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Conserved domains on  [gi|386781117|ref|NP_001247575|]
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inositol polyphosphate 5-phosphatase K [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 14-320 9.40e-142

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


The actual alignment was detected with superfamily member cd09094:

Pssm-ID: 469791  Cd Length: 300  Bit Score: 407.53  E-value: 9.40e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSDLLQLNNQNLNLDIYVIGLQELNSGIISLLSDAAFNDSWSSFLMDVLSPLSFVKVSHVRM 93
Cdd:cd09094    1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  94 QGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNC 173
Cdd:cd09094   81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 174 EGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNS 253
Cdd:cd09094  161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386781117 254 NDYDTSEKKRKPAWTDRILWRLKrqPQAGPDTPRLpapdfSLSLRSYSSHMVYSISDHKPVTGTFDL 320
Cdd:cd09094  241 DEYDTSGKKRKPAWTDRILWKVN--PDASTEEKFL-----SITQTSYKSHMEYGISDHKPVTAQFRL 300
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 331-431 1.63e-36

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


:

Pssm-ID: 465482  Cd Length: 102  Bit Score: 129.67  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  331 IVLMPEDLWTV-ENDMMVSYSSTLDFPSSPWDWIGLYKVGLRDINDYVSYAWVGDSQVSCSDNLNQVYIDISNIP-ATED 408
Cdd:pfam17751   1 VVFQNVGEWYPpDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPkEPEG 80

                          90       100
                  ....*....|....*....|...
gi 386781117  409 EFLLCYYSNSLrSVVGISRPFQI 431
Cdd:pfam17751  81 FYQFCYVSNLG-SVVGISTPFQF 102
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 14-320 9.40e-142

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate 5-phosphatase J and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase J (INPP5J), also known as PIB5PA or PIPP, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5J hydrolyzes PI(4,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4 at ruffling membranes. These proteins contain a C-terminal, SKIP carboxyl homology domain (SKICH), which may direct plasma membrane ruffle localization.


Pssm-ID: 197328  Cd Length: 300  Bit Score: 407.53  E-value: 9.40e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSDLLQLNNQNLNLDIYVIGLQELNSGIISLLSDAAFNDSWSSFLMDVLSPLSFVKVSHVRM 93
Cdd:cd09094    1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  94 QGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNC 173
Cdd:cd09094   81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 174 EGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNS 253
Cdd:cd09094  161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386781117 254 NDYDTSEKKRKPAWTDRILWRLKrqPQAGPDTPRLpapdfSLSLRSYSSHMVYSISDHKPVTGTFDL 320
Cdd:cd09094  241 DEYDTSGKKRKPAWTDRILWKVN--PDASTEEKFL-----SITQTSYKSHMEYGISDHKPVTAQFRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 12-323 6.03e-104

Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+)-sensitive enzymes.


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 311.21  E-value: 6.03e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117    12 RRLSIHVVTWNVASAAPPL-DLSD---LLQLNNQNLNLDIYVIGLQELNSGI--ISLLSDAAFNDSWSSFLMDVLSP-LS 84
Cdd:smart00128   1 RDIKVLIGTWNVGGLESPKvDVTSwlfQKIEVKQSEKPDIYVIGLQEVVGLApgVILETIAGKERLWSDLLESSLNGdGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117    85 FVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHF 164
Cdd:smart00128  81 YNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117   165 DRILEMQNCEGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFP 244
Cdd:smart00128 161 KTILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117   245 PTYKFDR-NSNDYDTSEKKRKPAWTDRILWRLKrqpqagpdtprlpAPDFsLSLRSYSSHMVYSISDHKPVTGTFDLELK 323
Cdd:smart00128 241 PTYKYDSvGTETYDTSEKKRVPAWCDRILYRSN-------------GPEL-IQLSEYHSGMEITTSDHKPVFATFRLKVT 306
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
12-323 3.72e-39

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 146.85  E-value: 3.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  12 RRLSIHVVTWNVASAAPPLDLSDLLQ-LNNQNLNLDIYVIGLQE---LNSGIISLLSDAAFNDSWSSFLMDVLS-PLSFV 86
Cdd:COG5411   28 KDVSIFVSTFNPPGKPPKASTKRWLFpEIEATELADLYVVGLQEvveLTPGSILSADPYDRLRIWESKVLDCLNgAQSDE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  87 KVSHVR---MQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEH 163
Cdd:COG5411  108 KYSLLRspqLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 164 FDRIleMQNCEGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCY-SGLWEKDQLSIAKKHDPLLREFQEGRLL 242
Cdd:COG5411  188 YRSI--ASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGRlDKLFEYDQLLWEMEVGNVFPGFKEPVIT 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 243 FPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRlkrqpqagpdtprlpapdfSLSLR--SYSSHMVYSISDHKPVTGTFDL 320
Cdd:COG5411  266 FPPTYKFDYGTDEYDTSDKGRIPSWTDRILYK-------------------SEQLTphSYSSIPHLMISDHRPVYATFRA 326


                 ...
gi 386781117 321 ELK 323
Cdd:COG5411  327 KIK 329
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 331-431 1.63e-36

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


Pssm-ID: 465482  Cd Length: 102  Bit Score: 129.67  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  331 IVLMPEDLWTV-ENDMMVSYSSTLDFPSSPWDWIGLYKVGLRDINDYVSYAWVGDSQVSCSDNLNQVYIDISNIP-ATED 408
Cdd:pfam17751   1 VVFQNVGEWYPpDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPkEPEG 80

                          90       100
                  ....*....|....*....|...
gi 386781117  409 EFLLCYYSNSLrSVVGISRPFQI 431
Cdd:pfam17751  81 FYQFCYVSNLG-SVVGISTPFQF 102
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 84-323 3.54e-24

Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 105.37  E-value: 3.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  84 SFVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPP-HISNNYQRLE 162
Cdd:PLN03191 363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRRN 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 163 ----------HFDRILEMQncEGRDIPNildHDLIIWFGDMNFRIEDFGLHfVRESIKNRCYSGLWEKDQLSIAKKHDPL 232
Cdd:PLN03191 443 advyeiirrtRFSSVLDTD--QPQTIPS---HDQIFWFGDLNYRLNMLDTE-VRKLVAQKRWDELINSDQLIKELRSGHV 516

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 233 LREFQEGRLLFPPTYKFDRNSNDY-----DTSEKKRKPAWTDRILWRLKRQPQAgpdtprlpapdfslslrSYSSHMVyS 307
Cdd:PLN03191 517 FDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQL-----------------CYKRSEI-R 578

                        250
                 ....*....|....*.
gi 386781117 308 ISDHKPVTGTFDLELK 323
Cdd:PLN03191 579 LSDHRPVSSMFLVEVE 594
 
Name Accession Description Interval E-value
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 14-320 9.40e-142

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate 5-phosphatase J and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase J (INPP5J), also known as PIB5PA or PIPP, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5J hydrolyzes PI(4,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4 at ruffling membranes. These proteins contain a C-terminal, SKIP carboxyl homology domain (SKICH), which may direct plasma membrane ruffle localization.


Pssm-ID: 197328  Cd Length: 300  Bit Score: 407.53  E-value: 9.40e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSDLLQLNNQNLNLDIYVIGLQELNSGIISLLSDAAFNDSWSSFLMDVLSPLSFVKVSHVRM 93
Cdd:cd09094    1 LRVYVVTWNVATAPPPIDVRSLLGLQSPEVAPDIYIIGLQEVNSKPVQFVSDLIFDDPWSDLFMDILSPKGYVKVSSIRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  94 QGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNC 173
Cdd:cd09094   81 QGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLNCHLPAHMEKWEQRIDDFETILSTQVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 174 EGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNS 253
Cdd:cd09094  161 NECNTPSILDHDYVFWFGDLNFRIEDVSIEFVRELVNSKKYHLLLEKDQLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386781117 254 NDYDTSEKKRKPAWTDRILWRLKrqPQAGPDTPRLpapdfSLSLRSYSSHMVYSISDHKPVTGTFDL 320
Cdd:cd09094  241 DEYDTSGKKRKPAWTDRILWKVN--PDASTEEKFL-----SITQTSYKSHMEYGISDHKPVTAQFRL 300
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 12-323 6.03e-104

Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+)-sensitive enzymes.


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 311.21  E-value: 6.03e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117    12 RRLSIHVVTWNVASAAPPL-DLSD---LLQLNNQNLNLDIYVIGLQELNSGI--ISLLSDAAFNDSWSSFLMDVLSP-LS 84
Cdd:smart00128   1 RDIKVLIGTWNVGGLESPKvDVTSwlfQKIEVKQSEKPDIYVIGLQEVVGLApgVILETIAGKERLWSDLLESSLNGdGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117    85 FVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHF 164
Cdd:smart00128  81 YNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAGASNVEQRNQDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117   165 DRILEMQNCEGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFP 244
Cdd:smart00128 161 KTILRALSFPERALLSQFDHDVVFWFGDLNFRLDSPSYEEVRRKISKKEFDDLLEKDQLNRQREAGKVFKGFQEGPITFP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117   245 PTYKFDR-NSNDYDTSEKKRKPAWTDRILWRLKrqpqagpdtprlpAPDFsLSLRSYSSHMVYSISDHKPVTGTFDLELK 323
Cdd:smart00128 241 PTYKYDSvGTETYDTSEKKRVPAWCDRILYRSN-------------GPEL-IQLSEYHSGMEITTSDHKPVFATFRLKVT 306
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 14-320 1.85e-85

Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate 5-phosphatases (5-phosphatases) are signal-modifying enzymes, which hydrolyze the 5-phosphate from the inositol ring of specific 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), such as PI(4,5)P2, PI(3,4,5)P3, PI(3,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4. These enzymes are Mg2+-dependent, and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, 5-phosphatases often contain additional domains and motifs, such as the SH2 domain, the Sac-1 domain, the proline-rich domain (PRD), CAAX, RhoGAP (RhoGTPase-activating protein), and SKICH [SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) carboxyl homology] domains, that are important for protein-protein interactions and/or for the subcellular localization of these enzymes. 5-phosphatases incorporate into large signaling complexes, and regulate diverse cellular processes including postsynaptic vesicular trafficking, insulin signaling, cell growth and survival, and endocytosis. Loss or gain of function of 5-phosphatases is implicated in certain human diseases. This family also contains a functionally unrelated nitric oxide transport protein, Cimex lectularius (bedbug) nitrophorin, which catalyzes a heme-assisted S-nitrosation of a proximal thiolate; the heme however binds at a site distinct from the active site of the 5-phosphatases.


Pssm-ID: 197308 [Multi-domain]  Cd Length: 299  Bit Score: 263.81  E-value: 1.85e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSDLLQLNNQNLNLDIYVIGLQELN--SGIISLLSDAAFNDSWSSFLMDVLSPLS-FVKVSH 90
Cdd:cd09074    1 VKIFVVTWNVGGGISPPENLENWLSPKGTEAPDIYAVGVQEVDmsVQGFVGNDDSAKAREWVDNIQEALNEKEnYVLLGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  91 VRMQGILLLVFAKYQHLPYIQILSTKSTP--TGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRIL 168
Cdd:cd09074   81 AQLVGIFLFVFVKKEHLPQIKDLEVEGVTvgTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAGQEEVERRNQDYRDIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 169 -EMQNCEG-RDIPNILDHDLIIWFGDMNFRIEDFGLHfVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPT 246
Cdd:cd09074  161 sKLKFYRGdPAIDSIFDHDVVFWFGDLNYRIDSTDDE-VRKLISQGDLDDLLEKDQLKKQKEKGKVFDGFQELPITFPPT 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781117 247 YKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQPQAgpdtprlpapdfslSLRSYSSHMVYSISDHKPVTGTFDL 320
Cdd:cd09074  240 YKFDPGTDEYDTSDKKRIPAWCDRILYKSKAGSEI--------------QPLSYTSVPLYKTSDHKPVRATFRV 299
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 14-319 1.61e-76

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol polyphosphate 5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and related proteins; This subfamily contains the INPP5c domain of type II inositol polyphosphate 5-phosphatase I (INPP5B), Oculocerebrorenal syndrome of Lowe 1 (OCRL-1), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5B and OCRL1 preferentially hydrolyze the 5-phosphate of phosphatidylinositol (4,5)- bisphosphate [PI(4,5)P2] and phosphatidylinositol (3,4,5)- trisphosphate [PI(3,4,5)P3]. INPP5B can also hydrolyze soluble inositol (1,4,5)-trisphosphate [I(1,4,5)P3] and inositol (1,3,4,5)-tetrakisphosphate [I(1,3,4,5)P4]. INPP5B participates in the endocytic pathway and in the early secretory pathway. In the latter, it may function in retrograde ERGIC (ER-to-Golgi intermediate compartment)-to-ER transport; it binds specific RAB proteins within the secretory pathway. In the endocytic pathway, it binds RAB5 and during endocytosis, may function in a RAB5-controlled cascade for converting PI(3,4,5)P3 to phosphatidylinositol 3-phosphate (PI3P). This cascade may link growth factor signaling and membrane dynamics. Mutation in OCRL1 is implicated in Lowe syndrome, an X-linked recessive multisystem disorder, which includes defects in eye, brain, and kidney function, and in Type 2 Dent's disease, a disorder with only the renal symptoms. OCRL-1 may have a role in membrane trafficking within the endocytic pathway and at the trans-Golgi network, and may participate in actin dynamics or signaling from endomembranes. OCRL1 and INPP5B have overlapping functions: deletion of both 5-phosphatases in mice is embryonic lethal, deletion of OCRL1 alone has no phenotype, and deletion of Inpp5b alone has only a mild phenotype (male sterility). Several of the proteins that interact with OCRL1 also bind INPP5B, for examples, inositol polyphosphate phosphatase interacting protein of 27kDa (IPIP27)A and B (also known as Ses1 and 2), and endocytic signaling adaptor APPL1. OCRL1, but not INPP5B, binds clathrin heavy chain, the plasma membrane AP2 adaptor subunit alpha-adaptin. In addition to this INPP5c domain, most proteins in this subfamily have a C-terminal RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain.


Pssm-ID: 197327  Cd Length: 292  Bit Score: 240.29  E-value: 1.61e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNV--ASAAPPLD--LSdllqlnNQNLNLDIYVIGLQELNsgiislLSDAAF--NDS-----WSSFLMDVLSP 82
Cdd:cd09093    1 FRIFVGTWNVngQSPDESLRpwLS------CDEEPPDIYAIGFQELD------LSAEAFlfNDSsreqeWVKAVERGLHP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  83 -LSFVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRL 161
Cdd:cd09093   69 dAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHLAAHMEEVERRN 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 162 EHFDRILE-MQNCEGRDIP-NILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEG 239
Cdd:cd09093  149 QDYKDICArMKFEDPDGPPlSISDHDVVFWLGDLNYRIQELPTEEVKELIEKNDLEELLKYDQLNIQRRAGKVFEGFTEG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 240 RLLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRqpqagpdtprlpapdfsLSLRSYSSHMVYSISDHKPVTGTFD 319
Cdd:cd09093  229 EINFIPTYKYDPGTDNWDSSEKCRAPAWCDRILWRGTN-----------------IVQLSYRSHMELKTSDHKPVSALFD 291
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 14-318 1.26e-59

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae Inp51p, Inp52p, and Inp53p, and related proteins; This subfamily contains the INPP5c domain of three Saccharomyces cerevisiae synaptojanin-like inositol polyphosphate 5-phosphatases (INP51, INP52, and INP53), Schizosaccharomyces pombe synaptojanin (SPsynaptojanin), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, these proteins have an N-terminal catalytic Sac1-like domain (found in other proteins including the phophoinositide phosphatase Sac1p), and a C-terminal proline-rich domain (PRD). The Sac1 domain allows Inp52p and Inp53p to recognize and dephosphorylate a wider range of substrates including PI3P, PI4P, and PI(3,5)P2. The Sac1 domain of Inp51p is non-functional. Disruption of any two of INP51, INP52, and INP53, in S. cerevisiae leads to abnormal vacuolar and plasma membrane morphology. During hyperosmotic stress, Inp52p and Inp53p localize at actin patches, where they may facilitate the hydrolysis of PI(4,5)P2, and consequently promote actin rearrangement to regulate cell growth. SPsynaptojanin is also active against a range of soluble and lipid inositol phosphates, including I(1,4,5)P3, I(1,3,4,5)P4, I(1,4,5,6)P4, PI(4,5)P2, and PIP3. Transformation of S. cerevisiae with a plasmid expressing the SPsynaptojanin 5-phosphatase domain rescues inp51/inp52/inp53 triple-mutant strains.


Pssm-ID: 197324  Cd Length: 291  Bit Score: 196.79  E-value: 1.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSDLLQLNNQNLNLDIYVIGLQE---LNSGIIsLLSDAAFNDSWSSFLMDVLSPLSFVKVSH 90
Cdd:cd09090    1 INIFVGTFNVNGKSYKDDLSSWLFPEENDELPDIVVIGLQEvveLTAGQI-LNSDPSKSSFWEKKIKTTLNGRGGEKYVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  91 VR---MQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRI 167
Cdd:cd09090   80 LRseqLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAGLTNYEERNNDYKTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 168 LE-MQNCEGRDIPnilDHDLIIWFGDMNFRIeDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPT 246
Cdd:cd09090  160 ARgLRFSRGRTIK---DHDHVIWLGDFNYRI-SLTNEDVRRFILNGKLDKLLEYDQLNQQMNAGEVFPGFSEGPITFPPT 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386781117 247 YKFDRNSNDYDTSEKKRKPAWTDRILWRlkrqpqagpdtprlpapdfSLSLR--SYSSHMVYsISDHKPVTGTF 318
Cdd:cd09090  236 YKYDKGTDNYDTSEKQRIPAWTDRILYR-------------------GENLRqlSYNSAPLR-FSDHRPVYATF 289
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 46-319 4.49e-52

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This subfamily contains the INPP5c domains of two human synaptojanins, synaptojanin 1 (Synj1) and synaptojanin 2 (Synj2), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs). They belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, Synjs contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25 (a mitochondrial outer membrane protein). Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors.


Pssm-ID: 197323 [Multi-domain]  Cd Length: 328  Bit Score: 177.97  E-value: 4.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  46 DIYVIGLQE---LNSGIISLLSDAAFNDsWSSFLMDVLS-PLSFVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTG 121
Cdd:cd09089   52 DIFAIGFEEmvdLNASNIVSASTTNQKE-WGEELQKTISrDHKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 122 LFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRIlemqnCEGRDIP---NILDHDLIIWFGDMNFRIe 198
Cdd:cd09089  131 LGGAAGNKGAVAIRFLLHSTSLCFVCSHFAAGQSQVKERNEDFAEI-----ARKLSFPmgrTLDSHDYVFWCGDFNYRI- 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 199 DFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQ 278
Cdd:cd09089  205 DLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFLEGEINFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKW 284

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 386781117 279 PQAGPDTPRLPAPDFSLSlrsySSHMVY------SISDHKPVTGTFD 319
Cdd:cd09089  285 PSDKTEESLVETNDPTWN----PGTLLYygraelKTSDHRPVVAIID 327
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 46-320 7.53e-42

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This subfamily contains the INPP5c domains of human synaptojanin 1 (Synj1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro.


Pssm-ID: 197332  Cd Length: 336  Bit Score: 151.35  E-value: 7.53e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  46 DIYVIGLQE---LNSGiiSLLSDAAFNDS-WSSFLMDVLS-PLSFVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPT 120
Cdd:cd09098   51 DIFAIGFEEmveLNAG--NIVSASTTNQKlWAAELQKTISrDQKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKT 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 121 GLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRIL-EMQNCEGRdipNILDHDLIIWFGDMNFRIeD 199
Cdd:cd09098  129 GMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIArKLSFPMGR---MLFSHDYVFWCGDFNYRI-D 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 200 FGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQP 279
Cdd:cd09098  205 IPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKLDFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWP 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386781117 280 ------------QAGPDTPRLPAPDFSLSLRSYSSHMVYSiSDHKPVTGTFDL 320
Cdd:cd09098  285 fdrsaedldllnASFPDNSKEQYTWSPGTLLHYGRAELKT-SDHRPVVALIDI 336
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 12-320 1.02e-39

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol polyphosphate-5-phosphatase E and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase E (also called type IV or 72 kDa 5-phosphatase), rat pharbin, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5E hydrolyzes the 5-phosphate from PI(3,5)P2, PI(4,5)P2 and PI(3,4,5)P3, forming PI3P, PI4P, and PI(3,4)P2, respectively. It is a very potent PI(3,4,5)P3 5-phosphatase. Its intracellular localization is chiefly cytosolic, with pronounced perinuclear/Golgi localization. INPP5E also has an N-terminal proline rich domain (PRD) and a C-terminal CAAX motif. This protein is expressed in a variety of tissues, including the breast, brain, testis, and haemopoietic cells. It is differentially expressed in several cancers, for example, it is up-regulated in cervical cancer and down-regulated in stomach cancer. It is a candidate target for therapeutics of obesity and related disorders, as it is expressed in the hypothalamus, and following insulin stimulation, it undergoes tyrosine phosphorylation, associates with insulin receptor substrate-1, -2, and PI3-kinase, and become active as a 5-phosphatase. INPP5E may play a role, along with other 5-phosphatases SHIP2 and SKIP, in regulating glucose homoeostasis and energy metabolism. Mice deficient in INPPE5 develop a multi-organ disorder associated with structural defects of the primary cilium.


Pssm-ID: 197329  Cd Length: 298  Bit Score: 144.49  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  12 RRLSIHVVTWNVAS-AAPPLDLSDLLQLNNQNLNLDIYVIGLQELNSGiisllsdaafNDSWSSFLMDVLSPlsfvkvSH 90
Cdd:cd09095    3 RNVGIFVATWNMQGqKELPENLDDFLLPTSADFAQDIYVIGVQEGCSD----------RREWEIRLQETLGP------SH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  91 VRMQ----GIL-LLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFD 165
Cdd:cd09095   67 VLLHsashGVLhLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGDGKVKERVLDYN 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 166 RILEMQNCEGRDIPNILDH---------DLIIWFGDMNFRIeDFGLHFVRESIKNRC---YSGLWEKDQLSIAKKHDPLL 233
Cdd:cd09095  147 KIIQALNLPRNVPTNPYKSesgdvttrfDEVFWFGDFNFRL-SGPRHLVDALINQGQevdVSALLQHDQLTREMSKGSIF 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 234 REFQEGRLLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKrqpQAGPDTPrlpapdfslslRSYSSHMVYSISDHKP 313
Cdd:cd09095  226 KGFQEAPIHFPPTYKFDIGSDVYDTSSKQRVPSYTDRILYRSR---QKGDVCC-----------LKYNSCPSIKTSDHRP 291


                 ....*..
gi 386781117 314 VTGTFDL 320
Cdd:cd09095  292 VFALFRV 298
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
12-323 3.72e-39

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 146.85  E-value: 3.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  12 RRLSIHVVTWNVASAAPPLDLSDLLQ-LNNQNLNLDIYVIGLQE---LNSGIISLLSDAAFNDSWSSFLMDVLS-PLSFV 86
Cdd:COG5411   28 KDVSIFVSTFNPPGKPPKASTKRWLFpEIEATELADLYVVGLQEvveLTPGSILSADPYDRLRIWESKVLDCLNgAQSDE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  87 KVSHVR---MQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEH 163
Cdd:COG5411  108 KYSLLRspqLGGILLRVFSLATNLPVVKPVSGTVKKTGFGGSSSNKGAVAIRFNYERTSFCFVNSHLAAGVNNIEERIFD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 164 FDRIleMQNCEGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCY-SGLWEKDQLSIAKKHDPLLREFQEGRLL 242
Cdd:COG5411  188 YRSI--ASNICFSRGLRIYDHDTIFWLGDLNYRVTSTNEEVRPEIASDDGRlDKLFEYDQLLWEMEVGNVFPGFKEPVIT 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 243 FPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRlkrqpqagpdtprlpapdfSLSLR--SYSSHMVYSISDHKPVTGTFDL 320
Cdd:COG5411  266 FPPTYKFDYGTDEYDTSDKGRIPSWTDRILYK-------------------SEQLTphSYSSIPHLMISDHRPVYATFRA 326


                 ...
gi 386781117 321 ELK 323
Cdd:COG5411  327 KIK 329
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 46-314 6.48e-39

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This subfamily contains the INPP5c domains of human synaptojanin 2 (Synj2) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25, a mitochondrial outer membrane protein. Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors.


Pssm-ID: 197333  Cd Length: 336  Bit Score: 143.24  E-value: 6.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  46 DIYVIGLQE---LNSGiiSLLSDAAFNDS-WSSFLMDVLS-PLSFVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPT 120
Cdd:cd09099   51 DIFAVGFEEmveLSAG--NIVNASTTNRKmWGEQLQKAISrSHRYILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKT 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 121 GLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILE-MQNCEGRdipNILDHDLIIWFGDMNFRIeD 199
Cdd:cd09099  129 GMGGKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQVKERNEDYKEITQkLSFPMGR---NVFSHDYVFWCGDFNYRI-D 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 200 FGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQP 279
Cdd:cd09099  205 LTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYDVGSEAYDTSDKCRTPAWTDRVLWWRKKWP 284

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 386781117 280 --QAGPDTPRLPAP-DFSLSLRS--------YSSHMVYSISDHKPV 314
Cdd:cd09099  285 feKTAGEINLLDSDlDFDTKIRHtwtpgalmYYGRAELQASDHRPV 330
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 331-431 1.63e-36

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


Pssm-ID: 465482  Cd Length: 102  Bit Score: 129.67  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  331 IVLMPEDLWTV-ENDMMVSYSSTLDFPSSPWDWIGLYKVGLRDINDYVSYAWVGDSQVSCSDNLNQVYIDISNIP-ATED 408
Cdd:pfam17751   1 VVFQNVGEWYPpDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWAKDDEVEGSNSVRQVLFKASYLPkEPEG 80

                          90       100
                  ....*....|....*....|...
gi 386781117  409 EFLLCYYSNSLrSVVGISRPFQI 431
Cdd:pfam17751  81 FYQFCYVSNLG-SVVGISTPFQF 102
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 14-319 1.93e-32

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and -2, and related proteins; This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D), and SHIP2 (also known as INPPL1). It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Both SHIP1 and -2 catalyze the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP1 also converts inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4] to inositol-1,3,4-polyphosphate [I(1,3,4)P3]. SHIP1 and SHIP2 have little overlap in their in vivo functions. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. SHIP2 is as an inhibitor of the insulin signaling pathway, and is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD), while SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif, and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate gene for conferring a predisposition for type 2 diabetes.


Pssm-ID: 197325  Cd Length: 307  Bit Score: 125.06  E-value: 1.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSD---------LLQLNNQNLNLDIYVIGLQElnsgiisllsDAAFNDSWSSFLMDVLSPLS 84
Cdd:cd09091    1 ISIFIGTWNMGSAPPPKNITSwftskgqgkTRDDVADYIPHDIYVIGTQE----------DPLGEKEWLDLLRHSLKELT 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  85 FVKVSHVRMQ---GILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRL 161
Cdd:cd09091   71 SLDYKPIAMQtlwNIRIVVLAKPEHENRISHVCTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 162 EHFDRILEMQNCEGR-----DIPNILDHdlIIWFGDMNFRIE--DFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLR 234
Cdd:cd09091  151 QNYLNILRFLSLGDKklsafNITHRFTH--LFWLGDLNYRLDlpIQEAENIIQKIEQQQFEPLLRHDQLNLEREEHKVFL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 235 EFQEGRLLFPPTYKFDRNSNDYDTSEKKRK-------PAWTDRILWRlkrqpqagpdtprlPAPDFSLSLRSYSSHMVYS 307
Cdd:cd09091  229 RFSEEEITFPPTYRYERGSRDTYAYTKQKAtgvkynlPSWCDRILWK--------------SYPETHIICQSYGCTDDIV 294

                        330
                 ....*....|..
gi 386781117 308 ISDHKPVTGTFD 319
Cdd:cd09091  295 TSDHSPVFGTFE 306
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 14-320 3.33e-32

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol 5-phosphatase-2 and related proteins; This subfamily contains the INPP5c domain of SHIP2 (SH2 domain containing inositol 5-phosphatase-2, also called INPPL1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP2 catalyzes the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. SHIP2 is an inhibitor of the insulin signaling pathway. It is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. Its interacting partners include filamin/actin, p130Cas, Shc, Vinexin, Interesectin 1, and c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1). A large variety of extracellular stimuli appear to lead to the tyrosine phosphorylation of SHIP2, including epidermal growth factor (EGF), platelet-derived growth factor (PDGF), insulin, macrophage colony-stimulating factor (M-CSF) and hepatocyte growth factor (HGF). SHIP2 is localized to the cytosol in quiescent cells; following growth factor stimulation and /or cell adhesion, it relocalizes to membrane ruffles. In addition to this INPP5c domain, SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate for conferring a predisposition for type 2 diabetes; it has been suggested that suppression of SHIP2 may be of benefit in the treatment of obesity and thereby prevent type 2 diabetes. SHIP2 and SHIP1 have little overlap in their in vivo functions.


Pssm-ID: 197335  Cd Length: 304  Bit Score: 124.31  E-value: 3.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSD---------LLQLNNQNLNLDIYVIGLQELNSGiisllsdaafNDSWSSFLMDVLSPLS 84
Cdd:cd09101    1 ISIFIGTWNMGSVPPPKSLASwltsrglgkTLDETTVTIPHDIYVFGTQENSVG----------DREWVDFLRASLKELT 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  85 FVKVSHVRMQ---GILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRL 161
Cdd:cd09101   71 DIDYQPIALQclwNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTHRRN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 162 EHFDRILEMQNCEGRDIpNILDHDL----IIWFGDMNFRIeDFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQ 237
Cdd:cd09101  151 QNYLDILRSLSLGDKQL-NAFDISLrfthLFWFGDLNYRL-DMDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLRFR 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 238 EGRLLFPPTYKFDRNSNDYDTSEKKRK-------PAWTDRILWRlkrqpqagpdtprlPAPDFSLSLRSYSSHMVYSISD 310
Cdd:cd09101  229 EEEISFPPTYRYERGSRDTYMWQKQKTtgmrtnvPSWCDRILWK--------------SYPETHIVCNSYGCTDDIVTSD 294

                        330
                 ....*....|
gi 386781117 311 HKPVTGTFDL 320
Cdd:cd09101  295 HSPVFGTFEV 304
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 14-320 1.04e-30

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and related proteins; This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP1's enzymic activity is restricted to phosphatidylinositol 3,4,5-trisphosphate [PI (3,4,5)P3] and inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4]. It converts these two phosphoinositides to phosphatidylinositol 3,4-bisphosphate [PI (3,4)P2] and inositol-1,3,4-polyphosphate [I(1,3,4)P3], respectively. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD). SHIP1's phosphorylated NPXY motifs interact with proteins with phosphotyrosine binding (PTB) domains, and facilitate the translocation of SHIP1 to the plasma membrane to hydrolyze PI(3,4,5)P3. SHIP1 generally acts to oppose the activity of phosphatidylinositol 3-kinase (PI3K). It acts as a negative signaling molecule, reducing the levels of PI(3,4,5)P3, thereby removing the latter as a membrane-targeting signal for PH domain-containing effector molecules. SHIP1 may also, in certain contexts, amplify PI3K signals. SHIP1 and SHIP2 have little overlap in their in vivo functions.


Pssm-ID: 197334  Cd Length: 307  Bit Score: 120.48  E-value: 1.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  14 LSIHVVTWNVASAAPPLDLSD---------LLQLNNQNLNLDIYVIGLQElnsgiiSLLSDAAFNDSWSSFLMDVLSpLS 84
Cdd:cd09100    1 ITIFIGTWNMGNAPPPKKITSwfqckgqgkTRDDTADYIPHDIYVIGTQE------DPLGEKEWLDTLKHSLREITS-IS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  85 FVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHF 164
Cdd:cd09100   74 FKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSEKKLRRNQNY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 165 DRILEMQNCEGR-----DIPNILDHdlIIWFGDMNFRIE--DFGLHFVRESIKNRCYSGLWEKDQLSIAKKHDPLLREFQ 237
Cdd:cd09100  154 FNILRFLVLGDKklspfNITHRFTH--LFWLGDLNYRVElpNTEAENIIQKIKQQQYQELLPHDQLLIERKESKVFLQFE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 238 EGRLLFPPTYKFDRNSNDY-------DTSEKKRKPAWTDRILWRlkrqpqagpdtprlPAPDFSLSLRSYSSHMVYSISD 310
Cdd:cd09100  232 EEEITFAPTYRFERGTRERyaytkqkATGMKYNLPSWCDRVLWK--------------SYPLVHVVCQSYGCTDDITTSD 297

                        330
                 ....*....|
gi 386781117 311 HKPVTGTFDL 320
Cdd:cd09100  298 HSPVFATFEV 307
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 84-323 3.54e-24

Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 105.37  E-value: 3.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117  84 SFVKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPP-HISNNYQRLE 162
Cdd:PLN03191 363 KYVRIVSKQMVGIYVSVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSgHKDGAEQRRN 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 163 ----------HFDRILEMQncEGRDIPNildHDLIIWFGDMNFRIEDFGLHfVRESIKNRCYSGLWEKDQLSIAKKHDPL 232
Cdd:PLN03191 443 advyeiirrtRFSSVLDTD--QPQTIPS---HDQIFWFGDLNYRLNMLDTE-VRKLVAQKRWDELINSDQLIKELRSGHV 516

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 233 LREFQEGRLLFPPTYKFDRNSNDY-----DTSEKKRKPAWTDRILWRLKRQPQAgpdtprlpapdfslslrSYSSHMVyS 307
Cdd:PLN03191 517 FDGWKEGPIKFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQL-----------------CYKRSEI-R 578

                        250
                 ....*....|....*.
gi 386781117 308 ISDHKPVTGTFDLELK 323
Cdd:PLN03191 579 LSDHRPVSSMFLVEVE 594
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 126-272 6.76e-04

Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I (INPP5A) hydrolyzes the 5-phosphate from inositol 1,3,4,5-tetrakisphosphate [I(1,3,4,5)P4] and inositol 1,4,5-trisphosphate [I(1,4,5)P3]. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. As the substrates of INPP5A mobilize intracellular calcium ions, INPP5A is a calcium signal-terminating enzyme. In platelets, phosphorylated pleckstrin binds and activates INPP5A in a 1:1 complex, and accelerates the degradation of the calcium ion-mobilizing I(1,4,5)P3.


Pssm-ID: 197326  Cd Length: 383  Bit Score: 41.69  E-value: 6.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 126 WGNKGGVNICLKLYGYYVSIINCHL-------------PPHISNNYQR-LEH-FDRILEMQNCEgrdIPNILdhdliiwF 190
Cdd:cd09092  152 WSRKGFMRTRWKINNCVFDLVNIHLfhdasnlaacessPSVYSQNRHRaLGYvLERLTDERFEK---VPFFV-------F 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781117 191 GDMNFRIEDFGL----------HFVRESIKNRCYSGLWEKDQ------LSIAKK-----HDPLLREFQEGRLL------- 242
Cdd:cd09092  222 GDFNFRLDTKSVvetlcakatmQTVRKADSNIVVKLEFREKDndnkvvLQIEKKkfdyfNQDVFRDNNGKALLkfdkele 301

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 386781117 243 ------------FPPTYKFDRNSNDYDTSEKKRKPAWTDRIL 272
Cdd:cd09092  302 vfkdvlyeldisFPPSYPYSEDPEQGTQYMNTRCPAWCDRIL 343
 
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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