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Conserved domains on  [gi|540344546|ref|NP_001269384|]
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neuronal acetylcholine receptor subunit alpha-2 isoform 2 precursor [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
Neur_chan_LBD pfam02931
Neurotransmitter-gated ion-channel ligand binding domain; This family is the extracellular ...
59-250 8.48e-99

Neurotransmitter-gated ion-channel ligand binding domain; This family is the extracellular ligand binding domain of these ion channels. This domain forms a pentameric arrangement in the known structure.


:

Pssm-ID: 251626  Cd Length: 215  Bit Score: 299.94  E-value: 8.48e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546   59 EDRLFKHLFRGYNRWARPVPNTS---------------DVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSE 123
Cdd:pfam02931   1 EERLLDDLLSGYDKRVRPVENGSdpvtvsvglyltqiiDVDEKNQDLTTNVWLRQQWTDERLAWNPEDYGGITSLRLPSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  124 MIWIPDIVLYNNADGEFAVT-HMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQME 202
Cdd:pfam02931  81 KIWKPDIVLYNNADGIHDVTtPNTNVRVYPDGTVLWSPPAIYKSSCPIDVTYFPFDEQNCSLKFGSWTYNGEEVDLQWED 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 540344546  203 QT-------VDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLP 250
Cdd:pfam02931 161 DTppveleeIDLSDFTENGEWDIVDVPAKRNENPYGCYSELYSDVTFYFTLRRKP 215
Neur_chan_memb pfam02932
Neurotransmitter-gated ion-channel transmembrane region; This family includes the four ...
257-505 1.46e-83

Neurotransmitter-gated ion-channel transmembrane region; This family includes the four transmembrane helices that form the ion channel.


:

Pssm-ID: 251627  Cd Length: 228  Bit Score: 261.05  E-value: 1.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  257 LIIPCLLISCLTVLVFYLPSDCG-EKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVL 335
Cdd:pfam02932   1 LIIPCVLISFLSWLVFWLPADAGpEKVTLGITTLLTMTVFLLLIRESLPKTSYVVPLIGKYLVFTMFVFTASVEYAVVVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  336 NVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVdaeerevvveeedrwACAGHVA 415
Cdd:pfam02932  81 NVHHRSPSTHKMPEWVRKLFLRKLPRLLFMKRPPESLSPPAAPHLRSSSSSSGSVLEP---------------ASGKESK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  416 PSVGTLCSHGHLHSGASGPKAEAllqegelLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFII 495
Cdd:pfam02932 146 GVGGPETSSGLPGGSGSGLGSPF-------RLSPELKKALEGVRFIAEHLRSRDEFDEVKEDWKYVAMVIDRLSRWIFPI 218
                         250
                  ....*....|
gi 540344546  496 VCFLGTIGLF 505
Cdd:pfam02932 219 AFVLGTLVYW 228
LIC TIGR00860
Cation transporter family protein; The Ligand-gated Ion Channel (LIC) Family of ...
57-507 2.11e-104

Cation transporter family protein; The Ligand-gated Ion Channel (LIC) Family of Neurotransmitter Receptors TC 1.A.9)Members of the LIC family of ionotropic neurotransmitter receptors are found only in vertebrate and invertebrate animals. They exhibit receptor specificity for (1)acetylcholine, (2) serotonin, (3) glycine, (4) glutamate and (5) g-aminobutyric acid (GABA). All of these receptor channels are probably hetero- orhomopentameric. The best characterized are the nicotinic acetyl-choline receptors which are pentameric channels of a2bgd subunit composition. All subunits arehomologous. The three dimensional structures of the protein complex in both the open and closed configurations have been solved at 0.9 nm resolution.The channel protein complexes of the LIC family preferentially transport cations or anions depending on the channel (e.g., the acetylcholine receptors are cationselective while glycine receptors are anion selective) [Transport and binding proteins, Cations and iron carrying compounds].


:

Pssm-ID: 233155 [Multi-domain]  Cd Length: 459  Bit Score: 322.82  E-value: 2.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546   57 ETEDRLFKHLFRGYNRWARPV----PNT----------SDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPS 122
Cdd:TIGR00860  29 EVERKLLDELLKNYDARVRPVfggpPVTvsfnlflrsiMDVDEKNMDYTTNIWLRQEWTDERLQWNPEEYPGVTLVRTPD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  123 EMIWIPDIVLYNNADGEFAVTHMTKA--HLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQ 200
Cdd:TIGR00860 109 DSIWVPDIFFYNEKDARFHGITMTNVlvRIHPNGSVLYSPRITLTLACPMDLRNFPFDVQNCSLKFESWGYTTNDIKLEW 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  201 MEQ---TVDLKDYWESGEWAIVNATGTyNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSD 277
Cdd:TIGR00860 189 KEQgavQVDDSLFISLPEFELLGVYGT-RYCTSETNTGEYPCLTFSFVLRRRPLYYLLQLYIPSILIVILSWVSFWLPAD 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  278 C-GEKITLCISVLLSLTVFLLLITEIIPSTSlVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTmphwvRGALL 356
Cdd:TIGR00860 268 AsGARVSLGITTLLTMTTFSSGVRESLPAVS-YVKAIDVYFAVCMAFVFLALLETAFVNYVHHKDPAQGK-----RHLLL 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  357 GCVPRWLLMNRPPppvELCHPLrlklspsyhwlesnvdaeerevvveeedrwACAGHVAPSVGTLCSHGHLHSGASGPKA 436
Cdd:TIGR00860 342 ERCAWRLCKQEPG---EDYRRP------------------------------ALDHASLSSVEMRAKDGGRGLESPTERQ 388
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 540344546  437 EALLQEGELLLSPHMQKALEGVHYIaDHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLP 507
Cdd:TIGR00860 389 RLLHSPPPAEGDLDLAGILEEVRIA-HRFRKRDESEEVVRDWKFRAKVIDKLSRMAFPLAFLLFNIGYWMS 458
 
Name Accession Description Interval E-value
Neur_chan_LBD pfam02931
Neurotransmitter-gated ion-channel ligand binding domain; This family is the extracellular ...
59-250 8.48e-99

Neurotransmitter-gated ion-channel ligand binding domain; This family is the extracellular ligand binding domain of these ion channels. This domain forms a pentameric arrangement in the known structure.


Pssm-ID: 251626  Cd Length: 215  Bit Score: 299.94  E-value: 8.48e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546   59 EDRLFKHLFRGYNRWARPVPNTS---------------DVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSE 123
Cdd:pfam02931   1 EERLLDDLLSGYDKRVRPVENGSdpvtvsvglyltqiiDVDEKNQDLTTNVWLRQQWTDERLAWNPEDYGGITSLRLPSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  124 MIWIPDIVLYNNADGEFAVT-HMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQME 202
Cdd:pfam02931  81 KIWKPDIVLYNNADGIHDVTtPNTNVRVYPDGTVLWSPPAIYKSSCPIDVTYFPFDEQNCSLKFGSWTYNGEEVDLQWED 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 540344546  203 QT-------VDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLP 250
Cdd:pfam02931 161 DTppveleeIDLSDFTENGEWDIVDVPAKRNENPYGCYSELYSDVTFYFTLRRKP 215
Neur_chan_memb pfam02932
Neurotransmitter-gated ion-channel transmembrane region; This family includes the four ...
257-505 1.46e-83

Neurotransmitter-gated ion-channel transmembrane region; This family includes the four transmembrane helices that form the ion channel.


Pssm-ID: 251627  Cd Length: 228  Bit Score: 261.05  E-value: 1.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  257 LIIPCLLISCLTVLVFYLPSDCG-EKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVL 335
Cdd:pfam02932   1 LIIPCVLISFLSWLVFWLPADAGpEKVTLGITTLLTMTVFLLLIRESLPKTSYVVPLIGKYLVFTMFVFTASVEYAVVVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  336 NVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVdaeerevvveeedrwACAGHVA 415
Cdd:pfam02932  81 NVHHRSPSTHKMPEWVRKLFLRKLPRLLFMKRPPESLSPPAAPHLRSSSSSSGSVLEP---------------ASGKESK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  416 PSVGTLCSHGHLHSGASGPKAEAllqegelLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFII 495
Cdd:pfam02932 146 GVGGPETSSGLPGGSGSGLGSPF-------RLSPELKKALEGVRFIAEHLRSRDEFDEVKEDWKYVAMVIDRLSRWIFPI 218
                         250
                  ....*....|
gi 540344546  496 VCFLGTIGLF 505
Cdd:pfam02932 219 AFVLGTLVYW 228
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
149-234 7.86e-03

Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241258  Cd Length: 139  Bit Score: 35.69  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546 149 HLFSTGTVHWvppaIYKSSCSIDVTFFPFDQQ--NCK--MKFGSWTYDKAKIDLEQMEqTVDLKDywesGEW-----AIV 219
Cdd:cd01224   28 ELIHSGELSK----ISSKGKAQERTFFLFDHQlvYCKkdLLKRDNLIYKGRIDLDNME-IEDLED----GKDkdsgvTVK 98
                         90
                 ....*....|....*...
gi 540344546 220 NATGTYNSKK---YDCCA 234
Cdd:cd01224   99 NAWKIYNTSKnkwYLLCA 116
LIC TIGR00860
Cation transporter family protein; The Ligand-gated Ion Channel (LIC) Family of ...
57-507 2.11e-104

Cation transporter family protein; The Ligand-gated Ion Channel (LIC) Family of Neurotransmitter Receptors TC 1.A.9)Members of the LIC family of ionotropic neurotransmitter receptors are found only in vertebrate and invertebrate animals. They exhibit receptor specificity for (1)acetylcholine, (2) serotonin, (3) glycine, (4) glutamate and (5) g-aminobutyric acid (GABA). All of these receptor channels are probably hetero- orhomopentameric. The best characterized are the nicotinic acetyl-choline receptors which are pentameric channels of a2bgd subunit composition. All subunits arehomologous. The three dimensional structures of the protein complex in both the open and closed configurations have been solved at 0.9 nm resolution.The channel protein complexes of the LIC family preferentially transport cations or anions depending on the channel (e.g., the acetylcholine receptors are cationselective while glycine receptors are anion selective) [Transport and binding proteins, Cations and iron carrying compounds].


Pssm-ID: 233155 [Multi-domain]  Cd Length: 459  Bit Score: 322.82  E-value: 2.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546   57 ETEDRLFKHLFRGYNRWARPV----PNT----------SDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPS 122
Cdd:TIGR00860  29 EVERKLLDELLKNYDARVRPVfggpPVTvsfnlflrsiMDVDEKNMDYTTNIWLRQEWTDERLQWNPEEYPGVTLVRTPD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  123 EMIWIPDIVLYNNADGEFAVTHMTKA--HLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQ 200
Cdd:TIGR00860 109 DSIWVPDIFFYNEKDARFHGITMTNVlvRIHPNGSVLYSPRITLTLACPMDLRNFPFDVQNCSLKFESWGYTTNDIKLEW 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  201 MEQ---TVDLKDYWESGEWAIVNATGTyNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSD 277
Cdd:TIGR00860 189 KEQgavQVDDSLFISLPEFELLGVYGT-RYCTSETNTGEYPCLTFSFVLRRRPLYYLLQLYIPSILIVILSWVSFWLPAD 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  278 C-GEKITLCISVLLSLTVFLLLITEIIPSTSlVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTmphwvRGALL 356
Cdd:TIGR00860 268 AsGARVSLGITTLLTMTTFSSGVRESLPAVS-YVKAIDVYFAVCMAFVFLALLETAFVNYVHHKDPAQGK-----RHLLL 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  357 GCVPRWLLMNRPPppvELCHPLrlklspsyhwlesnvdaeerevvveeedrwACAGHVAPSVGTLCSHGHLHSGASGPKA 436
Cdd:TIGR00860 342 ERCAWRLCKQEPG---EDYRRP------------------------------ALDHASLSSVEMRAKDGGRGLESPTERQ 388
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 540344546  437 EALLQEGELLLSPHMQKALEGVHYIaDHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLP 507
Cdd:TIGR00860 389 RLLHSPPPAEGDLDLAGILEEVRIA-HRFRKRDESEEVVRDWKFRAKVIDKLSRMAFPLAFLLFNIGYWMS 458
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
28-75 4.88e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 251763 [Multi-domain]  Cd Length: 979  Bit Score: 44.68  E-value: 4.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 540344546   28 EAKRPPPRAPgdplsSPSPTALpQGGSHTETEDRLFKHLFRGYNRWAR 75
Cdd:pfam03154 523 ESPPPPPRSP-----SPEPTVV-NTPSHASQSARFYKHLDRGYNSCAR 564
 
Name Accession Description Interval E-value
Neur_chan_LBD pfam02931
Neurotransmitter-gated ion-channel ligand binding domain; This family is the extracellular ...
59-250 8.48e-99

Neurotransmitter-gated ion-channel ligand binding domain; This family is the extracellular ligand binding domain of these ion channels. This domain forms a pentameric arrangement in the known structure.


Pssm-ID: 251626  Cd Length: 215  Bit Score: 299.94  E-value: 8.48e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546   59 EDRLFKHLFRGYNRWARPVPNTS---------------DVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSE 123
Cdd:pfam02931   1 EERLLDDLLSGYDKRVRPVENGSdpvtvsvglyltqiiDVDEKNQDLTTNVWLRQQWTDERLAWNPEDYGGITSLRLPSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  124 MIWIPDIVLYNNADGEFAVT-HMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQME 202
Cdd:pfam02931  81 KIWKPDIVLYNNADGIHDVTtPNTNVRVYPDGTVLWSPPAIYKSSCPIDVTYFPFDEQNCSLKFGSWTYNGEEVDLQWED 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 540344546  203 QT-------VDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLP 250
Cdd:pfam02931 161 DTppveleeIDLSDFTENGEWDIVDVPAKRNENPYGCYSELYSDVTFYFTLRRKP 215
Neur_chan_memb pfam02932
Neurotransmitter-gated ion-channel transmembrane region; This family includes the four ...
257-505 1.46e-83

Neurotransmitter-gated ion-channel transmembrane region; This family includes the four transmembrane helices that form the ion channel.


Pssm-ID: 251627  Cd Length: 228  Bit Score: 261.05  E-value: 1.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  257 LIIPCLLISCLTVLVFYLPSDCG-EKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVL 335
Cdd:pfam02932   1 LIIPCVLISFLSWLVFWLPADAGpEKVTLGITTLLTMTVFLLLIRESLPKTSYVVPLIGKYLVFTMFVFTASVEYAVVVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  336 NVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVdaeerevvveeedrwACAGHVA 415
Cdd:pfam02932  81 NVHHRSPSTHKMPEWVRKLFLRKLPRLLFMKRPPESLSPPAAPHLRSSSSSSGSVLEP---------------ASGKESK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  416 PSVGTLCSHGHLHSGASGPKAEAllqegelLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFII 495
Cdd:pfam02932 146 GVGGPETSSGLPGGSGSGLGSPF-------RLSPELKKALEGVRFIAEHLRSRDEFDEVKEDWKYVAMVIDRLSRWIFPI 218
                         250
                  ....*....|
gi 540344546  496 VCFLGTIGLF 505
Cdd:pfam02932 219 AFVLGTLVYW 228
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
149-234 7.86e-03

Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241258  Cd Length: 139  Bit Score: 35.69  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546 149 HLFSTGTVHWvppaIYKSSCSIDVTFFPFDQQ--NCK--MKFGSWTYDKAKIDLEQMEqTVDLKDywesGEW-----AIV 219
Cdd:cd01224   28 ELIHSGELSK----ISSKGKAQERTFFLFDHQlvYCKkdLLKRDNLIYKGRIDLDNME-IEDLED----GKDkdsgvTVK 98
                         90
                 ....*....|....*...
gi 540344546 220 NATGTYNSKK---YDCCA 234
Cdd:cd01224   99 NAWKIYNTSKnkwYLLCA 116
LIC TIGR00860
Cation transporter family protein; The Ligand-gated Ion Channel (LIC) Family of ...
57-507 2.11e-104

Cation transporter family protein; The Ligand-gated Ion Channel (LIC) Family of Neurotransmitter Receptors TC 1.A.9)Members of the LIC family of ionotropic neurotransmitter receptors are found only in vertebrate and invertebrate animals. They exhibit receptor specificity for (1)acetylcholine, (2) serotonin, (3) glycine, (4) glutamate and (5) g-aminobutyric acid (GABA). All of these receptor channels are probably hetero- orhomopentameric. The best characterized are the nicotinic acetyl-choline receptors which are pentameric channels of a2bgd subunit composition. All subunits arehomologous. The three dimensional structures of the protein complex in both the open and closed configurations have been solved at 0.9 nm resolution.The channel protein complexes of the LIC family preferentially transport cations or anions depending on the channel (e.g., the acetylcholine receptors are cationselective while glycine receptors are anion selective) [Transport and binding proteins, Cations and iron carrying compounds].


Pssm-ID: 233155 [Multi-domain]  Cd Length: 459  Bit Score: 322.82  E-value: 2.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546   57 ETEDRLFKHLFRGYNRWARPV----PNT----------SDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPS 122
Cdd:TIGR00860  29 EVERKLLDELLKNYDARVRPVfggpPVTvsfnlflrsiMDVDEKNMDYTTNIWLRQEWTDERLQWNPEEYPGVTLVRTPD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  123 EMIWIPDIVLYNNADGEFAVTHMTKA--HLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQ 200
Cdd:TIGR00860 109 DSIWVPDIFFYNEKDARFHGITMTNVlvRIHPNGSVLYSPRITLTLACPMDLRNFPFDVQNCSLKFESWGYTTNDIKLEW 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  201 MEQ---TVDLKDYWESGEWAIVNATGTyNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSD 277
Cdd:TIGR00860 189 KEQgavQVDDSLFISLPEFELLGVYGT-RYCTSETNTGEYPCLTFSFVLRRRPLYYLLQLYIPSILIVILSWVSFWLPAD 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  278 C-GEKITLCISVLLSLTVFLLLITEIIPSTSlVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTmphwvRGALL 356
Cdd:TIGR00860 268 AsGARVSLGITTLLTMTTFSSGVRESLPAVS-YVKAIDVYFAVCMAFVFLALLETAFVNYVHHKDPAQGK-----RHLLL 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344546  357 GCVPRWLLMNRPPppvELCHPLrlklspsyhwlesnvdaeerevvveeedrwACAGHVAPSVGTLCSHGHLHSGASGPKA 436
Cdd:TIGR00860 342 ERCAWRLCKQEPG---EDYRRP------------------------------ALDHASLSSVEMRAKDGGRGLESPTERQ 388
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 540344546  437 EALLQEGELLLSPHMQKALEGVHYIaDHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLP 507
Cdd:TIGR00860 389 RLLHSPPPAEGDLDLAGILEEVRIA-HRFRKRDESEEVVRDWKFRAKVIDKLSRMAFPLAFLLFNIGYWMS 458
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
28-75 4.88e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 251763 [Multi-domain]  Cd Length: 979  Bit Score: 44.68  E-value: 4.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 540344546   28 EAKRPPPRAPgdplsSPSPTALpQGGSHTETEDRLFKHLFRGYNRWAR 75
Cdd:pfam03154 523 ESPPPPPRSP-----SPEPTVV-NTPSHASQSARFYKHLDRGYNSCAR 564
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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