ID C7B1B1_SINDV Unreviewed; 783 AA.
AC C7B1B1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 22-FEB-2023, entry version 52.
DE RecName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
DE Flags: Fragment;
OS Sindbis virus (SINV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11034 {ECO:0000313|EMBL:ACU25460.1};
OH NCBI_TaxID=48156; Acrocephalus scirpaceus (Eurasian reed-warbler).
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=53527; Culex.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=45807; Motacilla alba (White wagtail) (Pied wagtail).
OH NCBI_TaxID=177155; Streptopelia turtur.
RN [1] {ECO:0000313|EMBL:ACU25460.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MRM 39 {ECO:0000313|EMBL:ACU25460.1};
RX PubMed=20420530; DOI=10.1089/vbz.2009.0069;
RA Lundstrom J.O., Pfeffer M.;
RT "Phylogeographic structure and evolutionary history of Sindbis virus.";
RL Vector Borne Zoonotic Dis. 10:889-907(2010).
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:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004165}. Host cytoplasm
CC {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004385}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ744527; ACU25460.1; -; mRNA.
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; 2.60.40.3200; 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; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
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 SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
DR PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE 2: Evidence at transcript level;
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 466..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..37
FT /note="Peptidase S3"
FT /evidence="ECO:0000259|PROSITE:PS51690"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACU25460.1"
FT NON_TER 783
FT /evidence="ECO:0000313|EMBL:ACU25460.1"
SQ SEQUENCE 783 AA; 85924 MW; C59B6CB796A4F4B7 CRC64;
AIVLGGADEG ARTALSVVTW NSKGKTIKTT PEGTEEWSAA PLVAAMCILG NMTFPCDQPP
TCYSREPARA LDILEANVDS AAYDDLMRAV LRCTPSSRAK RSITDDFTLT SPYLGTCPYC
HHTEPCFSPI KIEQVWDEAD DNTIRIQTSA QFGYDQSGAA SVNKYRIMSL KQDHTVEEGS
MDAIKISTSG PCRRLSHKGY FLLAKCPPGD SVTVSISAGD SATSCTLARK IKPKFVGREK
YDLPPVHGKK IPCYIYDRLK ETSAGYITMH RPGPHAYTTY LEESSGKVYA KPPSGKNVTY
ECKCGDYKTD TVSARTEITG CTALKQCIAY RSDQTKWVFN SPDLIRHADH TAQGKMHLPF
KLVPSTCLVP LAHVPQVVHG FKHISLQLDT DHLTLLTTRR LGEKPEPTSE WIIGKTVRNF
SVGRDGFEYI WGNHEPVRVW AQESAPGDPH GWPHEIVQHY YHRHPVYTVM VLVAATLAIV
LGVSVASACV CRARRECLTP YALAPNAVVP TSIALLCCIR PTSAEPFSET MTYLWTNSQP
FFWAQLCIPL AAIIVLVRCC SCCLPFLVVA GAYLAKVDAF EHATTVPNVP RIPYKALVER
AGYAPLNLEI TVMSSELIPS TNLEYVTCKY TTVVPSPKVK CCGTLECSSA RHADYNCKVF
GGVYPFMWGG ALCFCDSENS QMSEAYVEFS ADCAADHAQA VKVHTAALKV GLRVVYGNTT
SMLDVYVNGV TPGTSKDLKV IAGPISAAYT PFDHKVIIHK GKVYNYDFPE YGAMKPGAFV
DIQ
//