1.A.6.3.2
FMRFamide (peptide)-gated sodium channel, FaNaC. The charge on aspartate-552 in TMS2 influcences the gating properties and potency of the channel (Kodani and Furukawa 2010; Kodani and Furukawa 2014). The FMRFamide-evoked current through AkFaNaC was depressed 2-3-fold by millimolar (1.8 mM) Ca2+ (Fujimoto et al. 2017). Both D552 and D556 were indispensable for the sensitivity of FaNaC to millimolar Ca2+. The Ca2+-sensitive gating was recapitulated by an allosteric model in which Ca2+-bound channels are more difficult to open. The desensitization of FaNaC was also inhibited by Ca2+ (Fujimoto et al. 2017).
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| Accession Number: | Q4H3X6 |
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| Protein Name: | FMRFamide-gated Na+ channel |
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| Length: | 653 |
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| Molecular Weight: | 73978.00 |
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| Species: | Aplysia kurodai (Kuroda's sea hare) [6501] |
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| Number of TMSs: | 2 |
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| Substrate |
sodium(1+) |
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1: MLGRGERIKP YHFRDSSADH MKYTSVAAKS GMVPEHRYTM VRSRHHGRHH HHHSYQEYNT
61: QRSAISLIAE LGSESNAHGL AKIVTSRDTK RKVIWALMVI IGFTAATLQL SLLVRKYLQF
121: QVVELSEIKD SMPVEYPSVT ICNIEPISLR KIRKAYNKNE SQNLKDWLNF TQTFHFKDMS
181: FMNSIRAFYE NLGTDAKKIS HDLRDLLIHC RFNREECTTE NFTSSFDGNY FNCFTFNGGQ
241: LRDQLQMHAT GPENGLSLII SIEKDEPLPG TYGVYNFENN ILHSAGVRVV VHAPGSMPSP
301: VDHGFDIPPG YSSSVGLKAL LHTRLSEPYG NCTEDSLEGI QTYRNTFFAC LQLCKQRRLI
361: RECKCKSSAL PDLSVENITF CGVIPDWKDI RRNVTGEYKM NQTIPTISLA CEARVQKQLN
421: NDRSYETDCG CYQPCSETSY LKSVSLSYWP LEFYQLSALE RFFSQKHPTD QQHFMKIAQD
481: FLSRLAHPQQ QALARNNSHD KDILTTSYSL SEKEMAKEAS DLIRQNLLRL NIYLEDLSVV
541: EYRQLPAYGL ADLFADIGGT LGLWMGISVL TIMELMELII RLFALIFNAE REVPKAPMHN
601: SNNGGSGGGD GSGGQHNFAN GDVEHERDTH FPDLGSSDFD FRRGGGIGAE SPV