| Tag |
Content |
LipidDB ID |
LipidDB-11034-00946 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
8.94 |
Molecular Weight |
136765.88 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
E1 envelope glycoprotein |
Protein Synonyms/Alias |
p130; 3.4.21.90; Coat protein; C; E3/E2; Spike glycoprotein E3; Spike glycoprotein E2; Spike glycoprotein E1; |
Gene Name |
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Gene Synonyms/Alias |
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Created Date |
21-JUL-1986 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
724 | Canonical | ACKARRECLTPYALA | [1] | S-Palmitoylation | 744 | Canonical | PTSLALLCCVRSANA | [2] | S-Palmitoylation | 745 | Canonical | TSLALLCCVRSANAE | [2] | S-Palmitoylation | 786 | Canonical | AFIVLMRCCSCCLPF | [3] | S-Palmitoylation | 787 | Canonical | FIVLMRCCSCCLPFL | [3] | S-Palmitoylation | 790 | Canonical | LMRCCSCCLPFLVVA | [3] | S-Palmitoylation |
|
Organism |
Sindbis virus (SINV) |
NCBI Taxa ID |
11034 |
Reference |
[1] Gaedigk-Nitschko K, Schlesinger MJ. Site-directed mutations in Sindbis virusE2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defectsin virus assembly and budding. Virology. 1991 Jul;183(1):206-14.[ PMID:1647069]
[2] Ivanova L, Schlesinger MJ. Site-directed mutations in the Sindbis virus E2glycoprotein identify palmitoylation sites and affect virus budding. J Virol.1993 May;67(5):2546-51.[ PMID:8474160]
[3] Gaedigk-Nitschko K, Ding MX, Levy MA, Schlesinger MJ. Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and theunderacylated protein affects virus release and virion structure. Virology. 1990 Mar;175(1):282-91.[ PMID:2309447]
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Functional Description |
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 clathrin-mediated endocytosis their membrane fuses with the host endosomal 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). |
Sequence Annotation |
Transmembrane: 696 712 Helical.
Transmembrane: 728 746 Helical.
Transmembrane: 768 784 Helical.
Transmembrane: 786 802 Helical.
Transmembrane: 1216 1234 Helical.
Domain: 114 264 Peptidase S3.
Region: 93 101 Ribosome-binding.
Active site: 141 141 Charge relay system.
Active site: 147 147 Charge relay system.
Active site: 215 215 Charge relay system.
Functional site: 264 265 Cleavage; by capsid protein.
Functional site: 328 329 Cleavage; by host furin.
Functional site: 751 752 Cleavage; by host signal peptidase.
Functional site: 806 807 Cleavage; by host signal peptidase.
|
Protein Length |
1245 AA. |
Protein Sequence
(Canonical) |
MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS ALVIGQATRP 60
QPPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP GKRQRMALKL EADRLFDVKN 120
EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY 180
TSEHPEGFYN WHHGAVQYSG GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT 240
ALSVVTWNSK GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCDRPPTCY TREPSRALDI 300
LEENVNHEAY DTLLNAILRC GSSGRSKRSV IDDFTLTSPY LGTCSYCHHT VPCFSPVKIE 360
QVWDEADDNT IRIQTSAQFG YDQSGAASAN KYRYMSLKQD HTVKEGTMDD IKISTSGPCR 420
RLSYKGYFLL AKCPPGDSVT VSIVSSNSAT SCTLARKIKP KFVGREKYDL PPVHGKKIPC 480
TVYDRLKETT AGYITMHRPR PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVS 540
TRTEITGCTA IKQCVAYKSD QTKWVFNSPD LIRHDDHTAQ GKLHLPFKLI PSTCMVPVAH 600
APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWIV GKTVRNFTVD RDGLEYIWGN 660
HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA SATVAMMIGV TVAVLCACKA 720
RRECLTPYAL APNAVIPTSL ALLCCVRSAN AETFTETMSY LWSNSQPFFW VQLCIPLAAF 780
IVLMRCCSCC LPFLVVAGAY LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM 840
SSEVLPSTNQ EYITCKFTTV VPSPKIKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC 900
FCDSENSQMS EAYVELSADC ASDHAQAIKV HTAAMKVGLR IVYGNTTSFL DVYVNGVTPG 960
TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA MKPGAFGDIQ ATSLTSKDLI 1020
ASTDIRLLKP SAKNVHVPYT QASSGFEMWK NNSGRPLQET APFGCKIAVN PLRAVDCSYG 1080
NIPISIDIPN AAFIRTSDAP LVSTVKCEVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS 1140
STATLQESTV HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN 1200
DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR 1245
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FASTA
(Canonical) |
>LipidDB-11034-00946|P03316
MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRP
QPPRPRPPPRQKKQAPKQPPKPKKPKTQEKKKKQPAKPKPGKRQRMALKLEADRLFDVKN
EDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTY
TSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRT
ALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCDRPPTCYTREPSRALDI
LEENVNHEAYDTLLNAILRCGSSGRSKRSVIDDFTLTSPYLGTCSYCHHTVPCFSPVKIE
QVWDEADDNTIRIQTSAQFGYDQSGAASANKYRYMSLKQDHTVKEGTMDDIKISTSGPCR
RLSYKGYFLLAKCPPGDSVTVSIVSSNSATSCTLARKIKPKFVGREKYDLPPVHGKKIPC
TVYDRLKETTAGYITMHRPRPHAYTSYLEESSGKVYAKPPSGKNITYECKCGDYKTGTVS
TRTEITGCTAIKQCVAYKSDQTKWVFNSPDLIRHDDHTAQGKLHLPFKLIPSTCMVPVAH
APNVIHGFKHISLQLDTDHLTLLTTRRLGANPEPTTEWIVGKTVRNFTVDRDGLEYIWGN
HEPVRVYAQESAPGDPHGWPHEIVQHYYHRHPVYTILAVASATVAMMIGVTVAVLCACKA
RRECLTPYALAPNAVIPTSLALLCCVRSANAETFTETMSYLWSNSQPFFWVQLCIPLAAF
IVLMRCCSCCLPFLVVAGAYLAKVDAYEHATTVPNVPQIPYKALVERAGYAPLNLEITVM
SSEVLPSTNQEYITCKFTTVVPSPKIKCCGSLECQPAAHADYTCKVFGGVYPFMWGGAQC
FCDSENSQMSEAYVELSADCASDHAQAIKVHTAAMKVGLRIVYGNTTSFLDVYVNGVTPG
TSKDLKVIAGPISASFTPFDHKVVIHRGLVYNYDFPEYGAMKPGAFGDIQATSLTSKDLI
ASTDIRLLKPSAKNVHVPYTQASSGFEMWKNNSGRPLQETAPFGCKIAVNPLRAVDCSYG
NIPISIDIPNAAFIRTSDAPLVSTVKCEVSECTYSADFGGMATLQYVSDREGQCPVHSHS
STATLQESTVHVLEKGAVTVHFSTASPQANFIVSLCGKKTTCNAECKPPADHIVSTPHKN
DQEFQAAISKTSWSWLFALFGGASSLLIIGLMIFACSMMLTSTRR
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Gene Ontology |
GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW GO:0098029; C:icosahedral viral capsid, spike; IDA:CACAO GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW GO:0019031; C:viral envelope; IEA:UniProtKB-KW GO:0055036; C:virion membrane; IEA:InterPro GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro GO:0005198; F:structural molecule activity; IEA:InterPro GO:0075512; P:clathrin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW GO:0061025; P:membrane fusion; IDA:CACAO GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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