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Conserved domains on  [gi|58865832|ref|NP_001012131|]
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inositol polyphosphate 1-phosphatase isoform 1 [Rattus norvegicus]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10108167)

inositol monophosphatase family protein similar to human inositol polyphosphate 1-phosphatase (INPP1) which hydrolyzes the 1 position phosphate from inositol 1,4-bisphosphate (Ins(1,4)P2) or inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), and to human 3'(2'),5'-bisphosphate nucleotidase 1 (BPNT1) which converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP and has 1000-fold lower activity towards (Ins(1,4)P2) and (Ins(1,3,4)P3)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
4-384 1.26e-102

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


:

Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 305.40  E-value: 1.26e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   4 ILLELLRVSEKAANIARACRQQEALFQLLIEEKkgaekNKKFAADFKTLADVLVQEVIKQNMENKFPGLgkKVFGEESNE 83
Cdd:cd01640   1 LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGK-----TKEGANDFKTLADRLSQRVIKHSLQKQFPKL--KIIGEEDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832  84 FTNDLGEKITVELQSteketaellsrvlngnmlasEALAKVVHedvdltdptleSLEISIPQEILGIWVDPIDSTYQYIK 163
Cdd:cd01640  74 FENQEDESRDVDLDE--------------------EILEESCP-----------SPSKDLPEEDLGVWVDPLDATQEYTE 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 164 GSanvksnqgvfpsgLQCVTILIGVYDlqTGLPLMGVINQPFASQNLTTLRWTGQCYWGLSymGNNIHSLQLAisksnse 243
Cdd:cd01640 123 GL-------------LEYVTVLIGVAV--KGKPIAGVIHQPFYEKTAGAGAWLGRTIWGLS--GLGAHSSDFK------- 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 244 tqtensdrESSNPFSAVISTSEKDTIK--TALSDVCGGSVFPAAGAGYKSLCVVQGLADIYIFSEDTTYKWDSCAAHAIL 321
Cdd:cd01640 179 --------EREDAGKIIVSTSHSHSVKevQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKKWDICAPEAIL 250
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865832 322 RAMGGGIVDMKEclerspdtgldlPQLLYHVENKgasgvdlWANKGGLIAYRSRNrLDTFLSR 384
Cdd:cd01640 251 RALGGDMTDLHG------------EPLSYSKAVK-------PVNKGGLLATIRSN-HEAYLDK 293
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
4-384 1.26e-102

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 305.40  E-value: 1.26e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   4 ILLELLRVSEKAANIARACRQQEALFQLLIEEKkgaekNKKFAADFKTLADVLVQEVIKQNMENKFPGLgkKVFGEESNE 83
Cdd:cd01640   1 LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGK-----TKEGANDFKTLADRLSQRVIKHSLQKQFPKL--KIIGEEDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832  84 FTNDLGEKITVELQSteketaellsrvlngnmlasEALAKVVHedvdltdptleSLEISIPQEILGIWVDPIDSTYQYIK 163
Cdd:cd01640  74 FENQEDESRDVDLDE--------------------EILEESCP-----------SPSKDLPEEDLGVWVDPLDATQEYTE 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 164 GSanvksnqgvfpsgLQCVTILIGVYDlqTGLPLMGVINQPFASQNLTTLRWTGQCYWGLSymGNNIHSLQLAisksnse 243
Cdd:cd01640 123 GL-------------LEYVTVLIGVAV--KGKPIAGVIHQPFYEKTAGAGAWLGRTIWGLS--GLGAHSSDFK------- 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 244 tqtensdrESSNPFSAVISTSEKDTIK--TALSDVCGGSVFPAAGAGYKSLCVVQGLADIYIFSEDTTYKWDSCAAHAIL 321
Cdd:cd01640 179 --------EREDAGKIIVSTSHSHSVKevQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKKWDICAPEAIL 250
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865832 322 RAMGGGIVDMKEclerspdtgldlPQLLYHVENKgasgvdlWANKGGLIAYRSRNrLDTFLSR 384
Cdd:cd01640 251 RALGGDMTDLHG------------EPLSYSKAVK-------PVNKGGLLATIRSN-HEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
56-376 1.51e-50

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 170.99  E-value: 1.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832    56 LVQEVIKQNMENKFpGLGKKVFGEESNEFTNDLGEKitvelqSTEKETAELLSRVLNGNMLasEALAKVVHEDVDLTDPT 135
Cdd:pfam00459   1 DLEEVLKVAVELAA-KAGEILREAFSNKLTIEEKGK------SGANDLVTAADKAAEELIL--EALAALFPSHKIIGEEG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   136 LESLE-ISIPQEILGIWVDPIDSTYQYIKGSanvksnqgvfpsglQCVTILIGVYDlqTGLPLMGVINQPFASQNLTTLR 214
Cdd:pfam00459  72 GAKGDqTELTDDGPTWIIDPIDGTKNFVHGI--------------PQFAVSIGLAV--NGEPVLGVIYQPFAGQLYSAAK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   215 WTGQCYWGLsymgnnihslQLAISKSNSetqTENSDRESSNPFSAVISTSEKDTIKTALSDVCGGSVFpAAGAGYKSLC- 293
Cdd:pfam00459 136 GKGAFLNGQ----------PLPVSRAPP---LSEALLVTLFGVSSRKDTSEASFLAKLLKLVRAPGVR-RVGSAALKLAm 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   294 VVQGLADIYIFSeDTTYKWDSCAAHAILRAMGGGIVDMKEClerspdtGLDLPQLLYHVENkgasgvdLWANKGGLIAYR 373
Cdd:pfam00459 202 VAAGKADAYIEF-GRLKPWDHAAGVAILREAGGVVTDADGG-------PFDLLAGRVIAAN-------PKVLHELLAAAL 266

                  ...
gi 58865832   374 SRN 376
Cdd:pfam00459 267 EEI 269
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
4-384 1.26e-102

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 305.40  E-value: 1.26e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   4 ILLELLRVSEKAANIARACRQQEALFQLLIEEKkgaekNKKFAADFKTLADVLVQEVIKQNMENKFPGLgkKVFGEESNE 83
Cdd:cd01640   1 LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGK-----TKEGANDFKTLADRLSQRVIKHSLQKQFPKL--KIIGEEDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832  84 FTNDLGEKITVELQSteketaellsrvlngnmlasEALAKVVHedvdltdptleSLEISIPQEILGIWVDPIDSTYQYIK 163
Cdd:cd01640  74 FENQEDESRDVDLDE--------------------EILEESCP-----------SPSKDLPEEDLGVWVDPLDATQEYTE 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 164 GSanvksnqgvfpsgLQCVTILIGVYDlqTGLPLMGVINQPFASQNLTTLRWTGQCYWGLSymGNNIHSLQLAisksnse 243
Cdd:cd01640 123 GL-------------LEYVTVLIGVAV--KGKPIAGVIHQPFYEKTAGAGAWLGRTIWGLS--GLGAHSSDFK------- 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 244 tqtensdrESSNPFSAVISTSEKDTIK--TALSDVCGGSVFPAAGAGYKSLCVVQGLADIYIFSEDTTYKWDSCAAHAIL 321
Cdd:cd01640 179 --------EREDAGKIIVSTSHSHSVKevQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKKWDICAPEAIL 250
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865832 322 RAMGGGIVDMKEclerspdtgldlPQLLYHVENKgasgvdlWANKGGLIAYRSRNrLDTFLSR 384
Cdd:cd01640 251 RALGGDMTDLHG------------EPLSYSKAVK-------PVNKGGLLATIRSN-HEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
56-376 1.51e-50

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 170.99  E-value: 1.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832    56 LVQEVIKQNMENKFpGLGKKVFGEESNEFTNDLGEKitvelqSTEKETAELLSRVLNGNMLasEALAKVVHEDVDLTDPT 135
Cdd:pfam00459   1 DLEEVLKVAVELAA-KAGEILREAFSNKLTIEEKGK------SGANDLVTAADKAAEELIL--EALAALFPSHKIIGEEG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   136 LESLE-ISIPQEILGIWVDPIDSTYQYIKGSanvksnqgvfpsglQCVTILIGVYDlqTGLPLMGVINQPFASQNLTTLR 214
Cdd:pfam00459  72 GAKGDqTELTDDGPTWIIDPIDGTKNFVHGI--------------PQFAVSIGLAV--NGEPVLGVIYQPFAGQLYSAAK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   215 WTGQCYWGLsymgnnihslQLAISKSNSetqTENSDRESSNPFSAVISTSEKDTIKTALSDVCGGSVFpAAGAGYKSLC- 293
Cdd:pfam00459 136 GKGAFLNGQ----------PLPVSRAPP---LSEALLVTLFGVSSRKDTSEASFLAKLLKLVRAPGVR-RVGSAALKLAm 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   294 VVQGLADIYIFSeDTTYKWDSCAAHAILRAMGGGIVDMKEClerspdtGLDLPQLLYHVENkgasgvdLWANKGGLIAYR 373
Cdd:pfam00459 202 VAAGKADAYIEF-GRLKPWDHAAGVAILREAGGVVTDADGG-------PFDLLAGRVIAAN-------PKVLHELLAAAL 266

                  ...
gi 58865832   374 SRN 376
Cdd:pfam00459 267 EEI 269
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
5-330 1.40e-29

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


Pssm-ID: 238814 [Multi-domain]  Cd Length: 184  Bit Score: 112.87  E-value: 1.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   5 LLELLRVSEKAANIARACRQQEALFQLlieekkgaeKNKKFAADFKTLADVLVQEVIKQNMENKFPGlgKKVFGEESNEF 84
Cdd:cd01636   1 LEELCRVAKEAGLAILKAFGRELSGKV---------KITKSDNDPVTTADVAAETLIRNMLKSSFPD--VKIVGEESGVA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832  85 TNDlgekitvelqsteketaellsrvlngnmlasealakvvhedvdltdptlesleiSIPQEILGIWVDPIDSTYQYIKG 164
Cdd:cd01636  70 EEV------------------------------------------------------MGRRDEYTWVIDPIDGTKNFING 95
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 165 sanvksnqgvfpsgLQCVTILIGVYdlqtglplmgvinqpfasqnlttlrwtgqcywglsymgnnihslqlaisksnset 244
Cdd:cd01636  96 --------------LPFVAVVIAVY------------------------------------------------------- 106
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 245 qtensdressnpfsaVISTSEKDTIKT------ALSDVCGGSVFPAAGAGYKSLCVVQGLADIYIFSEDTTYKWDSCAAH 318
Cdd:cd01636 107 ---------------VILILAEPSHKRvdekkaELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGKRRAWDVAASA 171
                       330
                ....*....|..
gi 58865832 319 AILRAMGGGIVD 330
Cdd:cd01636 172 AIVREAGGIMTD 183
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
8-334 1.37e-21

Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.


Pssm-ID: 238815 [Multi-domain]  Cd Length: 238  Bit Score: 92.76  E-value: 1.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832   8 LLRVSEKAANIARACRQQEAlfqllieekkgAEKNKKFAADFKTLADVLVQEVIKQNMENKFPGlgKKVFGEESNEFTND 87
Cdd:cd01637   4 ALKAVREAGALILEAFGEEL-----------TVETKKGDGDLVTEADLAAEELIVDVLKALFPD--DGILGEEGGGSGNV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832  88 LGEKITVelqsteketaellsrvlngnmlasealakvvhedvdltdptlesleisipqeilgiWVDPIDSTYQYIKGsan 167
Cdd:cd01637  71 SDGGRVW--------------------------------------------------------VIDPIDGTTNFVAG--- 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 168 vksnqgvfpsgLQCVTILIGVYDlqTGLPLMGVINQPFAsqnlttlrwtGQCYWGLSYMGNNIHSLQLAISKSNSetqte 247
Cdd:cd01637  92 -----------LPNFAVSIALYE--DGKPVLGVIYDPML----------DELYYAGRGKGAFLNGKKLPLSKDTP----- 143
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 248 nsDRESSNPFSAVISTSEKDTIKTALSDVCGGsVFPAAGAGYKSLCVVQGLADIYIFSEDTtyKWDSCAAHAILRAMGGG 327
Cdd:cd01637 144 --LNDALLSTNASMLRSNRAAVLASLVNRALG-IRIYGSAGLDLAYVAAGRLDAYLSSGLN--PWDYAAGALIVEEAGGI 218

                ....*..
gi 58865832 328 IVDMKEC 334
Cdd:cd01637 219 VTDLDGE 225
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
151-330 6.58e-05

Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate fructose-1,6-bisphosphate, inositol monophospate, 3'-phosphoadenosine-5'-phosphate, or similar substrates.


Pssm-ID: 238819 [Multi-domain]  Cd Length: 248  Bit Score: 44.17  E-value: 6.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 151 WV-DPIDSTYQYIKGsanvksnqgvFPSglqcVTILIGVydLQTGLPLMGVINQPFasqnlttlrwTGQCYWGLSYMGnn 229
Cdd:cd01641  75 WVlDPIDGTKSFIRG----------LPV----WGTLIAL--LHDGRPVLGVIDQPA----------LGERWIGARGGG-- 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865832 230 ihslqlaiSKSNSETQTENSDRESSNPFSAVISTSEKDTIKTA-------LSDVCGGSVFPAAGAGYKSLCvvQGLADIY 302
Cdd:cd01641 127 --------TFLNGAGGRPLRVRACADLAEAVLSTTDPHFFTPGdraaferLARAVRLTRYGGDCYAYALVA--SGRVDLV 196
                       170       180
                ....*....|....*....|....*....
gi 58865832 303 IfseDTTYK-WDSCAAHAILRAMGGGIVD 330
Cdd:cd01641 197 V---EAGLKpYDVAALIPIIEGAGGVITD 222
 
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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