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Conserved domains on  [gi|84662753|ref|NP_001033794|]
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probable G-protein coupled receptor 149 [Homo sapiens]

Protein Classification

G protein-coupled receptor family protein; olfactory receptor subfamily 2A protein( domain architecture ID 11606634)

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| olfactory receptor (OR) subfamily 2A protein, such as human olfactory receptor 2A2 and related proteins in other mammals and sauropsids; ORs play a central role in olfaction, the sense of smell, and belong to the class A rhodopsin-like family of seven-transmembrane G protein-coupled receptors (7TM GPCRs)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
35-374 8.05e-124

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. 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: 320139  Cd Length: 256  Bit Score: 369.86  E-value: 8.05e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753  35 YLFCLTCLMTFAALVGSIYSLISLLKMQNRTVVSMLVASWSVDDLMSVLSVTIFMFLQWPNEVPgyFQFLCTTSALMYLC 114
Cdd:cd15011   1 LLFCLTLIIALLTLLGSIYSLLSLLKMRNKTTLSVLVASLSVDDLLSVVPVSIFMLMQWETDGL--PQPLCTTSALLYLF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 115 QGLSSNLKATLLVSYNFYTMHRGVGSQTaSRRSGQVLGVVLTVWAASLLLSALPLCGWGAFVRTPWGCLVDCSSSYVLFL 194
Cdd:cd15011  79 QGLSSNLKASLIASYNFYTTKKLGWLQT-TKRSVRVPWAVLTIWAASLLLSALPLCGWGSFVPTSWGCLVDCQSSYILFL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 195 SIVYALAFGLLVGLSVPLTHRLLCSEEpprlhsnyqeisrgasipgtpptagrvvslspedapgpslrrsggcspssdtv 274
Cdd:cd15011 158 FSLYSLCFCILVVLSVPLTYQLLCSDE----------------------------------------------------- 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 275 fgpgapaaagaeacrrenrgtlygtrsfTVSVAQKRFALILALTKVVLWLPMMMHMVVQNVVGFQSLPLETFSFLLTLLA 354
Cdd:cd15011 185 ----------------------------TVSFAQKRFSLILALTKVILWLPMMIQMVVQHVTGFQSLSLETLSFLLTLLA 236
                       330       340
                ....*....|....*....|
gi 84662753 355 TTVTPVFVLSKRWTHLPCGC 374
Cdd:cd15011 237 AAVTPLFVLSERWIHLPCGC 256
 
Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
35-374 8.05e-124

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. 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: 320139  Cd Length: 256  Bit Score: 369.86  E-value: 8.05e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753  35 YLFCLTCLMTFAALVGSIYSLISLLKMQNRTVVSMLVASWSVDDLMSVLSVTIFMFLQWPNEVPgyFQFLCTTSALMYLC 114
Cdd:cd15011   1 LLFCLTLIIALLTLLGSIYSLLSLLKMRNKTTLSVLVASLSVDDLLSVVPVSIFMLMQWETDGL--PQPLCTTSALLYLF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 115 QGLSSNLKATLLVSYNFYTMHRGVGSQTaSRRSGQVLGVVLTVWAASLLLSALPLCGWGAFVRTPWGCLVDCSSSYVLFL 194
Cdd:cd15011  79 QGLSSNLKASLIASYNFYTTKKLGWLQT-TKRSVRVPWAVLTIWAASLLLSALPLCGWGSFVPTSWGCLVDCQSSYILFL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 195 SIVYALAFGLLVGLSVPLTHRLLCSEEpprlhsnyqeisrgasipgtpptagrvvslspedapgpslrrsggcspssdtv 274
Cdd:cd15011 158 FSLYSLCFCILVVLSVPLTYQLLCSDE----------------------------------------------------- 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 275 fgpgapaaagaeacrrenrgtlygtrsfTVSVAQKRFALILALTKVVLWLPMMMHMVVQNVVGFQSLPLETFSFLLTLLA 354
Cdd:cd15011 185 ----------------------------TVSFAQKRFSLILALTKVILWLPMMIQMVVQHVTGFQSLSLETLSFLLTLLA 236
                       330       340
                ....*....|....*....|
gi 84662753 355 TTVTPVFVLSKRWTHLPCGC 374
Cdd:cd15011 237 AAVTPLFVLSERWIHLPCGC 256
 
Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
35-374 8.05e-124

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. 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: 320139  Cd Length: 256  Bit Score: 369.86  E-value: 8.05e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753  35 YLFCLTCLMTFAALVGSIYSLISLLKMQNRTVVSMLVASWSVDDLMSVLSVTIFMFLQWPNEVPgyFQFLCTTSALMYLC 114
Cdd:cd15011   1 LLFCLTLIIALLTLLGSIYSLLSLLKMRNKTTLSVLVASLSVDDLLSVVPVSIFMLMQWETDGL--PQPLCTTSALLYLF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 115 QGLSSNLKATLLVSYNFYTMHRGVGSQTaSRRSGQVLGVVLTVWAASLLLSALPLCGWGAFVRTPWGCLVDCSSSYVLFL 194
Cdd:cd15011  79 QGLSSNLKASLIASYNFYTTKKLGWLQT-TKRSVRVPWAVLTIWAASLLLSALPLCGWGSFVPTSWGCLVDCQSSYILFL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 195 SIVYALAFGLLVGLSVPLTHRLLCSEEpprlhsnyqeisrgasipgtpptagrvvslspedapgpslrrsggcspssdtv 274
Cdd:cd15011 158 FSLYSLCFCILVVLSVPLTYQLLCSDE----------------------------------------------------- 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 275 fgpgapaaagaeacrrenrgtlygtrsfTVSVAQKRFALILALTKVVLWLPMMMHMVVQNVVGFQSLPLETFSFLLTLLA 354
Cdd:cd15011 185 ----------------------------TVSFAQKRFSLILALTKVILWLPMMIQMVVQHVTGFQSLSLETLSFLLTLLA 236
                       330       340
                ....*....|....*....|
gi 84662753 355 TTVTPVFVLSKRWTHLPCGC 374
Cdd:cd15011 237 AAVTPLFVLSERWIHLPCGC 256
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
36-366 3.92e-37

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.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 139.87  E-value: 3.92e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753  36 LFCLTCLMTFAALVGSIYSLISLLKMQNR-TVVSMLVASWSVDDLMSVLSVTIFMFLQWPNEVPGYFQFLCTTSALMYLC 114
Cdd:cd14964   1 TTIILSLLTCLGLLGNLLVLLSLVRLRKRpRSTRLLLASLAACDLLASLVVLVLFFLLGLTEASSRPQALCYLIYLLWYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 115 QGLSSnLKATLLVSYNFYTMHRGVGSQTASRRSGQVLGVVLTVWAASLLLSALPLCGWGAFVRTPWgclvdCSSSYVLFL 194
Cdd:cd14964  81 ANLAS-IWTTLVLTYHRYFALCGPLKYTRLSSPGKTRVIILGCWGVSLLLSIPPLVGKGAIPRYNT-----LTGSCYLIC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 195 SIVYALAFGLLVGLSVPLTHRLLCSEEPPRLHSNYQEISRgasipgtpptagrvvslspedapgpslrrsggcspssdtv 274
Cdd:cd14964 155 TTIYLTWGFLLVSFLLPLVAFLVIFSRIVLRLRRRVRAIR---------------------------------------- 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 275 fgpgapaaagaeacrrenrgtLYGTRSFTVSVAQKRFALILALTKVVLWLPMMMHMVVQNVV--GFQSLPLETFSFLLTL 352
Cdd:cd14964 195 ---------------------SAASLNTDKNLKATKSLLILVITFLLCWLPFSIVFILHALVaaGQGLNLLSILANLLAV 253
                       330
                ....*....|....
gi 84662753 353 LATTVTPVFVLSKR 366
Cdd:cd14964 254 LASTLNPFIYCLGN 267
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
36-218 8.88e-07

rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor superfamily; Class A rhodopsin-like receptors constitute about 90% of all GPCRs. The class A GPCRs include the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, 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, 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. Based on sequence similarity, GPCRs can be divided into six major classes: class A (rhodopsin-like family), class B (Methuselah-like, adhesion and secretin-like receptor family), class C (metabotropic glutamate receptor family), class D (fungal mating pheromone receptors), class E (cAMP receptor family), and class F (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.


Pssm-ID: 410626 [Multi-domain]  Cd Length: 275  Bit Score: 51.14  E-value: 8.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753  36 LFCLTCLMTFAALVGSIYSLISLLKMQN-RTVVSMLVASWSVDDLMSVLSVTIFMFLQWPNEVPGYFQFLCTTSALMYLC 114
Cdd:cd00637   1 LAVLYILIFVVGLVGNLLVILVILRNRRlRTVTNYFILNLAVADLLVGLLVIPFSLVSLLLGRWWFGDALCKLLGFLQSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84662753 115 QGLSSNLkaTL-LVSYNFYTMHRGVGSQTASRRSGQVLGVVLTVWAASLLLSALPLCGWGAFVRTPWGCLVDCSSSYVlf 193
Cdd:cd00637  81 SLLASIL--TLtAISVDRYLAIVHPLRYRRRFTRRRAKLLIALIWLLSLLLALPPLLGWGVYDYGGYCCCCLCWPDLT-- 156
                       170       180
                ....*....|....*....|....*
gi 84662753 194 LSIVYALAFgLLVGLSVPLTHRLLC 218
Cdd:cd00637 157 LSKAYTIFL-FVLLFLLPLLVIIVC 180
 
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.
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