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Conserved domains on  [gi|2462572806|ref|XP_054197806|]
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inositol polyphosphate 1-phosphatase isoform X1 [Homo sapiens]

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 ...
4-387 3.16e-96

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: 289.22  E-value: 3.16e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806   4 ILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGeknkkFAVDFKTLADVLVQEVIKQNMENKFPGLekNIFGEESNE 83
Cdd:cd01640     1 LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGKTKE-----GANDFKTLADRLSQRVIKHSLQKQFPKL--KIIGEEDNE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806  84 FTNDWGEKITLRLcsteeetaellskvlngnkvASEALARVVHqdvaftdptldSTEINVPQDILGIWVDPIDSTYQYIK 163
Cdd:cd01640    74 FENQEDESRDVDL--------------------DEEILEESCP-----------SPSKDLPEEDLGVWVDPLDATQEYTE 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 164 GSadiksnqgifpcgLQCVTILIGVYDiqTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTnmHSLQLtisrrngs 243
Cdd:cd01640   123 GL-------------LEYVTVLIGVAV--KGKPIAGVIHQPFYEKTAGAGAWLGRTIWGLSGLGA--HSSDF-------- 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 244 ethtgntgseAAFSPSFSAVISTSEKETIK--AALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAH 321
Cdd:cd01640   178 ----------KEREDAGKIIVSTSHSHSVKevQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKKWDICAPE 247
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572806 322 AILRAMGGGIVDLKEclernpetgldlPQLVYHVEnegaagvDRWANKGGLIAYRsRKRLETFLSL 387
Cdd:cd01640   248 AILRALGGDMTDLHG------------EPLSYSKA-------VKPVNKGGLLATI-RSNHEAYLDK 293
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
4-387 3.16e-96

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: 289.22  E-value: 3.16e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806   4 ILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGeknkkFAVDFKTLADVLVQEVIKQNMENKFPGLekNIFGEESNE 83
Cdd:cd01640     1 LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGKTKE-----GANDFKTLADRLSQRVIKHSLQKQFPKL--KIIGEEDNE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806  84 FTNDWGEKITLRLcsteeetaellskvlngnkvASEALARVVHqdvaftdptldSTEINVPQDILGIWVDPIDSTYQYIK 163
Cdd:cd01640    74 FENQEDESRDVDL--------------------DEEILEESCP-----------SPSKDLPEEDLGVWVDPLDATQEYTE 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 164 GSadiksnqgifpcgLQCVTILIGVYDiqTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTnmHSLQLtisrrngs 243
Cdd:cd01640   123 GL-------------LEYVTVLIGVAV--KGKPIAGVIHQPFYEKTAGAGAWLGRTIWGLSGLGA--HSSDF-------- 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 244 ethtgntgseAAFSPSFSAVISTSEKETIK--AALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAH 321
Cdd:cd01640   178 ----------KEREDAGKIIVSTSHSHSVKevQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKKWDICAPE 247
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572806 322 AILRAMGGGIVDLKEclernpetgldlPQLVYHVEnegaagvDRWANKGGLIAYRsRKRLETFLSL 387
Cdd:cd01640   248 AILRALGGDMTDLHG------------EPLSYSKA-------VKPVNKGGLLATI-RSNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
56-378 3.62e-44

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 154.42  E-value: 3.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806  56 LVQEVIKQNMENKFPGLEKnIFGEESNEFTNDWGEKitlrlcSTEEETAELLSKVLNGNKVasEALARVVHQDVAFTDPT 135
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEI-LREAFSNKLTIEEKGK------SGANDLVTAADKAAEELIL--EALAALFPSHKIIGEEG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 136 LDSTE-INVPQDILGIWVDPIDSTYQYIKGSadiksnqgifpcglQCVTILIGVYDiqTGVPLMGVINQPFVSRDPNTLR 214
Cdd:pfam00459  72 GAKGDqTELTDDGPTWIIDPIDGTKNFVHGI--------------PQFAVSIGLAV--NGEPVLGVIYQPFAGQLYSAAK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 215 WKGQCYWGLsymgtnmhslQLTISRRngseTHTGNTGSEAAFSpsFSAVISTSEKETIKAALSRVCGDRIFgAAGAGYKS 294
Cdd:pfam00459 136 GKGAFLNGQ----------PLPVSRA----PPLSEALLVTLFG--VSSRKDTSEASFLAKLLKLVRAPGVR-RVGSAALK 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 295 LC-VVQGLVDIYIFSeDTTFKWDSCAAHAILRAMGGGIVDLKEClernpetGLDLPQLVYHVENegaagvdRWANKGGLI 373
Cdd:pfam00459 199 LAmVAAGKADAYIEF-GRLKPWDHAAGVAILREAGGVVTDADGG-------PFDLLAGRVIAAN-------PKVLHELLA 263

                  ....*
gi 2462572806 374 AYRSR 378
Cdd:pfam00459 264 AALEE 268
 
Name Accession Description Interval E-value
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
4-387 3.16e-96

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: 289.22  E-value: 3.16e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806   4 ILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGeknkkFAVDFKTLADVLVQEVIKQNMENKFPGLekNIFGEESNE 83
Cdd:cd01640     1 LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGKTKE-----GANDFKTLADRLSQRVIKHSLQKQFPKL--KIIGEEDNE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806  84 FTNDWGEKITLRLcsteeetaellskvlngnkvASEALARVVHqdvaftdptldSTEINVPQDILGIWVDPIDSTYQYIK 163
Cdd:cd01640    74 FENQEDESRDVDL--------------------DEEILEESCP-----------SPSKDLPEEDLGVWVDPLDATQEYTE 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 164 GSadiksnqgifpcgLQCVTILIGVYDiqTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTnmHSLQLtisrrngs 243
Cdd:cd01640   123 GL-------------LEYVTVLIGVAV--KGKPIAGVIHQPFYEKTAGAGAWLGRTIWGLSGLGA--HSSDF-------- 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 244 ethtgntgseAAFSPSFSAVISTSEKETIK--AALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAH 321
Cdd:cd01640   178 ----------KEREDAGKIIVSTSHSHSVKevQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIKKWDICAPE 247
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572806 322 AILRAMGGGIVDLKEclernpetgldlPQLVYHVEnegaagvDRWANKGGLIAYRsRKRLETFLSL 387
Cdd:cd01640   248 AILRALGGDMTDLHG------------EPLSYSKA-------VKPVNKGGLLATI-RSNHEAYLDK 293
Inositol_P pfam00459
Inositol monophosphatase family;
56-378 3.62e-44

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 154.42  E-value: 3.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806  56 LVQEVIKQNMENKFPGLEKnIFGEESNEFTNDWGEKitlrlcSTEEETAELLSKVLNGNKVasEALARVVHQDVAFTDPT 135
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEI-LREAFSNKLTIEEKGK------SGANDLVTAADKAAEELIL--EALAALFPSHKIIGEEG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 136 LDSTE-INVPQDILGIWVDPIDSTYQYIKGSadiksnqgifpcglQCVTILIGVYDiqTGVPLMGVINQPFVSRDPNTLR 214
Cdd:pfam00459  72 GAKGDqTELTDDGPTWIIDPIDGTKNFVHGI--------------PQFAVSIGLAV--NGEPVLGVIYQPFAGQLYSAAK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 215 WKGQCYWGLsymgtnmhslQLTISRRngseTHTGNTGSEAAFSpsFSAVISTSEKETIKAALSRVCGDRIFgAAGAGYKS 294
Cdd:pfam00459 136 GKGAFLNGQ----------PLPVSRA----PPLSEALLVTLFG--VSSRKDTSEASFLAKLLKLVRAPGVR-RVGSAALK 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 295 LC-VVQGLVDIYIFSeDTTFKWDSCAAHAILRAMGGGIVDLKEClernpetGLDLPQLVYHVENegaagvdRWANKGGLI 373
Cdd:pfam00459 199 LAmVAAGKADAYIEF-GRLKPWDHAAGVAILREAGGVVTDADGG-------PFDLLAGRVIAAN-------PKVLHELLA 263

                  ....*
gi 2462572806 374 AYRSR 378
Cdd:pfam00459 264 AALEE 268
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
5-334 2.02e-28

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: 109.79  E-value: 2.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806   5 LRELLCVSEKAANIARACRQQEALFQLLIEEkkegeknkkFAVDFKTLADVLVQEVIKQNMENKFPGleKNIFGEESNEF 84
Cdd:cd01636     1 LEELCRVAKEAGLAILKAFGRELSGKVKITK---------SDNDPVTTADVAAETLIRNMLKSSFPD--VKIVGEESGVA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806  85 TNDWGekitlrlcsteeetaellskvlngnkvasealarvvhqdvaftdptldsteinvPQDILGIWVDPIDSTYQYIKG 164
Cdd:cd01636    70 EEVMG------------------------------------------------------RRDEYTWVIDPIDGTKNFING 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 165 sadiksnqgifpcgLQCVTILIGVYDIqtgvplmgvinqpfvsrdpntlrwkgqcywglsymgtnmhslqlTISRRNGSE 244
Cdd:cd01636    96 --------------LPFVAVVIAVYVI--------------------------------------------LILAEPSHK 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 245 THTGNtgseaafspsfsavistseketiKAALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAHAIL 324
Cdd:cd01636   118 RVDEK-----------------------KAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGKRRAWDVAASAAIV 174
                         330
                  ....*....|
gi 2462572806 325 RAMGGGIVDL 334
Cdd:cd01636   175 REAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
6-337 2.87e-24

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: 100.08  E-value: 2.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806   6 RELLC-VSEKAANIARACRQQEAlfqllieekkeGEKNKKFAVDFKTLADVLVQEVIKQNMENKFPGleKNIFGEESNEf 84
Cdd:cd01637     1 LELALkAVREAGALILEAFGEEL-----------TVETKKGDGDLVTEADLAAEELIVDVLKALFPD--DGILGEEGGG- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806  85 tndwgekitlrlcsteeetaellskvlngnkvasealarvvhqdvaftdptldstEINVPQDILGIWVDPIDSTYQYIKG 164
Cdd:cd01637    67 -------------------------------------------------------SGNVSDGGRVWVIDPIDGTTNFVAG 91
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 165 sadiksnqgifpcgLQCVTILIGVYDIqtGVPLMGVINQPFvsrdpntlrwKGQCYWGLSYMGTNMHSLQLTISRRNGSE 244
Cdd:cd01637    92 --------------LPNFAVSIALYED--GKPVLGVIYDPM----------LDELYYAGRGKGAFLNGKKLPLSKDTPLN 145
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 245 THtgNTGSEAAFSPSFSAvistsekETIKAALSRVCGDRIFGAAGagYKSLCVVQGLVDIYIFSEDttFKWDSCAAHAIL 324
Cdd:cd01637   146 DA--LLSTNASMLRSNRA-------AVLASLVNRALGIRIYGSAG--LDLAYVAAGRLDAYLSSGL--NPWDYAAGALIV 212
                         330
                  ....*....|...
gi 2462572806 325 RAMGGGIVDLKEC 337
Cdd:cd01637   213 EEAGGIVTDLDGE 225
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
151-334 3.86e-07

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: 50.72  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 151 WV-DPIDSTyqyikgsadiKSnqgiFPCGLQCVTILIGVYDiqTGVPLMGVINQPFVsrdpntlrwkGQCYWGLSYMGTN 229
Cdd:cd01641    75 WVlDPIDGT----------KS----FIRGLPVWGTLIALLH--DGRPVLGVIDQPAL----------GERWIGARGGGTF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572806 230 MhslqltiSRRNGSETHTgntgSEAAfSPSfSAVISTSEKETIKAA-------LSRVCGDRIFGAAGAGYKSLCvvQGLV 302
Cdd:cd01641   129 L-------NGAGGRPLRV----RACA-DLA-EAVLSTTDPHFFTPGdraaferLARAVRLTRYGGDCYAYALVA--SGRV 193
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462572806 303 DIYIfseDTTFK-WDSCAAHAILRAMGGGIVDL 334
Cdd:cd01641   194 DLVV---EAGLKpYDVAALIPIIEGAGGVITDW 223
 
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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