NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907103530|ref|XP_036014666|]
View 

RPE-retinal G protein-coupled receptor isoform X3 [Mus musculus]

Protein Classification

G protein-coupled receptor family protein( domain architecture ID 705710)

G protein-coupled receptor family protein is a seven-transmembrane G protein-coupled receptor (7TM-GPCR) family protein which typically transmits an extracellular signal into the cell by the conformational rearrangement of the 7TM helices and by the subsequent binding and activation of an intracellular heterotrimeric G protein; GPCR ligands include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
13-144 5.44e-70

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


The actual alignment was detected with superfamily member cd15072:

Pssm-ID: 475119 [Multi-domain]  Cd Length: 260  Bit Score: 211.45  E-value: 5.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  13 RQLAWDTAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFME 92
Cdd:cd15072   105 SKLQWSTAISLVLFVWLFSAFWAAMPLLGWGEYDYEPLGTCCTLDYSKGDRNYVSYLFTMAFFNFILPLFILLTSYSSIE 184
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907103530  93 QKFSRSGHLPVNTTLPGRMLLLGWGPYALLYLYAAIADVSFISPKLQMVQIL 144
Cdd:cd15072   185 QKLKKEGHLRFNTGLPLLTLLICWGPYAILALYAAITDVTSISPKLRMVPAL 236
 
Name Accession Description Interval E-value
7tmA_Retinal_GPR cd15072
retinal G protein coupled receptor, member of the class A family of seven-transmembrane G ...
13-144 5.44e-70

retinal G protein coupled receptor, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represents the retinal G-protein coupled receptor (RGR) found exclusively in retinal pigment epithelium (RPE) and Muller cells. RGR is a member of the class A rhodopsin-like receptor family. As with other opsins, RGR binds all-trans retinal and contains a conserved lysine reside on the seventh helix. RGR functions as a photoisomerase to catalyze the conversion of all-trans-retinal to 11-cis-retinal. Two mutations in RGR gene are found in patients with retinitis pigmentosa, indicating that RGR is essential to the visual process.


Pssm-ID: 320200 [Multi-domain]  Cd Length: 260  Bit Score: 211.45  E-value: 5.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  13 RQLAWDTAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFME 92
Cdd:cd15072   105 SKLQWSTAISLVLFVWLFSAFWAAMPLLGWGEYDYEPLGTCCTLDYSKGDRNYVSYLFTMAFFNFILPLFILLTSYSSIE 184
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907103530  93 QKFSRSGHLPVNTTLPGRMLLLGWGPYALLYLYAAIADVSFISPKLQMVQIL 144
Cdd:cd15072   185 QKLKKEGHLRFNTGLPLLTLLICWGPYAILALYAAITDVTSISPKLRMVPAL 236
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
6-129 1.31e-04

7 transmembrane receptor (rhodopsin family); This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins.


Pssm-ID: 459624 [Multi-domain]  Cd Length: 256  Bit Score: 40.36  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530   6 RYPASSGRQLAWdtaiPLVLFVWMSSAFWASLPL-MGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFIT 84
Cdd:pfam00001  92 RYKRRRTPRRAK----VLILVIWVLALLLSLPPLlFGWTLTVPEGNVTVCFIDFPEDLSKPVSYTLLISVLGFLLPLLVI 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907103530  85 HTSY-------RFMEQKFSRSGHLPVNTTLpGRMLL-------LGWGPYALLYLYAAIA 129
Cdd:pfam00001 168 LVCYtliirtlRKSASKQKSSERTQRRRKA-LKTLAvvvvvfiLCWLPYHIVNLLDSLA 225
 
Name Accession Description Interval E-value
7tmA_Retinal_GPR cd15072
retinal G protein coupled receptor, member of the class A family of seven-transmembrane G ...
13-144 5.44e-70

retinal G protein coupled receptor, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represents the retinal G-protein coupled receptor (RGR) found exclusively in retinal pigment epithelium (RPE) and Muller cells. RGR is a member of the class A rhodopsin-like receptor family. As with other opsins, RGR binds all-trans retinal and contains a conserved lysine reside on the seventh helix. RGR functions as a photoisomerase to catalyze the conversion of all-trans-retinal to 11-cis-retinal. Two mutations in RGR gene are found in patients with retinitis pigmentosa, indicating that RGR is essential to the visual process.


Pssm-ID: 320200 [Multi-domain]  Cd Length: 260  Bit Score: 211.45  E-value: 5.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  13 RQLAWDTAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFME 92
Cdd:cd15072   105 SKLQWSTAISLVLFVWLFSAFWAAMPLLGWGEYDYEPLGTCCTLDYSKGDRNYVSYLFTMAFFNFILPLFILLTSYSSIE 184
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907103530  93 QKFSRSGHLPVNTTLPGRMLLLGWGPYALLYLYAAIADVSFISPKLQMVQIL 144
Cdd:cd15072   185 QKLKKEGHLRFNTGLPLLTLLICWGPYAILALYAAITDVTSISPKLRMVPAL 236
7tmA_Peropsin cd15073
retinal pigment epithelium-derived rhodopsin homolog, member of the class A family of ...
12-141 1.60e-21

retinal pigment epithelium-derived rhodopsin homolog, member of the class A family of seven-transmembrane G protein-coupled receptors; Peropsin, also known as a retinal pigment epithelium-derived rhodopsin homolog (RRH), is a visual pigment-like protein found exclusively in the apical microvilli of the retinal pigment epithelium. Peropsin belongs to the type 2 opsin family of the class A G-protein coupled receptors. Peropsin presumably plays a physiological role in the retinal pigment epithelium either by detecting light directly or monitoring the levels of retinoids, the primary light absorber in visual perception, or other pigment-related compounds in the eye.


Pssm-ID: 320201 [Multi-domain]  Cd Length: 280  Bit Score: 87.48  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  12 GRQLAWDTAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFM 91
Cdd:cd15073   108 GRKMTTNTYTVMILLAWTNAFFWAAMPLVGWASYALDPTGATCTINWRKNDSSFVSYTMSVIVVNFIVPLAVMFYCYYNV 187
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907103530  92 EQ---KFSRSGHLPVNTTLPGR-------------MLLLGWGPYALLYLYAAIADVSFISPKLQMV 141
Cdd:cd15073   188 SRfvkKVLASDCLESVNIDWTDqndvtkmsvimivMFLVAWSPYSIVCLWASFGEPKKIPPWMAII 253
7tmA_Opsins_type2_animals cd14969
type 2 opsins in animals, member of the class A family of seven-transmembrane G ...
13-141 1.60e-19

type 2 opsins in animals, member of the class A family of seven-transmembrane G protein-coupled receptors; This rhodopsin family represents the type 2 opsins found in vertebrates and invertebrates except sponge. Type 2 opsins primarily function as G protein coupled receptors and are responsible for vision as well as for circadian rhythm and pigment regulation. On the contrary, type 1 opsins such as bacteriorhodopsin and proteorhodopsin are found in both prokaryotic and eukaryotic microbes, functioning as light-gated ion channels, proton pumps, sensory receptors and in other unknown functions. Although these two opsin types share seven-transmembrane domain topology and a conserved lysine reside in the seventh helix, type 1 opsins do not activate G-proteins and are not evolutionarily related to type 2. Type 2 opsins can be classified into six distinct subfamilies including the vertebrate opsins/encephalopsins, the G(o) opsins, the G(s) opsins, the invertebrate G(q) opsins, the photoisomerases, and the neuropsins.


Pssm-ID: 381741 [Multi-domain]  Cd Length: 284  Bit Score: 82.25  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  13 RQLAWDTAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSY---- 88
Cdd:cd14969   109 FRLSKRRALILIAFIWLYGLFWALPPLFGWSSYVPEGGGTSCSVDWYSKDPNSLSYIVSLFVFCFFLPLAIIIFCYykiy 188
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907103530  89 RFMEQKFSRSGHLPVNTTLPGR----------------MLLLGWGPYALLYLYAAIADVSFISPKLQMV 141
Cdd:cd14969   189 RTLRKMSKRAARRKNSAITKRTkkaekkvakmvlvmivAFLIAWTPYAVVSLYVSFGGESTIPPLLATI 257
7tmA_Opsin5_neuropsin cd15074
neuropsin (Opsin-5), member of the class A family of seven-transmembrane G protein-coupled ...
19-145 9.93e-14

neuropsin (Opsin-5), member of the class A family of seven-transmembrane G protein-coupled receptors; Neuropsin, also known as Opsin-5, is a photoreceptor protein expressed in the retina, brain, testes, and spinal cord. Neuropsin belongs to the type 2 opsin family of the class A G-protein coupled receptors. Mammalian neuropsin activates Gi protein-mediated photo-transduction pathway in a UV-dependent manner, whereas, in non-mammalian vertebrates, neuropsin is involved in regulating the photoperiodic control of seasonal reproduction in birds such as quail. As with other opsins, it may also act as a retinal photoisomerase.


Pssm-ID: 320202 [Multi-domain]  Cd Length: 284  Bit Score: 66.53  E-value: 9.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  19 TAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSR--GDRNFISFLFTMAFFNFLVPLFITHTSY-------- 88
Cdd:cd15074   115 HVCIVIVAIWLYALFWAVAPLVGWGSYGPEPFGTSCSIDWTGasASVGGMSYIISIFIFCYLLPVLIIVFSYvkiirkvk 194
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907103530  89 --RFMEQKFSRSGH----LPVNTTLPGRML----LLGWGPYALLYLYAAIADVSFISPklqMVQILP 145
Cdd:cd15074   195 ssRKRVAGFDSRSKrqhkIERKVTKVAVLIcagfLIAWTPYAVVSMWSAFGSPDSVPI---LASILP 258
7tmA_Opsin_Gq_invertebrates cd15337
invertebrate Gq opsins, member of the class A family of seven-transmembrane G protein-coupled ...
20-136 7.11e-12

invertebrate Gq opsins, member of the class A family of seven-transmembrane G protein-coupled receptors; The invertebrate Gq-coupled opsin subfamily includes the arthropod and mollusc visual opsins. Like the vertebrate visual opsins, arthropods possess color vision by the use of multiple opsins sensitive to different light wavelengths. The invertebrate Gq opsins are closely related to the vertebrate melanopsins, the primary photoreceptor molecules for non-visual responses to light, and the R1-R6 photoreceptors, which are the fly equivalent to the vertebrate rods. The Gq opsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320459 [Multi-domain]  Cd Length: 292  Bit Score: 61.18  E-value: 7.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  20 AIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSY----------- 88
Cdd:cd15337   118 AFIMIIIIWLWSLLWSIPPFFGWGRYVPEGFQTSCTFDYLSRDLNNRLFILGLFIFGFLCPLLIIIFCYvniiravrnhe 197
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907103530  89 --------------RFMEQKFSRSGHLPVNTT-LPGRMLLLGWGPYALLYLYAAIADVSFISP 136
Cdd:cd15337   198 kemtqtaksgmgkdTEKNDARKKAEIRIAKVAiILISLFLLSWTPYAVVALLGQFGPAYWITP 260
7tmA_Melanopsin-like cd15083
vertebrate melanopsins and related opsins, member of the class A family of seven-transmembrane ...
4-136 3.59e-09

vertebrate melanopsins and related opsins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represent the Gq-coupled rhodopsin subfamily consists of melanopsins, insect photoreceptors R1-R6, invertebrate Gq opsins as well as their closely related opsins. Melanopsins (also called Opsin-4) are the primary photoreceptor molecules for non-visual functions such as the photo-entrainment of the circadian rhythm and pupillary constriction in mammals. Mammalian melanopsins are expressed only in the inner retina, whereas non-mammalian vertebrate melanopsins are localized in various extra-retinal tissues such as iris, brain, pineal gland, and skin. The outer photoreceptors (R1-R6) are the insect Drosophila equivalent to the vertebrate rods and are responsible for image formation and motion detection. The invertebrate G(q) opsins includes the arthropod and mollusk visual opsins as well as invertebrate melanopsins, which are also found in vertebrates. Arthropods possess color vision by the use of multiple opsins sensitive to different light wavelengths. Members of this subfamily belong to the class A of the G protein-coupled receptors and have seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320211 [Multi-domain]  Cd Length: 291  Bit Score: 53.88  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530   4 LQRY-----PASSGRQLAWDTAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFL 78
Cdd:cd15083    96 VDRYlvitrPMKASVRISHRRALIVIAVVWLYSLLWVLPPLFGWSRYVLEGLLTSCSFDYLSRDDANRSYVICLLIFGFV 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  79 VPLFITHTSYRFM-------EQKFSRSGHLPVNTTLPGR-------------------MLLLGWGPYALLYLYAAIADVS 132
Cdd:cd15083   176 LPLLIIIYCYSFIfravrrhEKAMKEMAKRFSKSELSSPkarrqaevktakialllvlLFCLAWTPYAVVALIGQFGYLE 255

                  ....
gi 1907103530 133 FISP 136
Cdd:cd15083   256 VLTP 259
7tmA_photoreceptors_insect cd15079
insect photoreceptors R1-R6 and similar proteins, member of the class A family of ...
11-90 4.46e-09

insect photoreceptors R1-R6 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes the insect photoreceptors and their closely related proteins. The Drosophila eye is composed of about 800 unit eyes called ommatidia, each of which contains eight photoreceptor cells (R1-R8). The six outer photoreceptors (R1-R6) function like the vertebrate rods and are responsible for motion detection in dim light and image formation. The R1-R6 photoreceptors express a blue-absorbing pigment, Rhodopsin 1(Rh1). The inner photoreceptors (R7 and R8) are considered the equivalent of the color-sensitive vertebrate cone cells, which express a range of different pigments. The R7 photoreceptors express one of two different UV absorbing pigments, either Rh3 or Rh4. Likewise, the R8 photoreceptors express either the blue absorbing pigment Rh5 or green absorbing pigment Rh6. These photoreceptors belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320207 [Multi-domain]  Cd Length: 292  Bit Score: 53.35  E-value: 4.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  11 SGRQLAWDTAIPLVLFVWMSSAFWASLPLM-GWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYR 89
Cdd:cd15079   106 NGNPLTRGKALLLILFIWLYALPWALLPLLfGWGRYVPEGFLTSCSFDYLTRDWNTRSFVATIFVFAYVIPLIIIIYCYS 185

                  .
gi 1907103530  90 F 90
Cdd:cd15079   186 F 186
7tmA_Melanopsin cd15336
vertebrate melanopsins (Opsin-4), member of the class A family of seven-transmembrane G ...
24-91 2.64e-07

vertebrate melanopsins (Opsin-4), member of the class A family of seven-transmembrane G protein-coupled receptors; Melanopsin (also called Opsin-4) is the G protein-coupled photopigment that mediates non-visual responses to light. In mammals, these photoresponses include the photo-entrainment of circadian rhythm, pupillary constriction, and acute nocturnal melatonin suppression. Mammalian melanopsins are expressed only in the inner retina, whereas non-mammalian vertebrate melanopsins are localized in various extra-retinal tissues such as iris, brain, pineal gland, and skin. Melanopsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320458 [Multi-domain]  Cd Length: 290  Bit Score: 48.56  E-value: 2.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907103530  24 VLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFM 91
Cdd:cd15336   121 ILLVWLYSLAWSLPPLFGWSAYVPEGLLTSCTWDYMTFTPSVRAYTMLLFCFVFFIPLGIIIYCYLFI 188
7tmA_Parapinopsin cd15075
non-visual parapinopsin, member of the class A family of seven-transmembrane G protein-coupled ...
24-136 3.73e-06

non-visual parapinopsin, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes the non-visual pineal pigment, parapinopsin, which is a member of the class A of the seven transmembrane G protein-coupled receptors. Parapinopsin serves as a UV-sensitive pigment for the wavelength discrimination in the pineal-related organs of lower vertebrates such as reptiles, amphibians, and fish. Although parapinopsin is phylogenetically related to vertebrate visual pigments such as rhodopsin, which releases its retinal chromophore and bleaches, the parapinopsin photoproduct is stable and does not bleach. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells.


Pssm-ID: 320203 [Multi-domain]  Cd Length: 279  Bit Score: 45.15  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  24 VLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFMEQKFSRSGHLPV 103
Cdd:cd15075   120 IASSWLWSLIWNTPPLFGWGSYQLEGVMTSCAPDWYSRDPVNVSYILCYFSFCFAIPFAIILVSYGYLLWTLRQVAKLGV 199
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907103530 104 N---TTLPGRM------------LLLGWGPYALLYLYAAIADVSFISP 136
Cdd:cd15075   200 AeggSTAKAEVqvarmvvvmvmaFLLCWLPYAAFALTVVSKPDVYINP 247
7tmA_amine_R-like cd14967
amine receptors and similar proteins, member of the class A family of seven-transmembrane G ...
19-141 7.97e-06

amine receptors and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; Amine receptors of the class A family of GPCRs include adrenoceptors, 5-HT (serotonin) receptors, muscarinic cholinergic receptors, dopamine receptors, histamine receptors, and trace amine receptors. The receptors of amine subfamily are major therapeutic targets for the treatment of neurological disorders and psychiatric diseases. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes.


Pssm-ID: 320098 [Multi-domain]  Cd Length: 259  Bit Score: 44.09  E-value: 7.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  19 TAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTC-CTLDYSRGdrnfisFLFTMAFFNFLVPLFITHTSYRFM------ 91
Cdd:cd14967   115 RALIMIAAVWVYSLLISLPPLVGWRDETQPSVVDCeCEFTPNKI------YVLVSSVISFFIPLLIMIVLYARIfrvarr 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907103530  92 EQKFSRSghlpvnTTLPGRMLLLGWGPYALLYLYAAIADVSFISPKLQMV 141
Cdd:cd14967   189 ELKAAKT------LAIIVGAFLLCWLPFFIIYLVSAFCPPDCVPPILYAV 232
7tmA_VA_opsin cd15082
non-visual VA (vertebrate ancient) opsins, member of the class A family of seven-transmembrane ...
24-138 9.01e-06

non-visual VA (vertebrate ancient) opsins, member of the class A family of seven-transmembrane G protein-coupled receptors; The vertebrate ancient (VA) opsin photopigments were originally identified in salmon and they appear to have diverged early in the evolution of vertebrate opsins. VA opsins are localized in the inner retina and the brain in teleosts. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extraretinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity, and body color change. The VA opsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320210 [Multi-domain]  Cd Length: 291  Bit Score: 44.02  E-value: 9.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  24 VLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFMEQKFSRSGHLPV 103
Cdd:cd15082   133 LLFVWTFSFIWTIPPVLGWSSYTVSKIGTTCEPNWYSGNMHDHTYIITFFTTCFILPLGVIFVSYGKLLQKLRKVSNTQG 212
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907103530 104 ---NTTLPGRML-----------LLGWGPYALLYLYAAIADVSFISPKL 138
Cdd:cd15082   213 rlgNARKPERQVtrmvvvmivafMVCWTPYAAFSILVTAHPTIHLDPRL 261
7tmA_Parietopsin cd15085
non-visual parietopsins, member of the class A family of seven-transmembrane G protein-coupled ...
23-88 1.64e-05

non-visual parietopsins, member of the class A family of seven-transmembrane G protein-coupled receptors; Parietopsin is a non-visual green light-sensitive opsin that was initially identified in the parietal eye of lizards. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity and body color change. Parietopsin belongs to the class A of the G protein-coupled receptors and shows strong homology to the vertebrate visual opsins.


Pssm-ID: 320213 [Multi-domain]  Cd Length: 280  Bit Score: 43.30  E-value: 1.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907103530  23 LVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSY 88
Cdd:cd15085   119 GLLFIWLFCLFWAVAPLFGWSSYGPEGVQTSCSIGWEERSWSNYSYLILYFLMCFVIPVAIIGFSY 184
7tmA_Encephalopsin cd15078
encephalopsins (opsin-3), member of the class A family of seven-transmembrane G ...
24-144 2.69e-05

encephalopsins (opsin-3), member of the class A family of seven-transmembrane G protein-coupled receptors; Encephalopsin, also called Opsin-3 or Panopsin, is a mammalian extra-retinal opsin that is highly localized in the brain. It is thought to play a role in encephalic photoreception. Encephalopsin belongs to the class A of the G protein-coupled receptors and shows strong homology to the vertebrate visual opsins.


Pssm-ID: 320206 [Multi-domain]  Cd Length: 279  Bit Score: 42.51  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  24 VLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFM------------ 91
Cdd:cd15078   117 ITYIWLYSLAWTGAPLLGWNRYTLEVHGLGCSFDWKSKDPNDTSFVLLFFLGCLVVPLGIMAYCYGHIlyeirmlrsved 196
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907103530  92 ------------EQKFSRSGHLPVNTtlpgrmLLLGWGPYALLYLYAAIADVSFISPKLQMVQIL 144
Cdd:cd15078   197 lqtfqvikilkyEKKVAKMCLLMIST------FLICWMPYAVVSLLVTSGYSKLVTPTIAIIPSL 255
7tmA_tmt_opsin cd15086
teleost multiple tissue (tmt) opsin, member of the class A family of seven-transmembrane G ...
24-145 4.60e-05

teleost multiple tissue (tmt) opsin, member of the class A family of seven-transmembrane G protein-coupled receptors; Teleost multiple tissue (tmt) opsins are homologs of encephalopsin. Mouse encephalopsin (or panopsin) is highly expressed in the brain and testes, whereas the teleost homologs are localized to multiple tissues. The exact functions of the encephalopsins and tmt-opsins are unknown. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity and body color change. Tmt opsins belong to the class A of the G protein-coupled receptors and show strong homology to the vertebrate visual opsins.


Pssm-ID: 320214 [Multi-domain]  Cd Length: 276  Bit Score: 42.03  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  24 VLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFMEQKFSRSGHLPV 103
Cdd:cd15086   120 VGGSWLYSLLWTLPPLLGWSSYGPEGPGTTCSVQWTSRSANSISYIICLFIFCLLLPFLVMVYCYGRLLYAIKQVGKINK 199
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907103530 104 NTT--LPGRML----------LLGWGPYALLYLYAAIADVSFISPklqMVQILP 145
Cdd:cd15086   200 STArkREQHVLlmvvtmvicyLLCWLPYGVMALLATFGKPGLVTP---VASIVP 250
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
6-129 1.31e-04

7 transmembrane receptor (rhodopsin family); This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins.


Pssm-ID: 459624 [Multi-domain]  Cd Length: 256  Bit Score: 40.36  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530   6 RYPASSGRQLAWdtaiPLVLFVWMSSAFWASLPL-MGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFIT 84
Cdd:pfam00001  92 RYKRRRTPRRAK----VLILVIWVLALLLSLPPLlFGWTLTVPEGNVTVCFIDFPEDLSKPVSYTLLISVLGFLLPLLVI 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907103530  85 HTSY-------RFMEQKFSRSGHLPVNTTLpGRMLL-------LGWGPYALLYLYAAIA 129
Cdd:pfam00001 168 LVCYtliirtlRKSASKQKSSERTQRRRKA-LKTLAvvvvvfiLCWLPYHIVNLLDSLA 225
7tmA_Prostanoid_R cd14981
G protein-coupled receptors for prostanoids, member of the class A family of ...
7-100 3.94e-04

G protein-coupled receptors for prostanoids, member of the class A family of seven-transmembrane G protein-coupled receptors; Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters.


Pssm-ID: 320112 [Multi-domain]  Cd Length: 288  Bit Score: 39.15  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530   7 YPASSGRQLAWdtaipLVLF-VWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGD--RNFISFLF---------TMAF 74
Cdd:cd14981   111 YNSHVKKRRAR-----LMLGaVWAFALLIASLPLLGLGSYVLQYPGTWCFLDFYSKNtgDAAYAYLYsilgllillVTLL 185
                          90       100
                  ....*....|....*....|....*.
gi 1907103530  75 FNFLVPLFITHTSYRFMEQKFSRSGH 100
Cdd:cd14981   186 CNLLVIITLLRMRRRKKRHRRSRRSA 211
7tmA_Pinopsin cd15084
non-visual pinopsins, member of the class A family of seven-transmembrane G protein-coupled ...
25-88 6.54e-04

non-visual pinopsins, member of the class A family of seven-transmembrane G protein-coupled receptors; Pinopsins are found in the pineal organ of birds, reptiles and amphibians, but are absent from teleosts and mammals. The vertebrate non-visual opsin family includes pinopsins, parapinopsin, VA (vertebrate ancient) opsins, and parietopsins. These non-visual opsins are expressed in various extra-retinal tissues and/or in non-rod, non-cone retinal cells. They are thought to be involved in light-dependent physiological functions such as photo-entrainment of circadian rhythm, photoperiodicity and body color change. Pinopsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320212 [Multi-domain]  Cd Length: 295  Bit Score: 38.69  E-value: 6.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907103530  25 LFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSY 88
Cdd:cd15084   131 AFTWGWSLLWTSPPLFGWSSYVPEGLRTSCGPNWYTGGTNNNSYILALFVTCFALPLSTIIFSY 194
7tmA_GPR61_GPR62-like cd15220
G protein-coupled receptors 61 and 62, member of the class A family of seven-transmembrane G ...
20-141 2.14e-03

G protein-coupled receptors 61 and 62, member of the class A family of seven-transmembrane G protein-coupled receptors; This subgroup includes the orphan receptors GPR61 and GPR62, which are both constitutively active and predominantly expressed in the brain. While GPR61 couples to G(s) subtype of G proteins, the signaling pathway and function of GPR 62 are unknown. GPR61-deficient mice displayed significant hyperphagia and heavier body weight compared to wild-type mice, suggesting that GPR61 is involved in the regulation of food intake and body weight. GPR61 transcript expression was found in the caudate, putamen, and thalamus of human brain, whereas GPR62 transcript expression was found in the basal forebrain, frontal cortex, caudate, putamen, thalamus, and hippocampus. Both receptors share the highest sequence homology with each other and comprise a conserved subgroup within the class A family of GPCRs, which includes receptors for hormones, neurotransmitters, sensory stimuli, and a variety of other ligands. All GPCRs have a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, which then activate the heterotrimeric G proteins. Members of this subgroup contain [A/E]RY motif, a variant of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of the class A GPCRs and important for efficient G protein-coupled signal transduction.


Pssm-ID: 410633 [Multi-domain]  Cd Length: 264  Bit Score: 37.04  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907103530  20 AIPLVLFVWMSSAFWASLPLMGWGHYDYEP--VGTCCTLDYSRGdRNFISFLFTMAFFNFLVPLFITHTSYRFMEQKFSr 97
Cdd:cd15220   116 VAAVLVGVWVKALLLGLLPVLGWPSYGGPApiAARHCSLHWSHS-GHRGVFVVLFALVCFLLPLLLILVVYCGVFKVFG- 193
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907103530  98 SGHLPVNTTLPGRMLLLGWGPYALLYLYAAIADVSFISPKLQMV 141
Cdd:cd15220   194 GGKAALTLAAIVGQFLCCWLPYFAFHLYSALAASPVSGGEAEEV 237
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH