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Conserved domains on  [gi|1862432915|ref|NP_001371596|]
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membrane-associated phosphatidylinositol transfer protein 2 isoform 8 [Homo sapiens]

Protein Classification

PITPNM family protein( domain architecture ID 10172309)

PITPNM (membrane-associated phosphatidylinositol transfer protein) family protein belonging to SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) superfamily; similar to Homo sapiens membrane-associated phosphatidylinositol transfer protein 2 isoform 8 that catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes

Gene Ontology:  GO:0048015|GO:0008526|GO:0008525
PubMed:  18922149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC_PITPNM1-2_like cd08889
Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); ...
 1-258 0e+00

Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain).


:

Pssm-ID: 176898  Cd Length: 260  Bit Score: 555.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:cd08889     1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  81 ALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPK 160
Cdd:cd08889    81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 161 LFQSTKTQRGPLSENWIEEYK--KQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLS 238
Cdd:cd08889   161 LYVSEKTGRGPLSDDWIEEYKdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                         250       260
                  ....*....|....*....|
gi 1862432915 239 MENIRELEKEAQLMLSRKMA 258
Cdd:cd08889   241 MEDIRKLEEETQLALAQKMA 260
 
Name Accession Description Interval E-value
SRPBCC_PITPNM1-2_like cd08889
Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); ...
 1-258 0e+00

Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain).


Pssm-ID: 176898  Cd Length: 260  Bit Score: 555.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:cd08889     1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  81 ALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPK 160
Cdd:cd08889    81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 161 LFQSTKTQRGPLSENWIEEYK--KQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLS 238
Cdd:cd08889   161 LYVSEKTGRGPLSDDWIEEYKdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                         250       260
                  ....*....|....*....|
gi 1862432915 239 MENIRELEKEAQLMLSRKMA 258
Cdd:cd08889   241 MEDIRKLEEETQLALAQKMA 260
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-250 1.66e-143

Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family (found in pfam00650), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. PITP alpha has a 16-fold greater affinity for PI than PC. Together with PITP beta, it is expressed ubiquitously in all tissues.


Pssm-ID: 460452  Cd Length: 245  Bit Score: 409.27  E-value: 1.66e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:pfam02121   1 MLIKEYRIPLPLTVEEYQIAQLYMVAKKSKEET-GGGEGVEVLENEPYEDGEGGKGQYTHKIYHLASKLPSWIRALLPKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  81 ALRVVEESWNAYPYTRTRFTCPFV-EKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDP 159
Cdd:pfam02121  80 ALYVEEKAWNAYPYTKTVYTCPFMkEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIANDKVSSKDYKEEEDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 160 KLFQSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSM 239
Cdd:pfam02121 160 TLFKSEKTGRGPLKEGWKKSTS----PIMCAYKLVTVEFKWWGLQTRVESFIH-KALRDIFLKFHRQAFCWIDEWYGMTM 234

                         250
                  ....*....|.
gi 1862432915 240 ENIRELEKEAQ 250
Cdd:pfam02121 235 EDIRELEEETQ 245
 
Name Accession Description Interval E-value
SRPBCC_PITPNM1-2_like cd08889
Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); ...
 1-258 0e+00

Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain).


Pssm-ID: 176898  Cd Length: 260  Bit Score: 555.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:cd08889     1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  81 ALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPK 160
Cdd:cd08889    81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 161 LFQSTKTQRGPLSENWIEEYK--KQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLS 238
Cdd:cd08889   161 LYVSEKTGRGPLSDDWIEEYKdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                         250       260
                  ....*....|....*....|
gi 1862432915 239 MENIRELEKEAQLMLSRKMA 258
Cdd:cd08889   241 MEDIRKLEEETQLALAQKMA 260
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-250 1.66e-143

Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family (found in pfam00650), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. PITP alpha has a 16-fold greater affinity for PI than PC. Together with PITP beta, it is expressed ubiquitously in all tissues.


Pssm-ID: 460452  Cd Length: 245  Bit Score: 409.27  E-value: 1.66e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:pfam02121   1 MLIKEYRIPLPLTVEEYQIAQLYMVAKKSKEET-GGGEGVEVLENEPYEDGEGGKGQYTHKIYHLASKLPSWIRALLPKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  81 ALRVVEESWNAYPYTRTRFTCPFV-EKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDP 159
Cdd:pfam02121  80 ALYVEEKAWNAYPYTKTVYTCPFMkEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIANDKVSSKDYKEEEDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 160 KLFQSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSM 239
Cdd:pfam02121 160 TLFKSEKTGRGPLKEGWKKSTS----PIMCAYKLVTVEFKWWGLQTRVESFIH-KALRDIFLKFHRQAFCWIDEWYGMTM 234

                         250
                  ....*....|.
gi 1862432915 240 ENIRELEKEAQ 250
Cdd:pfam02121 235 EDIRELEEETQ 245
SRPBCC_PITP cd07815
Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins; ...
 3-257 6.98e-135

Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of the phosphatidylinositol transfer protein (PITP) family of lipid transfer proteins. This family of proteins includes Class 1 PITPs (PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator and related proteins), Class IIA PITPs (PITPNM1/PITPalphaI/Nir2, PITPNM2/PITPalphaII/Nir3, Drosophila RdgB, and related proteins), and Class IIB PITPs (PITPNC1/RdgBbeta and related proteins). The PITP family belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Class III PITPs, exemplified by the Sec14p family, are found in yeast and plants but are unrelated in sequence and structure to Class I and II PITPs and belong to a different superfamily.


Pssm-ID: 176857  Cd Length: 251  Bit Score: 387.84  E-value: 6.98e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   3 IKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKAAL 82
Cdd:cd07815     2 IKEFRIVLPLTVEEYQIGQLYMVAKASKEET-GSGEGVEVLKNEPYEDENGGKGQYTHKIYHLGSKLPSWLRALAPKSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  83 RVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPKLF 162
Cdd:cd07815    81 TIEEKSWNAYPYCKTVYSCPFFEKFSISIESMHKPDLGTQENAHNLSAEQLAQRKVVVIDIANDSVASKDYKPEEDPKLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 163 QSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSMENI 242
Cdd:cd07815   161 KSKKTGRGPLRKGWRKSTK----PIMCAYKLVTVDFPYWGLQNKVENFIQ-KVERDVFLNYHRQAFCWIDEWFDLTMEDI 235

                         250
                  ....*....|....*
gi 1862432915 243 RELEKEAQLMLSRKM 257
Cdd:cd07815   236 REFEEETKELLDAKR 250
SRPBCC_PITPNA-B_like cd08888
Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); ...
 2-256 4.99e-103

Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); This subgroup includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class 1 phosphatidylinositol transfer proteins (PITPs), PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator, and related proteins. These are single domain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. In addition, PITPNB transfers sphingomyelin in vitro, with a low affinity. PITPNA is found chiefly in the nucleus and cytoplasm; it is enriched in the brain and predominantly localized in the axons. A reduced expression of PITPNA contributes to the neurodegenerative phenotype of the mouse vibrator mutation. The role of PITPNA in vivo may be to provide PtdIns for localized PI3K-dependent signaling, thereby controlling the polarized extension of axonal processes. PITPNA homozygous null mice die soon after birth from complicated organ failure, including intestinal and hepatic steatosis, hypoglycemia, and spinocerebellar disease. PITPNB is associated with the Golgi and ER, and is highly expressed in the liver. Deletion of the PITPNB gene results in embryonic lethality. The PtdIns and PtdCho exchange activity of PITPNB is required for COPI-mediated retrograde transport from the Golgi to the ER. Drosophila vibrator localizes to the ER, and has an essential role in cytokinesis during mitosis and meiosis.


Pssm-ID: 176897  Cd Length: 258  Bit Score: 307.06  E-value: 4.99e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   2 IIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKAA 81
Cdd:cd08888     1 LIKEFRVILPLSVEEYQVGQLYSVAEASKNET-GGGEGIEVLVNEPYEKDDGEKGQYTHKIYHLQSKVPGFVRMLAPEGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  82 LRVVEESWNAYPYTRTRFTCPFV-EKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPV--PHNeYKTEED 158
Cdd:cd08888    80 LEIHEKAWNAYPYCRTIITNEYMkEDFLIIIETWHKPDLGTQENVHNLDPEEWKEVEVVYIDIADRSQvdPKD-YKADED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 159 PKLFQSTKTQRGPLSENWIEE-YKKQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTgLRRVMVRAHRQAWCWQDEWYGL 237
Cdd:cd08888   159 PAKFQSEKTGRGPLGPNWKKElVNQKDCPIMCAYKLVTVEFKWWGLQNKVENFIQKQ-ERRLFTNFHRQVFCWLDKWHGL 237

                         250
                  ....*....|....*....
gi 1862432915 238 SMENIRELEKEAQLMLSRK 256
Cdd:cd08888   238 TMDDIRRMEDETKKELDEM 256
SRPBCC_PITPNC1_like cd08890
Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs); This ...
 2-258 1.03e-90

Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs); This subgroup includes the N-terminal SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain of mammalian Class IIB phosphatidylinositol transfer protein (PITP), PITPNC1/RdgBbeta, and related proteins. These are metazoan proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Mammalian PITPNC1 contains an amino-terminal SRPBCC PITP-like domain and a short carboxyl-terminal domain. It is a cytoplasmic protein, and is ubiquitously expressed. It can transfer phosphatidylinositol (PtdIns) in vitro with a similar ability to other PITPs.


Pssm-ID: 176899  Cd Length: 250  Bit Score: 275.14  E-value: 1.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915   2 IIKEYRIPLPMTVEEYRIAQLYMIQKKSrNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKAa 81
Cdd:cd08890     1 LLKEYRICMPLTVEEYRIGQLYMISRHS-HEQSERGEGVEVVQNEPCEDPEHGNGQFTEKRVYLNSRLPSWARAVVPKI- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915  82 LRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPKL 161
Cdd:cd08890    79 FYVTEKAWNYYPYTITEYTCSFLPKFSIHIETKYEDNKGKSENCIFLSEAELSEREVCHLDIAYDEIPEKYYKEEEDPKY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862432915 162 FQSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSMEN 241
Cdd:cd08890   159 FKSEKTGRGPLKEGWRETHK----PIMCSYKLVTVKFEVWGLQTRVEQFVH-KVVRDILLLGHRQAFAWVDEWYDMTMDD 233

                         250
                  ....*....|....*..
gi 1862432915 242 IRELEKEAQLMLSRKMA 258
Cdd:cd08890   234 VREYERTIQEKTNEKIG 250
 
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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