Reviewed, UniProtKB/Swiss-Prot P03315 (POLS_SFV)

Names and origin

Protein names	Recommended name:     Structural polyprotein Alternative name(s):     p130 Cleaved into the following 6 chains:     1- Recommended name:             Capsid protein               EC=3.4.21.-         Alternative name(s):             Coat protein               Short name=C     2- Recommended name:             p62         Alternative name(s):             E3/E2     3- Recommended name:             E3 protein         Alternative name(s):             Spike glycoprotein E3     4- Recommended name:             E2 envelope glycoprotein         Alternative name(s):             Spike glycoprotein E2     5- Recommended name:             6K protein     6- Recommended name:             E1 envelope glycoprotein         Alternative name(s):             Spike glycoprotein E1
Organism	Semliki forest virus (SFV)
Taxonomic identifier	11033 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Togaviridae › Alphavirus › SFV complex
Virus host	Aedes [TaxID: 7158] Culex tritaeniorhynchus (Mosquito) [TaxID: 7178] Atelerix albiventris (Middle-African hedgehog) [TaxID: 9368] Homo sapiens (Human) [TaxID: 9606] Rhipicephalus [TaxID: 34630] Quelea [TaxID: 158617] Halcyon [TaxID: 170865]

Protein attributes

Sequence length	1253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 endocytosis their membrane fuses with the target cell 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. Ref.9 Ref.10 Ref.11 E3 protein's function is unknown. Ref.9 Ref.10 Ref.11 E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane. Ref.9 Ref.10 Ref.11 6K is a constitutive membrane protein involved in virus glycoprotein processing, membrane permeabilization, and the budding of viral particles. Present in low amount in virions, about 3% compared to viral glycoproteins. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Ref.9 Ref.10 Ref.11 E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after cell and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group. Ref.9 Ref.10 Ref.11
Subunit structure	p62 and E1 form a heterodimer shortly after synthesis. Processing of p62 into E2 and E3 results in a heterodimer of E2 and E1. Spike at virion surface are constituted of three E2-E1 heterodimers. After target cell attachment and endocytosis, E1 change conformation to form homotrimers.
Subcellular location	Capsid protein: Virion By similarity. Host cytoplasm By similarity. p62: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity. E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity. E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity. 6K protein: Host cell membrane; Multi-pass membrane protein By similarity. Virion membrane; Multi-pass membrane protein By similarity.
Post-translational modification	Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking p62 signal peptide. The remaining polyprotein is then targeted to the endoplasmic reticulum, where host signal peptidase cleaves it into p62, 6K and E1 proteins. p62 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle. Protein processing process takes about 30 minutes at physiologic temperatures. The folding of the p62/6K/E1 precursor requires the formation of intrachain disulfide bonds and has been shown to involve a transient covalent interaction between the nascent and newly synthesized heterodimer and the host-cell chaperones, P4HB/PDI and PDIA3/ERp57. The folding pathway also includes non covalent interaction with human CANX/calnexin and CALR/calreticulin. Ref.6 Ref.8 Ref.13 Ref.16 Envelope E1, E2 and E3 proteins are N-glycosylated. Ref.20 E2 is palmitoylated via thioester bonds. These palmitoylations may induce disruption of the C-terminus transmembrane. This would result in the reorientation of E2 c-terminus from lumenal to cytoplasmic side. 6K protein is also palmitoylated with about four covalently bound fatty acids per molecule. E1 is stearoylated. Ref.5
Miscellaneous	The mature virion nucleocapsid consists of 240 copies of the capsid protein. 80 spike trimers of E1 and E2 are present at the surface of mature virion. They project about 100 Angstroms from the outer surface and are located at the local and strict three fold axis of the icosaedral lattice. The glycoproteins splay out to form a protein shell or skirt covering most of the outer surface of the membrane bilayer. Structural polyprotein is translated from a subgenomic RNA synthesized during togavirus replication.
Sequence similarities	Contains 1 peptidase S3 domain.

Ontologies

Keywords
Cellular component	Capsid protein Cell membrane Cytoplasm Membrane Virion
Domain	Signal Transmembrane
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: InterPro virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 267

267

Capsid protein

PRO_0000041311

Chain

268 – 755

488

p62

PRO_0000226237

Chain

268 – 333

66

E3 protein

PRO_0000041312

Signal peptide

268 – 282

15

Not cleaved Potential

Chain

334 – 755

422

E2 envelope glycoprotein

PRO_0000041313

Chain

756 – 815

60

6K protein

PRO_0000041314

Chain

816 – 1253

438

E1 envelope glycoprotein

PRO_0000041315

Regions

Topological domain

268 – 701

434

Extracellular Potential

Transmembrane

702 – 722

21

Potential

Topological domain

723 – 755

33

Cytoplasmic Potential

Topological domain

756 – 770

15

Extracellular Potential

Transmembrane

771 – 791

21

Potential

Topological domain

792

1

Cytoplasmic Potential

Transmembrane

793 – 813

21

Potential

Topological domain

814 – 1230

417

Extracellular Potential

Transmembrane

1231 – 1251

21

Potential

Topological domain

1252 – 1253

2

Cytoplasmic Potential

Domain

112 – 267

156

Peptidase S3

Region

1 – 113

113

Intrinsically disordered, in contact with genomic RNA in nucleocapsid Potential

Region

94 – 106

13

Ribosome-binding

Region

728 – 748

21

Transient transmembrane before p62-6K protein processing Potential

Region

899 – 916

18

E1 fusion peptide loop

Sites

Active site

145

1

Charge relay system By similarity

Active site

151

1

Charge relay system By similarity

Active site

219

1

Charge relay system By similarity

Site

267 – 268

2

Cleavage; by capsid protein

Site

333 – 334

2

Cleavage; by host furin

Site

755 – 756

2

Cleavage; by host signal peptidase

Site

815 – 816

2

Cleavage; by host signal peptidase

Amino acid modifications

Lipidation

718

1

S-palmitoyl cysteine; by host Potential

Lipidation

728

1

S-palmitoyl cysteine; by host By similarity

Lipidation

748

1

S-palmitoyl cysteine; by host By similarity

Lipidation

749

1

S-palmitoyl cysteine; by host By similarity

Lipidation

1248

1

S-stearoyl cysteine; by host

Glycosylation

280

1

N-linked (GlcNAc...); by host Potential

Glycosylation

327

1

N-linked (GlcNAc...); by host Potential

Glycosylation

533

1

N-linked (GlcNAc...); by host Potential

Glycosylation

595

1

N-linked (GlcNAc...); by host Potential

Glycosylation

956

1

N-linked (GlcNAc...); by host Ref.20

Disulfide bond

119 ↔ 134

Ref.20 Ref.18

Disulfide bond

864 ↔ 929

Ref.20 Ref.18

Disulfide bond

877 ↔ 909

Ref.20 Ref.18

Disulfide bond

878 ↔ 911

Ref.20 Ref.18

Disulfide bond

883 ↔ 893

Ref.20 Ref.18

Disulfide bond

1074 ↔ 1086

Ref.20 Ref.18

Disulfide bond

1116 ↔ 1191

Ref.20 Ref.18

Disulfide bond

1121 ↔ 1195

Ref.20 Ref.18

Disulfide bond

1143 ↔ 1185

Ref.20 Ref.18

Experimental info

Mutagenesis

267

1

W → A or R: Complete loss of cleavage by capsid protease.

Mutagenesis

330

1

R → S: Complete loss of p62 precursor processing. Ref.6

Mutagenesis

333

1

R → F: Complete loss of p62 precursor processing. Ref.6

Mutagenesis

755

1

A → F: Complete loss of p62 precursor-6K cleavage. Ref.8

Mutagenesis

815

1

A → F: Complete loss of 6K protein-E1 envelope glycoprotein cleavage. Ref.8

Mutagenesis

859

1

L → F: E1 fusion is less cholesterol and sphingolipid dependent. Ref.15

Mutagenesis

890

1

D → A: Shifts the pH threshold for fusion to a more acidic range. Ref.7

Mutagenesis

894

1

K → Q: No effect on E1 fusion activity. Ref.7

Mutagenesis

898

1

G → A: Shifts the pH threshold for fusion to a more acidic range. Ref.7 Ref.12

Mutagenesis

898

1

G → D: No effect on E1 fusion activity. Ref.7 Ref.12

Mutagenesis

901

1

P → D: Retention of E1 protein in endoplasmic reticulum. Ref.7

Mutagenesis

903

1

M → L: No effect on E1 fusion activity. Ref.7

Mutagenesis

906

1

G → A: Shifts the pH threshold for fusion to a more acidic range. Ref.7 Ref.12

Mutagenesis

906

1

G → D: Complete loss of E1 fusion activity. Ref.7 Ref.12

Mutagenesis

906

1

G → P: Retention of E1 protein in endoplasmic reticulum. Ref.7 Ref.12

Mutagenesis

993

1

V → A: E1 fusion is less cholesterol and sphingolipid dependent. Ref.15

Secondary structure

1

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1253

Helix Strand Turn

Details...

Beta strand

120 – 125

6

Beta strand

128 – 134

7

Beta strand

139 – 141

3

Beta strand

148 – 152

5

Helix

153 – 156

4

Beta strand

161 – 163

3

Turn

164 – 167

4

Beta strand

168 – 172

5

Helix

175 – 180

6

Beta strand

190 – 195

6

Beta strand

198 – 203

6

Beta strand

206 – 210

5

Beta strand

222 – 224

3

Beta strand

230 – 239

10

Beta strand

241 – 251

11

Beta strand

253 – 259

7

Beta strand

818 – 824

7

Beta strand

830 – 834

5

Beta strand

842 – 855

14

Beta strand

861 – 863

3

Beta strand

866 – 869

4

Beta strand

892 – 898

7

Turn

905 – 907

3

Beta strand

911 – 914

4

Beta strand

916 – 925

10

Helix

929 – 931

3

Beta strand

934 – 937

4

Beta strand

941 – 952

12

Beta strand

955 – 961

7

Beta strand

963 – 965

3

Beta strand

968 – 971

4

Beta strand

974 – 977

4

Beta strand

990 – 994

5

Helix

1007 – 1009

3

Beta strand

1017 – 1022

6

Beta strand

1041 – 1043

3

Helix

1054 – 1061

8

Helix

1066 – 1068

3

Beta strand

1075 – 1077

3

Turn

1078 – 1081

4

Beta strand

1082 – 1085

4

Beta strand

1090 – 1097

8

Turn

1099 – 1101

3

Beta strand

1111 – 1122

12

Beta strand

1129 – 1139

11

Beta strand

1141 – 1148

8

Beta strand

1153 – 1155

3

Beta strand

1157 – 1161

5

Beta strand

1166 – 1172

7

Beta strand

1174 – 1177

4

Beta strand

1179 – 1184

6

Beta strand

1187 – 1192

6

Sequences

	Sequence		Length	Mass (Da)
	P03315-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 2A73228D08B82AC5	FASTA	1,253	138,017
	10 20 30 40 50 60 MNYIPTQTFY GRRWRPRPAA RPWPLQATPV APVVPDFQAQ QMQQLISAVN ALTMRQNAIA 70 80 90 100 110 120 PARPPKPKKK KTTKPKPKTQ PKKINGKTQQ QKKKDKQADK KKKKPGKRER MCMKIENDCI 130 140 150 160 170 180 FEVKHEGKVT GYACLVGDKV MKPAHVKGVI DNADLAKLAF KKSSKYDLEC AQIPVHMRSD 190 200 210 220 230 240 ASKYTHEKPE GHYNWHHGAV QYSGGRFTIP TGAGKPGDSG RPIFDNKGRV VAIVLGGANE 250 260 270 280 290 300 GSRTALSVVT WNKDMVTRVT PEGSEEWSAP LITAMCVLAN ATFPCFQPPC VPCCYENNAE 310 320 330 340 350 360 ATLRMLEDNV DRPGYYDLLQ AALTCRNGTR HRRSVSQHFN VYKATRPYIA YCADCGAGHS 370 380 390 400 410 420 CHSPVAIEAV RSEATDGMLK IQFSAQIGID KSDNHDYTKI RYADGHAIEN AVRSSLKVAT 430 440 450 460 470 480 SGDCFVHGTM GHFILAKCPP GEFLQVSIQD TRNAVRACRI QYHHDPQPVG REKFTIRPHY 490 500 510 520 530 540 GKEIPCTTYQ QTTAETVEEI DMHMPPDTPD RTLLSQQSGN VKITVGGKKV KYNCTCGTGN 550 560 570 580 590 600 VGTTNSDMTI NTCLIEQCHV SVTDHKKWQF NSPFVPRADE PARKGKVHIP FPLDNITCRV 610 620 630 640 650 660 PMAREPTVIH GKREVTLHLH PDHPTLFSYR TLGEDPQYHE EWVTAAVERT IPVPVDGMEY 670 680 690 700 710 720 HWGNNDPVRL WSQLTTEGKP HGWPHQIVQY YYGLYPAATV SAVVGMSLLA LISIFASCYM 730 740 750 760 770 780 LVAARSKCLT PYALTPGAAV PWTLGILCCA PRAHAASVAE TMAYLWDQNQ ALFWLEFAAP 790 800 810 820 830 840 VACILIITYC LRNVLCCCKS LSFLVLLSLG ATARAYEHST VMPNVVGFPY KAHIERPGYS 850 860 870 880 890 900 PLTLQMQVVE TSLEPTLNLE YITCEYKTVV PSPYVKCCGA SECSTKEKPD YQCKVYTGVY 910 920 930 940 950 960 PFMWGGAYCF CDSENTQLSE AYVDRSDVCR HDHASAYKAH TASLKAKVRV MYGNVNQTVD 970 980 990 1000 1010 1020 VYVNGDHAVT IGGTQFIFGP LSSAWTPFDN KIVVYKDEVF NQDFPPYGSG QPGRFGDIQS 1030 1040 1050 1060 1070 1080 RTVESNDLYA NTALKLARPS PGMVHVPYTQ TPSGFKYWLK EKGTALNTKA PFGCQIKTNP 1090 1100 1110 1120 1130 1140 VRAMNCAVGN IPVSMNLPDS AFTRIVEAPT IIDLTCTVAT CTHSSDFGGV LTLTYKTNKN 1150 1160 1170 1180 1190 1200 GDCSVHSHSN VATLQEATAK VKTAGKVTLH FSTASASPSF VVSLCSARAT CSASCEPPKD 1210 1220 1230 1240 1250 HIVPYAASHS NVVFPDMSGT ALSWVQKISG GLGAFAIGAI LVLVVVTCIG LRR

References

[1]	"The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region." Garoff H., Frischauf A.-M., Simons K., Lehrach H., Delius H. Proc. Natl. Acad. Sci. U.S.A. 77:6376-6380(1980) [PubMed: 6935652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-305.
[2]	"Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins." Garoff H., Frischauf A.-M., Simons K., Lehrach H., Delius H. Nature 288:236-241(1980) [PubMed: 6985476] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 266-1253.
[3]	"Carboxyl-terminal sequence analysis of the four structural proteins of Semliki Forest virus." Kalkkinen N. FEBS Lett. 115:163-166(1980) [PubMed: 7398872] [Abstract] Cited for: PROTEIN SEQUENCE OF C-TERMINUS FOR CAPSID PROTEIN; E3 PROTEIN; E2 ENVELOPE GLYCOPROTEIN; 6K PROTEIN AND E1 ENVELOPE GLYCOPROTEIN.
[4]	"An evolutionary tree relating eight alphaviruses, based on amino-terminal sequences of their glycoproteins." Bell J.R., Kinney R.M., Trent D.W., Strauss E.G., Strauss J.H. Proc. Natl. Acad. Sci. U.S.A. 81:4702-4706(1984) [PubMed: 6087344] [Abstract] Cited for: PROTEIN SEQUENCE OF 334-402 AND 816-881.
[5]	"Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki Forest virus E1)." Schmidt M., Schmidt M.F., Rott R. J. Biol. Chem. 263:18635-18639(1988) [PubMed: 3143715] [Abstract] Cited for: STEAROYLATION AT CYS-1248, PALMITOYLATION.
[6]	"Processing of the p62 envelope precursor protein of Semliki Forest virus." Jain S.K., DeCandido S., Kielian M. J. Biol. Chem. 266:5756-5761(1991) [PubMed: 2005112] [Abstract] Cited for: CLEAVAGE SITE OF P62, MUTAGENESIS OF ARG-330 AND ARG-333.
[7]	"Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein." Levy-Mintz P., Kielian M. J. Virol. 65:4292-4300(1991) [PubMed: 2072453] [Abstract] Cited for: MUTAGENESIS OF ASP-890; LYS-894; GLY-898; PRO-901; MET-903 AND GLY-906.
[8]	"Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor." Liljestrom P., Garoff H. J. Virol. 65:147-154(1991) [PubMed: 1985194] [Abstract] Cited for: CLEAVAGE BY SIGNAL PEPTIDASE, MUTAGENESIS OF ALA-755 AND ALA-815.
[9]	"Fate of the 6K membrane protein of Semliki Forest virus during virus assembly." Lusa S., Garoff H., Liljestrom P. Virology 185:843-846(1991) [PubMed: 1962454] [Abstract] Cited for: FUNCTION OF 6K PROTEIN.
[10]	"Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein." Wahlberg J.M., Bron R., Wilschut J., Garoff H. J. Virol. 66:7309-7318(1992) [PubMed: 1433520] [Abstract] Cited for: FUNCTION OF E1 PROTEIN.
[11]	"The 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding process." Loewy A., Smyth J., von Bonsdorff C.H., Liljestrom P., Schlesinger M.J. J. Virol. 69:469-475(1995) [PubMed: 7983743] [Abstract] Cited for: FUNCTION OF 6K PROTEIN.
[12]	"A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit." Vashishtha M., Phalen T., Marquardt M.T., Ryu J.S., Ng A.C., Kielian M. J. Cell Biol. 140:91-99(1998) [PubMed: 9425157] [Abstract] Cited for: MUTAGENESIS OF GLY-898 AND GLY-906.
[13]	"Role of the C-terminal tryptophan residue for the structure-function of the alphavirus capsid protein." Skoging U., Liljestrom P. J. Mol. Biol. 279:865-872(1998) [PubMed: 9642067] [Abstract] Cited for: AUTOPROTEOLYTIC CLEAVAGE BY CAPSID PROTEIN.
[14]	"Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells." Molinari M., Helenius A. Nature 402:90-93(1999) [PubMed: 10573423] [Abstract] Cited for: INTERACTION WITH HUMAN CHAPERONES P4HB/PDI AND PDIA3/ERP57.
[15]	"Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion protein." Chatterjee P.K., Eng C.H., Kielian M. J. Virol. 76:12712-12722(2002) [PubMed: 12438597] [Abstract] Cited for: MUTAGENESIS OF LEU-859 AND VAL-993.
[16]	"Furin processing and proteolytic activation of Semliki Forest virus." Zhang X., Fugere M., Day R., Kielian M. J. Virol. 77:2981-2989(2003) [PubMed: 12584323] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF P62 BY HOST FURIN.
[17]	"Structure of Semliki Forest virus core protein." Choi H.-K., Lu G., Lee S., Wengler G., Rossmann M.G. Proteins 27:345-359(1997) [PubMed: 9094737] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 119-267.
[18]	"Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus." Mancini E.J., Clarke M., Gowen B.E., Rutten T., Fuller S.D. Mol. Cell 5:255-266(2000) [PubMed: 10882067] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 119-267, DISULFIDE BONDS.
[19]	"The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH." Lescar J., Roussel A., Wien M.W., Navaza J., Fuller S.D., Wengler G., Wengler G., Rey F.A. Cell 105:137-148(2001) [PubMed: 11301009] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 816-1205.
[20]	"Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus." Gibbons D.L., Vaney M.C., Roussel A., Vigouroux A., Reilly B., Lepault J., Kielian M., Rey F.A. Nature 427:320-325(2004) [PubMed: 14737160] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 816-1206, GLYCOSYLATION AT ASN-956, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBLGenBankDDBJ

X04129 Genomic RNA. Translation: CAA27742.1. Sequence problems.

PIR

VHWV. A93861.

RefSeq

NP_463458.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DYL	electron microscopy	9.00	A/B/C/D	119-267	[»]
1I9W	X-ray	3.00	A	816-1205	[»]
1RER	X-ray	3.20	A/B/C	816-1206	[»]
1VCP	X-ray	3.00	A/B/C	119-267	[»]
1VCQ	X-ray	3.10	A/B	119-267	[»]
2ALA	X-ray	3.00	A	816-1206	[»]
2V33	X-ray	1.55	A/B	1107-1197	[»]

ModBase

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Protein family/group databases

MEROPS

S03.001.

TCDB

1.H.4.1.1. viral pore-forming membrane fusion protein-4 (VMFP4) family.

Genome annotation databases

GeneID

922351.

Family and domain databases

InterPro

IPR002548. Alpha_E1_glycop.
IPR000936. Alpha_E2_glycop.
IPR002533. Alpha_E3_glycop.
IPR000930. Peptidase_S3.
[Graphical view]

Pfam

PF01589. Alpha_E1_glycop. 1 hit.
PF00943. Alpha_E2_glycop. 1 hit.
PF01563. Alpha_E3_glycop. 1 hit.
PF00944. Peptidase_S3. 1 hit.
[Graphical view]

PRINTS

PR00798. TOGAVIRIN.

ProtoNet

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Entry information

Entry name

POLS_SFV

Accession

Primary (citable) accession number: P03315

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)