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Conserved domains on  [gi|310171|gb|AAA41446|]
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inositol triphosphate receptor subtype 3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 225-439 4.84e-158

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: 486.86  E-value: 4.84e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    225 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 304
Cdd:cd23289    1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    305 RFKHLATGNYLAAEENPSYKGDVSDPKAAGPGAQSRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 384
Cdd:cd23289   81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 310171    385 SYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 439
Cdd:cd23289  161 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 4-230 9.95e-105

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: 334.08  E-value: 9.95e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171        4 MSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQTKQDKEK 83
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171       84 IADVvllqkLQHAAQMEQKQNdtenkkvhgdvVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGN-EGSWL 162
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 310171      163 FIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLH-ASNYELSDNVGcKEVNSVNCNTSWKINLFMQFRDH 230
Cdd:pfam08709  145 IITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 475-670 1.05e-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: 267.53  E-value: 1.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      475 LLEDLVFFVSDVPNN---GQNVLDIMVTKPNRERQKLMRDENILKQIFG---ILKAPFrdkggEGPLVRLEELSDQKNAP 548
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPF-----TGALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      549 YQYMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAE---DTITALLHNNRKLLEKHITKTEVETFVSLVRKN 625
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 310171      626 -REPRFLDYLSDLCVSNRIAIPVTQELICKCVLDpkNSDILIQTEL 670
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1864-1973 4.45e-39

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: 141.51  E-value: 4.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     1864 TSVLIMRPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDIMCGSttgglgllglyINEDNVGLVIQTLET 1942
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 310171     1943 LTEYCQGPCHENQTCIvtHESNGIDIITALI 1973
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1191-1303 3.10e-04

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: 44.50  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     1191 KKQQRLLKNMDAHKVML---DLLQIPY-----------DKNDNKMMEILRYTHQFLQKFCAGNPGNQALLHKHLQLFLTP 1256
Cdd:pfam01365   32 RQRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 310171     1257 --------GLLeaETMQHIFLNNYQLC-SEISEPVLQHFVHCWPTHGRHVQYLDFL 1303
Cdd:pfam01365  112 lgspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
Ion_trans super family cl37996
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2235-2527 5.28e-04

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


The actual alignment was detected with superfamily member pfam00520:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 44.18  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2235 SPLISLLFWILICFSIAALFTKHYsvrplivalvlrsiyYLGIGPTLNILGALNLTNKIVFVVSFV------GNRGTFIR 2308
Cdd:pfam00520    1 SRYFELFILLLILLNTIFLALETY---------------FQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFR 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2309 gykamvmDMEFLYHVGYILTSVLGLFAHE-----------LFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALI 2377
Cdd:pfam00520   66 -------SPWNILDFVVVLPSLISLVLSSvgslsglrvlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2378 LVYLFSIVGFLFLKDDFILEVDRLPGNHSrastlgmphgaatfmgtcsgdkmdcvsevsvpeileedeeldsteraCDTL 2457
Cdd:pfam00520  139 FLFIFAIIGYQLFGGKLKTWENPDNGRTN-----------------------------------------------FDNF 171

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2458 LMCIVTVMNhgLRNGGGVGDILRKPSkDESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2527
Cdd:pfam00520  172 PNAFLWLFQ--TMTTEGWGDIMYDTI-DGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 225-439 4.84e-158

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: 486.86  E-value: 4.84e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    225 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 304
Cdd:cd23289    1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    305 RFKHLATGNYLAAEENPSYKGDVSDPKAAGPGAQSRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 384
Cdd:cd23289   81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 310171    385 SYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 439
Cdd:cd23289  161 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 4-230 9.95e-105

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: 334.08  E-value: 9.95e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171        4 MSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQTKQDKEK 83
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171       84 IADVvllqkLQHAAQMEQKQNdtenkkvhgdvVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGN-EGSWL 162
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 310171      163 FIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLH-ASNYELSDNVGcKEVNSVNCNTSWKINLFMQFRDH 230
Cdd:pfam08709  145 IITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 475-670 1.05e-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: 267.53  E-value: 1.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      475 LLEDLVFFVSDVPNN---GQNVLDIMVTKPNRERQKLMRDENILKQIFG---ILKAPFrdkggEGPLVRLEELSDQKNAP 548
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPF-----TGALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      549 YQYMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAE---DTITALLHNNRKLLEKHITKTEVETFVSLVRKN 625
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 310171      626 -REPRFLDYLSDLCVSNRIAIPVTQELICKCVLDpkNSDILIQTEL 670
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 234-432 1.22e-71

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: 238.03  E-value: 1.22e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      234 VLKGGDVVRLFHAEQEKFLTCDEYRGKlQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGN 313
Cdd:pfam02815    2 YLKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      314 YLAAEENPsykgdvsdpkaagpGAQSRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLC 393
Cdd:pfam02815   81 YLHSHEEQ--------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVC 146

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 310171      394 TNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIV 432
Cdd:pfam02815  147 TGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1864-1973 4.45e-39

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: 141.51  E-value: 4.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     1864 TSVLIMRPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDIMCGSttgglgllglyINEDNVGLVIQTLET 1942
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 310171     1943 LTEYCQGPCHENQTCIvtHESNGIDIITALI 1973
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
113-167 2.10e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.25  E-value: 2.10e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 310171       113 GDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTL--DATGNEGSWLFIQPF 167
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
295-348 6.06e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 6.06e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 310171       295 GGAGHWNGLYRFKHLATGNYLAAEENPsykgdvsdPKAAGPGAQSRTGRRNAGE 348
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEK--------LPPWGDGQQEVTGYGNPAI 46
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1191-1303 3.10e-04

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: 44.50  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     1191 KKQQRLLKNMDAHKVML---DLLQIPY-----------DKNDNKMMEILRYTHQFLQKFCAGNPGNQALLHKHLQLFLTP 1256
Cdd:pfam01365   32 RQRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 310171     1257 --------GLLeaETMQHIFLNNYQLC-SEISEPVLQHFVHCWPTHGRHVQYLDFL 1303
Cdd:pfam01365  112 lgspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2235-2527 5.28e-04

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 44.18  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2235 SPLISLLFWILICFSIAALFTKHYsvrplivalvlrsiyYLGIGPTLNILGALNLTNKIVFVVSFV------GNRGTFIR 2308
Cdd:pfam00520    1 SRYFELFILLLILLNTIFLALETY---------------FQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFR 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2309 gykamvmDMEFLYHVGYILTSVLGLFAHE-----------LFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALI 2377
Cdd:pfam00520   66 -------SPWNILDFVVVLPSLISLVLSSvgslsglrvlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2378 LVYLFSIVGFLFLKDDFILEVDRLPGNHSrastlgmphgaatfmgtcsgdkmdcvsevsvpeileedeeldsteraCDTL 2457
Cdd:pfam00520  139 FLFIFAIIGYQLFGGKLKTWENPDNGRTN-----------------------------------------------FDNF 171

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2458 LMCIVTVMNhgLRNGGGVGDILRKPSkDESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2527
Cdd:pfam00520  172 PNAFLWLFQ--TMTTEGWGDIMYDTI-DGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 116-184 6.09e-03

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: 40.39  E-value: 6.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 310171    116 VKYGSVIQLLHMKSNKYLTVNKRlPALLEKNAMRVTldATGNEGSWLFIQPFWKLRSNGDNVVVGDKVI 184
Cdd:cd23276   66 VRDGDEVRLLHKETNRYLRTHDA-AAPVTSKHKEVS--AYPDENEDGDDNDLWVVEIVKDEGKLEDKRI 131
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 225-439 4.84e-158

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: 486.86  E-value: 4.84e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    225 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 304
Cdd:cd23289    1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    305 RFKHLATGNYLAAEENPSYKGDVSDPKAAGPGAQSRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 384
Cdd:cd23289   81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 310171    385 SYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 439
Cdd:cd23289  161 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 225-439 2.33e-131

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: 410.21  E-value: 2.33e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    225 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 304
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    305 RFKHLATGNYLAAEENPSYKGDvsdpkaagpgaQSRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 384
Cdd:cd23277   81 RFKHLATGQYLAAEVDPDPTPD-----------PTRSKLRGAPGKPVYCLVSVPHGNDIASIFELDPTTLQRGDSLVPRS 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 310171    385 SYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 439
Cdd:cd23277  150 SYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 219-439 3.74e-127

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: 398.64  E-value: 3.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    219 WKINLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAG 298
Cdd:cd23288    1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    299 HWNGLYRFKHLATGNYLAAEENPSYKGDVSDPKAAGPGAQSRTGR-RNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKT 377
Cdd:cd23288   81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKkRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 310171    378 DSFVPRNSYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 439
Cdd:cd23288  161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 225-444 2.18e-113

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: 359.38  E-value: 2.18e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    225 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 304
Cdd:cd23287    1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    305 RFKHLATGNYLAAEENPSYKGDVSDPKAAGPGAQ--SRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVP 382
Cdd:cd23287   81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQdaSRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 310171    383 RNSYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEIRDLDF 444
Cdd:cd23287  161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 4-230 9.95e-105

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: 334.08  E-value: 9.95e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171        4 MSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQTKQDKEK 83
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171       84 IADVvllqkLQHAAQMEQKQNdtenkkvhgdvVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGN-EGSWL 162
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 310171      163 FIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLH-ASNYELSDNVGcKEVNSVNCNTSWKINLFMQFRDH 230
Cdd:pfam08709  145 IITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 475-670 1.05e-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: 267.53  E-value: 1.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      475 LLEDLVFFVSDVPNN---GQNVLDIMVTKPNRERQKLMRDENILKQIFG---ILKAPFrdkggEGPLVRLEELSDQKNAP 548
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPF-----TGALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      549 YQYMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAE---DTITALLHNNRKLLEKHITKTEVETFVSLVRKN 625
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 310171      626 -REPRFLDYLSDLCVSNRIAIPVTQELICKCVLDpkNSDILIQTEL 670
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 234-432 1.22e-71

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: 238.03  E-value: 1.22e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      234 VLKGGDVVRLFHAEQEKFLTCDEYRGKlQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGN 313
Cdd:pfam02815    2 YLKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171      314 YLAAEENPsykgdvsdpkaagpGAQSRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLC 393
Cdd:pfam02815   81 YLHSHEEQ--------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVC 146

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 310171      394 TNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIV 432
Cdd:pfam02815  147 TGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1864-1973 4.45e-39

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: 141.51  E-value: 4.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     1864 TSVLIMRPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDIMCGSttgglgllglyINEDNVGLVIQTLET 1942
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 310171     1943 LTEYCQGPCHENQTCIvtHESNGIDIITALI 1973
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 229-435 5.29e-29

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: 116.33  E-value: 5.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    229 DHLEEVLKGGDVVRLFHAEQEKFLTCDE--------YRGKLQVFLRTTLRQ-SATSATSSNALWEVEVVHhDPCRGGAGH 299
Cdd:cd23280    1 KENENFLKGGDVVRLFHKELEAYLSAEGsfvdevltEDVHLRVRPVDDRKPrTLFPPTSGDTFWQIEKED-TPLKGGVIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    300 WNGLYRFKHLATGNYLAAEENpsykgdvsdpkaagpgaqsrtgrrnageKIKYRLVAVPHGNDIASLFELDPTTLQKTDS 379
Cdd:cd23280   80 WGDQCRLRHLPTGKYLAVDDK----------------------------TGNGKVVLTSDPSDPSTVFRLHPVTKETSEE 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 310171    380 fVPRNSYVRLRHLCTNTWIQSTNAPIDVEEERPIRLM---------LGTCPTKEDKEAFAIVSVP 435
Cdd:cd23280  132 -VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLswdgaklrkVSLSLERQDDDAFTIQEVD 195
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 238-410 2.92e-25

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: 104.77  E-value: 2.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    238 GDVVRLFHAEQEKFLTCDEYR-----GKLQVFLRTTLRQsatsaTSSNALWEVEVVHHDPcrGGAGHWNGLYRFKHLATG 312
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKNyptgsGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    313 NYLAAEENPSykgdvsdpkaagpgaqsrtgrrNAGEKIKYRLVAVPHGnDIASLFELDPT-TLQKTDSFVPRNSYVRLRH 391
Cdd:cd23263   74 KYLSSEEGKK----------------------SPKSNHQEVLCLTDNP-DKSSLFKFEPIgSTKYKQKYVKKDSYFRLKH 130

                        170
                 ....*....|....*....
gi 310171    392 LCTNTWIQSTNAPIDVEEE 410
Cdd:cd23263  131 VNTNFWLHSHEKKFNINNK 149
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
113-167 2.10e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.25  E-value: 2.10e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 310171       113 GDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTL--DATGNEGSWLFIQPF 167
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
295-348 6.06e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 6.06e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 310171       295 GGAGHWNGLYRFKHLATGNYLAAEENPsykgdvsdPKAAGPGAQSRTGRRNAGE 348
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEK--------LPPWGDGQQEVTGYGNPAI 46
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
232-288 9.34e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.33  E-value: 9.34e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310171       232 EEVLKGGDVVRLFHAEQEKFLTCDE---YR---GKLQVFLRTtlrqsaTSATSSNALWEVEVV 288
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDeklPPwgdGQQEVTGYG------NPAIDANTLWLIEPV 57
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 232-319 1.28e-04

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: 45.26  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    232 EEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQvfLRTTLRQSATSATSSNALWEVEvvhhdPCR----GGAGHWNGLYRFK 307
Cdd:cd23290    5 EGYVTGGHVLRLFHGHMDECLTISAADSDDQ--RRLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQPLRIR 77

                         90
                 ....*....|..
gi 310171    308 HLATGNYLAAEE 319
Cdd:cd23290   78 HVTTGRYLALTE 89
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 237-320 1.65e-04

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: 44.99  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    237 GGDVVRLFHAEQEKFLTCDEYRGKLQVFlRTTLRQSATSATSSNALWEVEVVHHDPCrGGAGHWNGLYRFKHLATGNYLA 316
Cdd:cd23278    1 GGDVLRLFHGHMDECLTIPAAGSKEDQH-RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRYLA 78


                 ....
gi 310171    317 AEEN 320
Cdd:cd23278   79 LTED 82
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 235-320 2.64e-04

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: 44.52  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    235 LKGGDVVRLFHAEQEKFLTCDEYRGKLQvfLRTTLRQSATSATSSNALWEVEvvhhdPCR----GGAGHWNGLYRFKHLA 310
Cdd:cd23292    3 LLGGHVVRLFHGHDECLTIPSTDQSDEQ--HRVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRHLT 75

                         90
                 ....*....|
gi 310171    311 TGNYLAAEEN 320
Cdd:cd23292   76 TGHYLALTED 85
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1191-1303 3.10e-04

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: 44.50  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     1191 KKQQRLLKNMDAHKVML---DLLQIPY-----------DKNDNKMMEILRYTHQFLQKFCAGNPGNQALLHKHLQLFLTP 1256
Cdd:pfam01365   32 RQRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 310171     1257 --------GLLeaETMQHIFLNNYQLC-SEISEPVLQHFVHCWPTHGRHVQYLDFL 1303
Cdd:pfam01365  112 lgspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 216-315 4.10e-04

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: 43.86  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171    216 NTSWKI---NLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKlqvFLRTTLRQSA----TSATSSNALWEVEVV 288
Cdd:cd23276   44 NNWWQIlkpRGDPSSNPPDPEYVRDGDEVRLLHKETNRYLRTHDAAAP---VTSKHKEVSAypdeNEDGDDNDLWVVEIV 120

                         90       100       110
                 ....*....|....*....|....*....|
gi 310171    289 hHDPCRGGAGHWNGL---YRFKHLATGNYL 315
Cdd:cd23276  121 -KDEGKLEDKRIKPLttrFRLRNKKTGCYL 149
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2235-2527 5.28e-04

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 44.18  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2235 SPLISLLFWILICFSIAALFTKHYsvrplivalvlrsiyYLGIGPTLNILGALNLTNKIVFVVSFV------GNRGTFIR 2308
Cdd:pfam00520    1 SRYFELFILLLILLNTIFLALETY---------------FQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFR 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2309 gykamvmDMEFLYHVGYILTSVLGLFAHE-----------LFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALI 2377
Cdd:pfam00520   66 -------SPWNILDFVVVLPSLISLVLSSvgslsglrvlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2378 LVYLFSIVGFLFLKDDFILEVDRLPGNHSrastlgmphgaatfmgtcsgdkmdcvsevsvpeileedeeldsteraCDTL 2457
Cdd:pfam00520  139 FLFIFAIIGYQLFGGKLKTWENPDNGRTN-----------------------------------------------FDNF 171

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310171     2458 LMCIVTVMNhgLRNGGGVGDILRKPSkDESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2527
Cdd:pfam00520  172 PNAFLWLFQ--TMTTEGWGDIMYDTI-DGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
174-224 1.15e-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: 1.15e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 310171       174 GDNVVVGDKVILNPVNAGQPLHAS---NYELSDN---VGCKEVNSVNCNTSWKINLF 224
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdekLPPWGDGqqeVTGYGNPAIDANTLWLIEPV 57
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 116-184 6.09e-03

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: 40.39  E-value: 6.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 310171    116 VKYGSVIQLLHMKSNKYLTVNKRlPALLEKNAMRVTldATGNEGSWLFIQPFWKLRSNGDNVVVGDKVI 184
Cdd:cd23276   66 VRDGDEVRLLHKETNRYLRTHDA-AAPVTSKHKEVS--AYPDENEDGDDNDLWVVEIVKDEGKLEDKRI 131
 
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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