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Conserved domains on  [gi|568944416|ref|XP_006507089|]
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inositol 1,4,5-trisphosphate receptor type 2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 218-439 1.18e-158

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) and similar proteins; ITPR2, also called IP3 receptor isoform 2 (IP3R 2), or InsP3R2, or type 2 inositol 1,4,5-trisphosphate receptor, or type 2 InsP3 receptor, is a key regulator for the activity of calcium ion transmembrane transportation, which plays a critical role in cell cycle and proliferation. It is a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of cAMP-dependent protein kinase (PKA). ITPR2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 467759 [Multi-domain]  Cd Length: 222  Bit Score: 488.01  E-value: 1.18e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  218 WKITLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAG 297
Cdd:cd23288     1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  298 QWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKNVKDGEIPTPKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRA 377
Cdd:cd23288    81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKKRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944416  378 DCLVPRNSYVRLRHLCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 439
Cdd:cd23288   161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-228 8.06e-98

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


:

Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 314.05  E-value: 8.06e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416     5 MSSFLYIGDIVSLYAEGSVNGFISTLGLVDDRCVVHPEAGDLANPPKKFRDCLFKVCPMNRYSAQKQYWKAKQAKQGNHt 84
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSPNGN- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416    85 eaALLKKLQHAAELEQKQNesenrkllgeiVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSLDAAGN-EGSWFYI 163
Cdd:pfam08709   80 --SLTDALKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFII 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568944416   164 HPFWKLRSEGDNIVVGDKVVLMPVNAGQPLH-ASNVELLDNPGcKEVNAVNCNTSWKITLFMKFSS 228
Cdd:pfam08709  147 TPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 475-670 2.90e-81

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 265.99  E-value: 2.90e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   475 LLEDLIFFVADVTNN---GQDVLDVVITKPNRERQKLMREQNILAQVFG---ILKAPFKekageGSMLRLEDLGDQRYAP 548
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT-----GALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   549 YKYVLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAE---DTITALLHNNRKLLEKHITAKEIETFVSLLRRN 625
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 568944416   626 -REPRFLDYLSDLCVSNSTAIPVTQELICKFMLSpgNADILIQTKL 670
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1915-2022 2.82e-38

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


:

Pssm-ID: 462482  Cd Length: 98  Bit Score: 138.81  E-value: 2.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1915 ITIMRPILRFLQLLCENHNRELQNFLRNQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINERNVALVNQTLESLT 1993
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 568944416  1994 EYCQGPCHENQTCIatHESNGIDIIIALI 2022
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1202-1344 3.14e-09

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


The actual alignment was detected with superfamily member pfam01365:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 59.13  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1202 QHQRLLKNMGAHSVVL---DLLQIPY-----------EKTDEKMNEVMDLAHTFLQNFCRGNPQNQVLLHKHLNLFLTP- 1266
Cdd:pfam01365   33 QRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQl 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1267 -------GLLeaETMRHIFMNNYHLC-NEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINg 1338
Cdd:pfam01365  113 gspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP- 189


                   ....*.
gi 568944416  1339 GEDVLI 1344
Cdd:pfam01365  190 NPDLLL 195
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 218-439 1.18e-158

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) and similar proteins; ITPR2, also called IP3 receptor isoform 2 (IP3R 2), or InsP3R2, or type 2 inositol 1,4,5-trisphosphate receptor, or type 2 InsP3 receptor, is a key regulator for the activity of calcium ion transmembrane transportation, which plays a critical role in cell cycle and proliferation. It is a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of cAMP-dependent protein kinase (PKA). ITPR2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467759 [Multi-domain]  Cd Length: 222  Bit Score: 488.01  E-value: 1.18e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  218 WKITLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAG 297
Cdd:cd23288     1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  298 QWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKNVKDGEIPTPKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRA 377
Cdd:cd23288    81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKKRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944416  378 DCLVPRNSYVRLRHLCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 439
Cdd:cd23288   161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-228 8.06e-98

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 314.05  E-value: 8.06e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416     5 MSSFLYIGDIVSLYAEGSVNGFISTLGLVDDRCVVHPEAGDLANPPKKFRDCLFKVCPMNRYSAQKQYWKAKQAKQGNHt 84
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSPNGN- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416    85 eaALLKKLQHAAELEQKQNesenrkllgeiVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSLDAAGN-EGSWFYI 163
Cdd:pfam08709   80 --SLTDALKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFII 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568944416   164 HPFWKLRSEGDNIVVGDKVVLMPVNAGQPLH-ASNVELLDNPGcKEVNAVNCNTSWKITLFMKFSS 228
Cdd:pfam08709  147 TPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 475-670 2.90e-81

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 265.99  E-value: 2.90e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   475 LLEDLIFFVADVTNN---GQDVLDVVITKPNRERQKLMREQNILAQVFG---ILKAPFKekageGSMLRLEDLGDQRYAP 548
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT-----GALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   549 YKYVLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAE---DTITALLHNNRKLLEKHITAKEIETFVSLLRRN 625
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 568944416   626 -REPRFLDYLSDLCVSNSTAIPVTQELICKFMLSpgNADILIQTKL 670
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 232-432 9.62e-74

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 243.81  E-value: 9.62e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   232 DVLKGGDVVRLFHAEQEKFLTCDDYEKKQHiFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLFRFKHLATG 311
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   312 NYLAAELNPdyrdaqnegknvkdgEIPTPKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPRNSYVRLRH 391
Cdd:pfam02815   80 RYLHSHEEQ---------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQH 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 568944416   392 LCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIV 432
Cdd:pfam02815  145 VCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1915-2022 2.82e-38

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


Pssm-ID: 462482  Cd Length: 98  Bit Score: 138.81  E-value: 2.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1915 ITIMRPILRFLQLLCENHNRELQNFLRNQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINERNVALVNQTLESLT 1993
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 568944416  1994 EYCQGPCHENQTCIatHESNGIDIIIALI 2022
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1202-1344 3.14e-09

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 59.13  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1202 QHQRLLKNMGAHSVVL---DLLQIPY-----------EKTDEKMNEVMDLAHTFLQNFCRGNPQNQVLLHKHLNLFLTP- 1266
Cdd:pfam01365   33 QRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQl 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1267 -------GLLeaETMRHIFMNNYHLC-NEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINg 1338
Cdd:pfam01365  113 gspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP- 189


                   ....*.
gi 568944416  1339 GEDVLI 1344
Cdd:pfam01365  190 NPDLLL 195
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
294-324 1.34e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.64  E-value: 1.34e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 568944416    294 GGAGQWNSLFRFKHLATGNYLAAELNPDYRD 324
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPW 31
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
112-166 3.91e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.10  E-value: 3.91e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 568944416    112 GEIVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSL--DAAGNEGSWFYIHPF 166
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 218-439 1.18e-158

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) and similar proteins; ITPR2, also called IP3 receptor isoform 2 (IP3R 2), or InsP3R2, or type 2 inositol 1,4,5-trisphosphate receptor, or type 2 InsP3 receptor, is a key regulator for the activity of calcium ion transmembrane transportation, which plays a critical role in cell cycle and proliferation. It is a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of cAMP-dependent protein kinase (PKA). ITPR2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467759 [Multi-domain]  Cd Length: 222  Bit Score: 488.01  E-value: 1.18e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  218 WKITLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAG 297
Cdd:cd23288     1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  298 QWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKNVKDGEIPTPKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRA 377
Cdd:cd23288    81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKKRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944416  378 DCLVPRNSYVRLRHLCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 439
Cdd:cd23288   161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 224-439 5.94e-134

MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor (ITPR); Inositol 1,4,5 trisphosphate receptors (ITPRs) are a family of endoplasmic reticulum Ca2+ channels essential for the control of intracellular Ca2+ levels in virtually every mammalian cell type. Calcium-mediated signaling through ITPRs is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. The ITPR family includes three isoforms (ITPR1, ITPR2 and ITPR3), which can control different cellular processes due to their unique biophysical properties, subcellular localization, and tissue distribution. ITPRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467748 [Multi-domain]  Cd Length: 204  Bit Score: 417.14  E-value: 5.94e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  224 MKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLF 303
Cdd:cd23277     1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  304 RFKHLATGNYLAAELNPDYRDAqnegknvkdgeiPTPKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPR 383
Cdd:cd23277    81 RFKHLATGQYLAAEVDPDPTPD------------PTRSKLRGAPGKPVYCLVSVPHGNDIASIFELDPTTLQRGDSLVPR 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568944416  384 NSYVRLRHLCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 439
Cdd:cd23277   149 SSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 224-439 5.83e-123

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) and similar proteins; ITPR3, also called IP3 receptor isoform 3 (IP3R 3), or InsP3R3, or type 3 inositol 1,4,5-trisphosphate receptor, or type 3 InsP3 receptor, acts as anti-oncogenic channel by propelling pro-apoptotic Ca2+ signals to mitochondria. It is the principal intracellular Ca2+ release channel in cholangiocytes and plays a particularly important role in cancer. ITPR3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467760 [Multi-domain]  Cd Length: 215  Bit Score: 386.32  E-value: 5.83e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  224 MKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLF 303
Cdd:cd23289     1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  304 RFKHLATGNYLAAELNPDYRDAQNEGKNVKDGeIPTPKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPR 383
Cdd:cd23289    81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMG-AQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPR 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568944416  384 NSYVRLRHLCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 439
Cdd:cd23289   160 NSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 224-444 4.69e-121

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) and similar proteins; ITPR1, also called IP3 receptor isoform 1 (IP3R 1), or InsP3R1, or type 1 inositol 1,4,5-trisphosphate receptor, or type 1 InsP3 receptor, is an intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. It is involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. It plays a role in endoplasmic reticulum (ER) stress-induced apoptosis. ITPR1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467758 [Multi-domain]  Cd Length: 222  Bit Score: 381.34  E-value: 4.69e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  224 MKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLF 303
Cdd:cd23287     1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  304 RFKHLATGNYLAAELNPDYRDAQNEGKNVKDGEIPTPKKK-RQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVP 382
Cdd:cd23287    81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRlRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944416  383 RNSYVRLRHLCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEVRDLDF 444
Cdd:cd23287   161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-228 8.06e-98

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 314.05  E-value: 8.06e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416     5 MSSFLYIGDIVSLYAEGSVNGFISTLGLVDDRCVVHPEAGDLANPPKKFRDCLFKVCPMNRYSAQKQYWKAKQAKQGNHt 84
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSPNGN- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416    85 eaALLKKLQHAAELEQKQNesenrkllgeiVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSLDAAGN-EGSWFYI 163
Cdd:pfam08709   80 --SLTDALKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFII 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568944416   164 HPFWKLRSEGDNIVVGDKVVLMPVNAGQPLH-ASNVELLDNPGcKEVNAVNCNTSWKITLFMKFSS 228
Cdd:pfam08709  147 TPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 475-670 2.90e-81

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 265.99  E-value: 2.90e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   475 LLEDLIFFVADVTNN---GQDVLDVVITKPNRERQKLMREQNILAQVFG---ILKAPFKekageGSMLRLEDLGDQRYAP 548
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT-----GALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   549 YKYVLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAE---DTITALLHNNRKLLEKHITAKEIETFVSLLRRN 625
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 568944416   626 -REPRFLDYLSDLCVSNSTAIPVTQELICKFMLSpgNADILIQTKL 670
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 232-432 9.62e-74

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 243.81  E-value: 9.62e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   232 DVLKGGDVVRLFHAEQEKFLTCDDYEKKQHiFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLFRFKHLATG 311
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416   312 NYLAAELNPdyrdaqnegknvkdgEIPTPKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPRNSYVRLRH 391
Cdd:pfam02815   80 RYLHSHEEQ---------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQH 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 568944416   392 LCTNTWVTSTTIPIDTEEERPVMLKIGTCQTKEDKEAFAIV 432
Cdd:pfam02815  145 VCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1915-2022 2.82e-38

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


Pssm-ID: 462482  Cd Length: 98  Bit Score: 138.81  E-value: 2.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1915 ITIMRPILRFLQLLCENHNRELQNFLRNQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINERNVALVNQTLESLT 1993
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 568944416  1994 EYCQGPCHENQTCIatHESNGIDIIIALI 2022
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 231-439 8.16e-26

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 107.09  E-value: 8.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  231 EDVLKGGDVVRLFHAEQEKFLTCD--------DYEKKQHIFLRTTLRQ-SATSATSSKALWEIEVVHhDPCRGGAGQWNS 301
Cdd:cd23280     4 ENFLKGGDVVRLFHKELEAYLSAEgsfvdevlTEDVHLRVRPVDDRKPrTLFPPTSGDTFWQIEKED-TPLKGGVIKWGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  302 LFRFKHLATGNYLAAELNpdyrdaqnegknvkdgeiptpkkkrqageKIMYTLVSVPHGNDIASLFELDATTLQRADcLV 381
Cdd:cd23280    83 QCRLRHLPTGKYLAVDDK-----------------------------TGNGKVVLTSDPSDPSTVFRLHPVTKETSE-EV 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568944416  382 PRNSYVRLRHLCTNTWVTSTTIPIDTEEERPVML---------KIGTCQTKEDKEAFAIVCVPLSEV 439
Cdd:cd23280   133 KFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGlswdgaklrKVSLSLERQDDDAFTIQEVDPDLV 199
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 237-434 8.04e-22

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 94.76  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  237 GDVVRLFHAEQEKFLTCDDY-----EKKQHIFLRTTLRQsatsaTSSKALWEIEVVHHDPcrGGAGQWNSLFRFKHLATG 311
Cdd:cd23263     1 GDVIWLKHSETGKYLHSHRKnyptgSGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  312 NYLAAELNPdyrdaqnegknvkdgeiPTPKKKRQagekimYTLVSVPHGnDIASLFELDAT-TLQRADCLVPRNSYVRLR 390
Cdd:cd23263    74 KYLSSEEGK-----------------KSPKSNHQ------EVLCLTDNP-DKSSLFKFEPIgSTKYKQKYVKKDSYFRLK 129

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568944416  391 HLCTNTWVTSTTIPIDTEEErpvMLKIGTCQtKEDKEAFAIVCV 434
Cdd:cd23263   130 HVNTNFWLHSHEKKFNINNK---TQQEVICH-GEREEVFKLWKA 169
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1202-1344 3.14e-09

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 59.13  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1202 QHQRLLKNMGAHSVVL---DLLQIPY-----------EKTDEKMNEVMDLAHTFLQNFCRGNPQNQVLLHKHLNLFLTP- 1266
Cdd:pfam01365   33 QRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQl 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  1267 -------GLLeaETMRHIFMNNYHLC-NEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINg 1338
Cdd:pfam01365  113 gspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP- 189


                   ....*.
gi 568944416  1339 GEDVLI 1344
Cdd:pfam01365  190 NPDLLL 195
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 234-315 3.12e-06

MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, also called RYR-3, or brain ryanodine receptor-calcium release channel, or brain-type ryanodine receptor, or type 3 ryanodine receptor, is a calcium channel that plays a role in cellular calcium signaling. It mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. It also mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. RYR-3 forms homotetramer and also forms heterotetramer with RYR-2. RYR-3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467763 [Multi-domain]  Cd Length: 187  Bit Score: 49.91  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  234 LKGGDVVRLFHAEQEKfLTCDDYEK--KQHiflRTTLRQSATSATSSKALWEIEvvhhdPCR----GGAGQWNSLFRFKH 307
Cdd:cd23292     3 LLGGHVVRLFHGHDEC-LTIPSTDQsdEQH---RVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRH 73


                  ....*...
gi 568944416  308 LATGNYLA 315
Cdd:cd23292    74 LTTGHYLA 81
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 215-314 7.88e-06

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 48.48  E-value: 7.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  215 NTSWKI---TLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYE---KKQHifLRTTLRQSATSATSSKALWEIEVVh 288
Cdd:cd23276    44 NNWWQIlkpRGDPSSNPPDPEYVRDGDEVRLLHKETNRYLRTHDAAapvTSKH--KEVSAYPDENEDGDDNDLWVVEIV- 120

                          90       100
                  ....*....|....*....|....*....
gi 568944416  289 HDPCRGGAGQWNSL---FRFKHLATGNYL 314
Cdd:cd23276   121 KDEGKLEDKRIKPLttrFRLRNKKTGCYL 149
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
294-324 1.34e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.64  E-value: 1.34e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 568944416    294 GGAGQWNSLFRFKHLATGNYLAAELNPDYRD 324
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPW 31
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 231-317 1.51e-05

MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, also called RYR-1, or skeletal muscle calcium release channel, or skeletal muscle ryanodine receptor, or skeletal muscle-type ryanodine receptor, or type 1 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. It can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. It is required for normal embryonic development of muscle fibers and skeletal muscle, as well as for normal heart morphogenesis, skin development and ossification during embryogenesis. RYR-1 forms homotetramer and can also form heterotetramers with RYR-2. RYR-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467761 [Multi-domain]  Cd Length: 192  Bit Score: 47.96  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  231 EDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHifLRTTLRQSATSATSSKALWEIEvvhhdPCR----GGAGQWNSLFRFK 306
Cdd:cd23290     5 EGYVTGGHVLRLFHGHMDECLTISAADSDDQ--RRLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQPLRIR 77

                          90
                  ....*....|.
gi 568944416  307 HLATGNYLAAE 317
Cdd:cd23290    78 HVTTGRYLALT 88
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 236-321 2.23e-05

MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also called RYRs) are intracellular Ca(2+) release channels located on the sarco/endoplasmic reticulum (SR/ER). They release calcium Ca(2+) intracellular stores to activate critical functions including muscle contraction and neurotransmitter release. The family includes three closely homologous proteins, RyR1, RyR2 and RyR3. RyR1 is present in skeletal muscle; RyR2 is in heart muscle; and RyR3 is expressed at low levels in many tissues including brain, smooth muscle, and slow-twitch skeletal muscle. RYR2 is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells. RyR1 and RyR2 release Ca2+ from the ER in response to excitation of muscle membranes to promote muscle contraction. RYR3 is involved in force production and calcium handling in extraocular muscle. RYRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467749 [Multi-domain]  Cd Length: 180  Bit Score: 47.30  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  236 GGDVVRLFHAEQEKFLTC--DDYEKKQHiflRTTLRQSATSATSSKALWEIEVVHHDPCrGGAGQWNSLFRFKHLATGNY 313
Cdd:cd23278     1 GGDVLRLFHGHMDECLTIpaAGSKEDQH---RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRY 76


                  ....*...
gi 568944416  314 LAaeLNPD 321
Cdd:cd23278    77 LA--LTED 82
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
112-166 3.91e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.10  E-value: 3.91e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 568944416    112 GEIVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSL--DAAGNEGSWFYIHPF 166
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
173-220 4.57e-04

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.02  E-value: 4.57e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568944416    173 GDNIVVGDKVVLMPVNAGQPLHAS-NVELLDNPGCKEVNAV-----NCNTSWKI 220
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdEKLPPWGDGQQEVTGYgnpaiDANTLWLI 54
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
231-287 1.11e-03

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 39.25  E-value: 1.11e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568944416    231 EDVLKGGDVVRLFHAEQEKFLTCDD---YE---KKQHIFLRTTLRQSATSatsskaLWEIEVV 287
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDeklPPwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 236-315 1.63e-03

MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, also called RYR-2, or cardiac muscle ryanodine receptor-calcium release channel, or cardiac muscle ryanodine receptor, or type 2 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity of RYR-2 is modulated by formation of heterotetramers with RYR-3. RYR-2 is required for cellular calcium ion homeostasis. it plays an essential role in embryonic heart development. RYR-2 forms homotetramer and also forms heterotetramers with RYR-1 and RYR-3. RYR-2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467762 [Multi-domain]  Cd Length: 184  Bit Score: 41.95  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944416  236 GGDVVRLFHAEQEKFLTCDDYEKKQHIfLRTTLRQSATSATSSKALWEIEVVHHdPCRGGAGQWNSLFRFKHLATGNYLA 315
Cdd:cd23291     1 GGDVLRLLHGHMDECLTVPSGEHGEEQ-RRTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGKYLS 78
 
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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