3.E.1.5.2
Learning/memory process protein of 704 aas and 7 N-terminal TMSs as the rhodopsin (Rh) domain with a C-terminal cyclic nucleotide phosphodiesterase (PDE) domain. The Rh-PDE enzyme light-dependently decreases the concentrations of cyclic nucleotides such as cGMP and cAMP. Photoexcitation of purified full-length Rh-PDE yields an "M" intermediate with a deprotonated Schiff base; its recovery is much faster than that of the enzyme domain (Watari et al. 2019). Mechanistic insights into rhodopsin-mediated, light-dependent regulation of second-messenger levels have thus been revealed (Watari et al. 2019).
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| Accession Number: | EGD79054.1 |
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| Protein Name: | EGD79054.1 learning/memory process protein [Salpingoeca rosetta] |
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| Length: | 705 |
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| Molecular Weight: | |
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| Species: | Salpingoeca rosetta [946362] |
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| Number of TMSs: | 5 |
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| Substrate |
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1: MGRKNAANSS MLQEASMNNY SMTSAASGAS SSGRGKRRAK TRNIAIASTK EVQWQGIFMI
61: IVWLCVMGSL IFFANPEASR RVFAKFSHLQ SFYGATSVAF AFATGLDILA YVNAVSDEKR
121: VLSGILAYVD GVACISYLSM ATLNLYFLVD STQGNPVWLM RYAEWIITCP TLLYWCGLAS
181: RADRSSVSDI ATADALLLAG GALSSILPSW PAFFVFAGSF ATYIYVMLHM WGMFGKAMQP
241: DFQPPPPLPR HALHLLRCEI VMSWSIFPLV EFLRRQGYID FQVGEAMNCV ADYAAKVGLA
301: MIMVNCNLEQ INALRVQQMH SALTGMLKVM RKTNLSSSRM AQLDGVDDDV KSWIMNEFSG
361: STDGKGGDDA KAQQRARGRK GHSAAMDAEK LAASSLFTWD FDALDKSDED LTAVCVRVFQ
421: ELHVIEQFNI DEKKLRKWLQ KVRTQYNKNP FHNWRHAVMV LHTTYLLLTS VATEFITEVE
481: LLAMLIAALS HDLDHNGLTN AFHINSRSEL ALVYNDQSVL ENHHSHLAFE ILLEKGCNVV
541: ENLDEDEFKR LRAVIINCIL NTDMATHHTK LSKMEEVNRL GGFINLAENN DQRLFVLAVL
601: LHTADLHNPI KPFESNKRWS ARLQKEFNNQ VELEAKMNLP SLPFMRGNDE ESLAKGEIGF
661: INFVVKPWHQ QLSQAFPKLD FLLDTIDANL AEWKAIAESY RQMH