRW RPFRPPLAAQ IEDLRRSIVN LTFKQRSPNP
PPGPPPKKKK SAPKPKPTQP KKKKQQAKRT KRKPKPGKRQ RMCMKLESDK TFPIMLNGQV
NGYACVVGGR LMKPLHVEGK IDNEQLAAVK LKKASMYDLE YGDVPQNMKS DTLQYTSDKP
PGFYNWHHGA VQYENGRFTV PRGVGGKGDS GRPILDNRGR VVAIVLGGAN EGTRTALSVV
TWNQKGVTIR DTPEGSEPWS LVTALCVLSN VTFPCDKPPV CYSLTPERTL 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
KAKQCIAYKS DQTKWVFNSP DLIRHTDHSV QGKLHIPFRL TPTVCPVPLA HTPTVTKWFK
GITLHLTAMR PTLLTTRKLG LRADATAEWI TGSTSRNFSV GREGLEYVWG NHEPVRVWAQ
ESAPGDPHGW PHEIIIHYYH RHPVYTVIVL CGVALAILVG TASSAACIAK ARRDCLTPYA
LAPNATVPTA LAVLCCIRPT NAETFGETLN HLWFNNQPFL WAQLCIPLAA LVILFRCFSC
CMPFLLVAGV CLGKVDAFEH ATTXPNVPGI PYKALVERAG YAPLNLEITV VSSELTPSTN
KEYVTCKFHT 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 GSLTLQYKAD REGHCPVHSH STTAVLKEAT
THVTAVGSIT LHFSTSSPQA NFIVSLCGKK STCNAECKPP ADHIIGEPHK VDQEFQAAVS
KTSWNWLLAL FGGASSLIVV GLIVLVCSSM LINTRR
//
