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3.E.1.7.1
Channelrhodopsin-1 (chlamyrhodopsin-3) (ChR1; Cop3; CSOA) (light-gated cation (H+, Na+, K+, and Ca2+) channel) (Nagel et al., 2003). TMSs 1 and 2 are the main structures involved in desensitization involving the stabilization of the protein's conformation and the alteration of the charge distribution around the retinal-Schiff base (Zamani et al. 2017). Replacing the glutamate located at the central gate of the ion channel with positively charged amino acyl residues reverses the ion selectivity and allows anion (chloride, Cl-) conduction (Zhang et al. 2019).

Accession Number:Q93WP2
Protein Name:ACOP1
Length:712
Molecular Weight:76442.00
Species:Chlamydomonas reinhardtii [3055]
Number of TMSs:10
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate protons

Cross database links:

Pfam: PF01036   

Gene Ontology

GO:0016020 C:membrane
GO:0005216 F:ion channel activity
GO:0006811 P:ion transport

References (1)

[1] “Channelrhodopsin-1: a light-gated proton channel in green algae.”  Nagel G.et.al.   12089443
Structure:
3UG9     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSRRPWLLAL ALAVALAAGS AGASTGSDAT VPVATQDGPD YVFHRAHERM LFQTSYTLEN 
61:	NGSVICIPNN GQCFCLAWLK SNGTNAEKLA ANILQWITFA LSALCLMFYG YQTWKSTCGW 
121:	EEIYVATIEM IKFIIEYFHE FDEPAVIYSS NGNKTVWLRY AEWLLTCPVI LIHLSNLTGL 
181:	ANDYNKRTMG LLVSDIGTIV WGTTAALSKG YVRVIFFLMG LCYGIYTFFN AAKVYIEAYH 
241:	TVPKGICRDL VRYLAWLYFC SWAMFPVLFL LGPEGFGHIN QFNSAIAHAI LDLASKNAWS 
301:	MMGHFLRVKI HEHILLYGDI RKKQKVNVAG QEMEVETMVH EEDDETQKVP TAKYANRDSF 
361:	IIMRDRLKEK GFETRASLDG DPNGDAEANA AAGGKPGMEM GKMTGMGMGM GAGMGMATID 
421:	SGRVILAVPD ISMVDFFREQ FARLPVPYEL VPALGAENTL QLVQQAQSLG GCDFVLMHPE 
481:	FLRDRSPTGL LPRLKMGGQR AAAFGWAAIG PMRDLIEGSG VDGWLEGPSF GAGINQQALV 
541:	ALINRMQQAK KMGMMGGMGM GMGGGMGMGM GMGMGMAPSM NAGMTGGMGG ASMGGAVMGM 
601:	GMGMQPMQQA MPAMSPMMTQ QPSMMSQPSA MSAGGAMQAM GGVMPSPAPG GRVGTNPLFG 
661:	SAPSPLSSQP GISPGMATPP AATAAPAAGG SEAEMLQQLM SEINRLKNEL GE