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| 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 | calcium(2+), monoatomic monocation |
Cross database links:
| RefSeq: | NP_463458.1 |
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| Entrez Gene ID: | 922351 |
| Pfam: | PF01589 PF00943 PF01563 PF00944 |
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
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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 | |
| Structure: | |
External Searches:
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Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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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