1.G.14.1.1 Influenza C virus hemagglutinin-fusion pore-forming protein of 655 aas and 4 TMSS, one N-terminal and three C-terminal but separated by about 100 residues. Pore formation is blocked by human interferon-induced transmembrane proteins such as IFM3 (Q01628) (Desai et al. 2014). The only spike of influenza C virus, the hemagglutinin-esterase-fusion glycoprotein (HEF) combines
receptor binding, receptor hydrolysis and membrane fusion activities in a single protein. Like other hemagglutinating
glycoproteins of influenza viruses, HEF is S-acylated, but only with stearic acid at a single
cysteine located at the cytosol-facing end of the transmembrane region. S-acylation is essential for replication of influenza viruses A, B and C by
affecting budding and/or membrane fusion (Wang et al. 2016).
|
Accession Number: | P07975 |
Protein Name: | Hemagglutinin-esterase-fusion glycoprotein |
Length: | 655 |
Molecular Weight: | 72131.00 |
Species: | Influenza C virus (strain C/Johannesburg/1/1966) [100673] |
Number of TMSs: | 3 |
Location1 / Topology2 / Orientation3: |
Virion membrane1 / Single-pass type I membrane protein2 |
Substrate |
molecule |
---|
1: MFFSLLLVLG LTEAEKIKIC LQKQVNSSFS LHNGFGGNLY ATEEKRMFEL VKPKAGASVL
61: NQSTWIGFGD SRTDKSNSAF PRSADVSAKT ADKFRFLSGG SLMLSMFGPP GKVDYLYQGC
121: GKHKVFYEGV NWSPHAAINC YRKNWTDIKL NFQKNIYELA SQSHCMSLVN ALDKTIPLQV
181: TAGTAGNCNN SFLKNPALYT QEVKPSENKC GKENLAFFTL PTQFGTYECK LHLVASCYFI
241: YDSKEVYNKR GCDNYFQVIY DSFGKVVGGL DNRVSPYTGN SGDTPTMQCD MLQLKPGRYS
301: VRSSPRFLLM PERSYCFDMK EKGPVTAVQS IWGKGRESDY AVDQACLSTP GCMLIQKQKP
361: YIGEADDHHG DQEMRELLSG LDYEARCISQ SGWVNETSPF TEKYLLPPKF GRCPLAAKEE
421: SIPKIPDGLL IPTSGTDTTV TKPKSRIFGI DDLIIGVLFV AIVETGIGGY LLGSRKESGG
481: GVTKESAEKG FEKIGNDIQI LKSSINIAIE KLNDRISHDE QAIRDLTLEI ENARSEALLG
541: ELGIIRALLV GNISIGLQES LWELASEITN RAGDLAVEVS PGCWIIDNNI CDQSCQNFIF
601: KFNETAPVPT IPPLDTKIDL QSDPFYWGSS LGLAITATIS LAALVISGIA ICRTK