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1.G.4.1.1
The Semliki Forest Virus (SFV) (Class II) Structural polyprotein (1253 aas; E1=816-1253 E2=334-774).  The fusion peptide is residues 895 - 913 (Apellániz et al. 2014). The 6K viroporin transports monovalent cations and Ca2+ (Hyser and Estes 2015).

Accession Number:P03315
Protein Name:Structural polyprotein
Length:1253
Molecular Weight:138017.00
Species:Semliki forest virus (SFV) [11033]
Number of TMSs:5
Location1 / Topology2 / Orientation3: Host cell membrane1 / Multi-pass membrane protein2
Substrate Ca2+, monovalent cations

Cross database links:

RefSeq: NP_463458.1   
Entrez Gene ID: 922351   
Pfam: PF01589    PF00943    PF01563    PF00944   
Drugbank: Drugbank Link   

Gene Ontology

GO:0030430 C:host cell cytoplasm
GO:0020002 C:host cell plasma membrane
GO:0016021 C:integral to membrane
GO:0019028 C:viral capsid
GO:0019031 C:viral envelope
GO:0055036 C:virion membrane
GO:0004252 F:serine-type endopeptidase activity
GO:0005198 F:structural molecule activity
GO:0006508 P:proteolysis

References (20)

[1] “The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region.”  Garoff H.et.al.   6935652
[2] “Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins.”  Garoff H.et.al.   6985476
[3] “Carboxyl-terminal sequence analysis of the four structural proteins of Semliki Forest virus.”  Kalkkinen N.et.al.   7398872
[4] “An evolutionary tree relating eight alphaviruses, based on amino-terminal sequences of their glycoproteins.”  Bell J.R.et.al.   6087344
[5] “Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki Forest virus E1).”  Schmidt M.et.al.   3143715
[6] “Processing of the p62 envelope precursor protein of Semliki Forest virus.”  Jain S.K.et.al.   2005112
[7] “Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein.”  Levy-Mintz P.et.al.   2072453
[8] “Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor.”  Liljestrom P.et.al.   1985194
[9] “Fate of the 6K membrane protein of Semliki Forest virus during virus assembly.”  Lusa S.et.al.   1962454
[10] “Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein.”  Wahlberg J.M.et.al.   1433520
[11] “The 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding process.”  Loewy A.et.al.   7983743
[12] “A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit.”  Vashishtha M.et.al.   9425157
[13] “Role of the C-terminal tryptophan residue for the structure-function of the alphavirus capsid protein.”  Skoging U.et.al.   9642067
[14] “Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells.”  Molinari M.et.al.   10573423
[15] “Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion protein.”  Chatterjee P.K.et.al.   12438597
[16] “Furin processing and proteolytic activation of Semliki Forest virus.”  Zhang X.et.al.   12584323
[17] “Structure of Semliki Forest virus core protein.”  Choi H.-K.et.al.   9094737
[18] “Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus.”  Mancini E.J.et.al.   10882067
[19] “The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH.”  Lescar J.et.al.   11301009
[20] “Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus.”  Gibbons D.L.et.al.   14737160
Structure:
1DYL   1I9W   1RER   1VCP   1VCQ   2ALA   2V33     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MNYIPTQTFY GRRWRPRPAA RPWPLQATPV APVVPDFQAQ QMQQLISAVN ALTMRQNAIA 
61:	PARPPKPKKK KTTKPKPKTQ PKKINGKTQQ QKKKDKQADK KKKKPGKRER MCMKIENDCI 
121:	FEVKHEGKVT GYACLVGDKV MKPAHVKGVI DNADLAKLAF KKSSKYDLEC AQIPVHMRSD 
181:	ASKYTHEKPE GHYNWHHGAV QYSGGRFTIP TGAGKPGDSG RPIFDNKGRV VAIVLGGANE 
241:	GSRTALSVVT WNKDMVTRVT PEGSEEWSAP LITAMCVLAN ATFPCFQPPC VPCCYENNAE 
301:	ATLRMLEDNV DRPGYYDLLQ AALTCRNGTR HRRSVSQHFN VYKATRPYIA YCADCGAGHS 
361:	CHSPVAIEAV RSEATDGMLK IQFSAQIGID KSDNHDYTKI RYADGHAIEN AVRSSLKVAT 
421:	SGDCFVHGTM GHFILAKCPP GEFLQVSIQD TRNAVRACRI QYHHDPQPVG REKFTIRPHY 
481:	GKEIPCTTYQ QTTAETVEEI DMHMPPDTPD RTLLSQQSGN VKITVGGKKV KYNCTCGTGN 
541:	VGTTNSDMTI NTCLIEQCHV SVTDHKKWQF NSPFVPRADE PARKGKVHIP FPLDNITCRV 
601:	PMAREPTVIH GKREVTLHLH PDHPTLFSYR TLGEDPQYHE EWVTAAVERT IPVPVDGMEY 
661:	HWGNNDPVRL WSQLTTEGKP HGWPHQIVQY YYGLYPAATV SAVVGMSLLA LISIFASCYM 
721:	LVAARSKCLT PYALTPGAAV PWTLGILCCA PRAHAASVAE TMAYLWDQNQ ALFWLEFAAP 
781:	VACILIITYC LRNVLCCCKS LSFLVLLSLG ATARAYEHST VMPNVVGFPY KAHIERPGYS 
841:	PLTLQMQVVE TSLEPTLNLE YITCEYKTVV PSPYVKCCGA SECSTKEKPD YQCKVYTGVY 
901:	PFMWGGAYCF CDSENTQLSE AYVDRSDVCR HDHASAYKAH TASLKAKVRV MYGNVNQTVD 
961:	VYVNGDHAVT IGGTQFIFGP LSSAWTPFDN KIVVYKDEVF NQDFPPYGSG QPGRFGDIQS 
1021:	RTVESNDLYA NTALKLARPS PGMVHVPYTQ TPSGFKYWLK EKGTALNTKA PFGCQIKTNP 
1081:	VRAMNCAVGN IPVSMNLPDS AFTRIVEAPT IIDLTCTVAT CTHSSDFGGV LTLTYKTNKN 
1141:	GDCSVHSHSN VATLQEATAK VKTAGKVTLH FSTASASPSF VVSLCSARAT CSASCEPPKD 
1201:	HIVPYAASHS NVVFPDMSGT ALSWVQKISG GLGAFAIGAI LVLVVVTCIG LRR