Q53496 (BACR_HALSR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cruxrhodopsin-2
Short name=COP-2
Short name=CR-2

Gene names

Name:

cop2

Organism

Haloarcula sp. (strain arg-2 / Andes heights)

Taxonomic identifier

69009 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Light-driven proton pump. May generate a protonmotive force sufficient to synthesize ATP in the light.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the archaeal/bacterial/fungal opsin family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Sensory transduction Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Chromophore
Molecular function	Photoreceptor protein Receptor Retinal protein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	phototransduction Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW proton transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ion channel activity Inferred from electronic annotation. Source: InterPro photoreceptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 255	255	Cruxrhodopsin-2		PRO_0000196274
Regions
	Topological domain	1 – 15	15	Extracellular By similarity
	Transmembrane	16 – 34	19	Helical; Name=Helix A; By similarity
	Topological domain	35 – 48	14	Cytoplasmic By similarity
	Transmembrane	49 – 67	19	Helical; Name=Helix B; By similarity
	Topological domain	68 – 83	16	Extracellular By similarity
	Transmembrane	84 – 101	18	Helical; Name=Helix C; By similarity
	Topological domain	102 – 112	11	Cytoplasmic By similarity
	Transmembrane	113 – 132	20	Helical; Name=Helix D; By similarity
	Topological domain	133 – 145	13	Extracellular By similarity
	Transmembrane	146 – 165	20	Helical; Name=Helix E; By similarity
	Topological domain	166 – 183	18	Cytoplasmic By similarity
	Transmembrane	184 – 202	19	Helical; Name=Helix F; By similarity
	Topological domain	203 – 214	12	Extracellular By similarity
	Transmembrane	215 – 234	20	Helical; Name=Helix G; By similarity
	Topological domain	235 – 255	21	Cytoplasmic By similarity
Sites
	Site	90	1	Primary proton acceptor By similarity
Amino acid modifications
	Modified residue	227	1	N6-(retinylidene)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q53496 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E665DDE946475708	FASTA	255	27,545
	10 20 30 40 50 60 MLQSGMSTYV PGGESIFLWV GTAGMFLGML YFIARGWSVS DQRRQKFYIA TIMIAAIAFV 70 80 90 100 110 120 NYLSMALGFG VTTIELGGEE RAIYWARYTD WLFTTPLLLY DLALLAGADR NTIYSLVGLD 130 140 150 160 170 180 VLMIGTGALA TLSAGSGVLP AGAERLVWWG ISTGFLLVLL YFLFSNLTDR ASELSGDLQS 190 200 210 220 230 240 KFSTLRNLVL VLWLVYPVLW LVGTEGLGLV GLPIETAAFM VLDLTAKIGF GIILLQSHAV 250 LDEGQTASEG AAVAD

References

[1]	"The light-driven proton pump, cruxrhodopsin-2 in Haloarcula sp. arg-2 (bR+, hR-), and its coupled ATP formation." Sugiyama Y., Yamada N., Mukohata Y. Biochim. Biophys. Acta 1188:287-292(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 47-67.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S76743 Genomic DNA. Translation: AAB32951.1.
3D structure databases
ProteinModelPortal	Q53496.
SMR	Q53496. Positions 13-235.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001425. Rhodopsin_arc/bac/fun. IPR018229. Rhodopsin_retinal_BS. [Graphical view]
Pfam	PF01036. Bac_rhodopsin. 1 hit. [Graphical view]
PRINTS	PR00251. BACTRLOPSIN.
SMART	SM01021. Bac_rhodopsin. 1 hit. [Graphical view]
PROSITE	PS00950. BACTERIAL_OPSIN_1. 1 hit. PS00327. BACTERIAL_OPSIN_RET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BACR_HALSR

Accession

Primary (citable) accession number: Q53496

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program