The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   2 IDVYIPSVGHQVYKSDKTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKKTCKVPDFPPKRVPNWMPKVQEQRRQGLEA 81
Cdd:cd06880   1 IEVSIPSYRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTPDFPPKRVRNWNPKVLEQRRQGLEA 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 62860124  82 YIQGVLWYNTdVPKELLDFLKVRHFHKDKKN 112
Cdd:cd06880  81 YLQGLLKINE-LPKQLLDFLGVRHFPSLPKS 110

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   2 IDVYIPSVGHQVYKSDKTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKKTCKVPDFPPKRVPNWMPKVQEQRRQGLEA 81
Cdd:cd06880   1 IEVSIPSYRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTPDFPPKRVRNWNPKVLEQRRQGLEA 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 62860124  82 YIQGVLWYNTdVPKELLDFLKVRHFHKDKKN 112
Cdd:cd06880  81 YLQGLLKINE-LPKQLLDFLGVRHFPSLPKS 110

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124     15 KSDKTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKK---TCKVPDFPPK----RVPNWMPKVQEQRRQGLEAYIQGVL 87
Cdd:smart00312   9 DGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKhfpRSILPPLPGKklfgRLNNFSEEFIEKRRRGLEKYLQSLL 88

                           90
                   ....*....|....*...
gi 62860124     88 ----WYNTDvpKELLDFL 101
Cdd:smart00312  89 nhpeLINHS--EVVLEFL 104

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   2 IDVYIPSVGHQVYKSDKTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKKTCKVPDFPPKRVPNWMPKVQEQRRQGLEA 81
Cdd:cd06880   1 IEVSIPSYRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTPDFPPKRVRNWNPKVLEQRRQGLEA 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 62860124  82 YIQGVLWYNTdVPKELLDFLKVRHFHKDKKN 112
Cdd:cd06880  81 YLQGLLKINE-LPKQLLDFLGVRHFPSLPKS 110

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   3 DVYIPSVgHQVYKSDKTHTVFRVDV-LFNGRRHTLDRRYSEFHALHKLLKKT---CKVPDFPPKRVPNWM-PKVQEQRRQ 77
Cdd:cd06093   1 SVSIPDY-EKVKDGGKKYVVYIIEVtTQGGEEWTVYRRYSDFEELHEKLKKKfpgVILPPLPPKKLFGNLdPEFIEERRK 79

                        90       100
                ....*....|....*....|....*..
gi 62860124  78 GLEAYIQGVLwYNTDV--PKELLDFLK 102
Cdd:cd06093  80 QLEQYLQSLL-NHPELrnSEELKEFLE 105

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124     15 KSDKTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKK---TCKVPDFPPK----RVPNWMPKVQEQRRQGLEAYIQGVL 87
Cdd:smart00312   9 DGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKhfpRSILPPLPGKklfgRLNNFSEEFIEKRRRGLEKYLQSLL 88

                           90
                   ....*....|....*...
gi 62860124     88 ----WYNTDvpKELLDFL 101
Cdd:smart00312  89 nhpeLINHS--EVVLEFL 104

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   2 IDVYIPSVGHQVYKSDkTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKKTCKVP---DFPPKR-VPNWMPKVQEQRRQ 77
Cdd:cd07277   1 INVWIPSVFLRGKGSD-AHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVrsfDFPPKKaIGNKDAKFVEERRK 79

                        90
                ....*....|
gi 62860124  78 GLEAYIQGVL 87
Cdd:cd07277  80 RLQVYLRRVV 89

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124  11 HQVYKSDKTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKKTCkvPD----FPPKRV--PNWMPKVQEQRRQGLEAYIQ 84
Cdd:cd06870  11 DEDREKKKRFTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQF--PAsnlkIPGKRLfgNNFDPDFIKQRRAGLDEFIQ 88

                        90       100
                ....*....|....*....|..
gi 62860124  85 GVLWYNtdvpkELLDFLKVRHF 106
Cdd:cd06870  89 RLVSDP-----KLLNHPDVRAF 105

The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   2 IDVYIPSVGHqVYKSDKTHTVFRVdvlFNGRRHTLDRRYSEFHALHKLLKKtcKVPDFP-PKRVPNWMPKVQEQ----RR 76
Cdd:cd06886   4 VPISIPDYKH-VEQNGEKFVVYNI---YMAGRQLCSRRYREFANLHQNLKK--EFPDFQfPKLPGKWPFSLSEQqldaRR 77

                        90
                ....*....|
gi 62860124  77 QGLEAYIQGV 86
Cdd:cd06886  78 RGLEQYLEKV 87

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62860124  18 KTHTVFRVDVLFNGRRHTLDRRYSEFHALHKLLKKtcKVP-----DFPPKRV-PNWMPKVQEQRRQGLEAYIQ 84
Cdd:cd06874  16 DEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKL--KYPevaalEFPPKKLfGNKSERVAKERRRQLETYLR 86

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62860124  20 HTVFRVDV-----LFNGRRHTLDRRYSEFHALHKLLKKTCK---VPDFPPKRVPNwMPKVQ----EQRRQGLEAYIQGV 86
Cdd:cd06859  18 YVVYRVTTktnlpDFKKSEFSVLRRYSDFLWLYERLVEKYPgriVPPPPEKQAVG-RFKVKfefiEKRRAALERFLRRI 95

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   6 IPSVGHQVYKSDKTHTVFRVDVLFNGRRHTLD-RRYSEFHALHKLLKKTckVPDF----PPKRV--PNWMPKVQEQRRQG 78
Cdd:cd07276   6 PPILGYEVMEERARFTVYKIRVENKVGDSWFVfRRYTDFVRLNDKLKQM--FPGFrlslPPKRWfkDNFDPDFLEERQLG 83

                ....*....
gi 62860124  79 LEAYIQGVL 87
Cdd:cd07276  84 LQAFVNNIM 92

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124  20 HTVFRVDV-LFNGRRHTLDRRYSEFHALHKLLK-----------KTCKVPDFPPKRVPNWMPKVQEQRRQGLEAYIQGVL 87
Cdd:cd06882  20 YYVFVIEVkTKGGSKYLIYRRYRQFFALQSKLEerfgpeagssaYDCTLPTLPGKIYVGRKAEIAERRIPLLNRYMKELL 99

The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It shows a similar domain architecture as SNX1-2, among others, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. SNX4 is implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and the long form of the leptin receptor.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62860124  34 HTLDRRYSEFHALHKLLKKT---CKVPDFPPKRVP---------NWMPKVQEQRRQGLEAYIQGV 86
Cdd:cd06864  46 SSLWRRYSEFELLRNYLVVTypyVIVPPLPEKRAMfmwqklssdTFDPDFVERRRAGLENFLLRV 110

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 62860124  38 RRYSEFHALHKLLKKTCKVPDFPPKRV-PNWMPKVQEQRRQGLEAYIQGVL 87
Cdd:cd06871  42 RRYNDFDLLNASLQISGISLPLPPKKLiGNMDREFIAERQQGLQNYLNVIL 92

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62860124  38 RRYSEFHALHKLLK------KTCKVPDFPPKRVPNWMPKVQEQRRQGLEAYIQGVL 87
Cdd:cd06878  54 RKLSEFHDLHRKLKecsswlKKVELPSLSKKWFKSIDKKFLDKSKNQLQKYLQFIL 109

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62860124   4 VYIPSVGHQVYKS-DKTHTVF-----RVDVLFNG---RRHTLDRRYSEFHALH-KLLKKTCKVPD--FPPKRVPNWMPKV 71
Cdd:cd06877   5 VSIPYVEMRRDPSnGERIYVFcieveRNDRRAKGhepQHWSVLRRYNEFYVLEsKLTEFHGEFPDapLPSRRIFGPKSYE 84

                        90
                ....*....|....*..
gi 62860124  72 Q-EQRRQGLEAYIQGVL 87
Cdd:cd06877  85 FlESKREIFEEFLQKLL 101

The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62860124  38 RRYSEFHALHKLLKKTckvpdFPPKRVPNWMPK---------VQEQRRQGLEAYIQGVL 87
Cdd:cd06879  67 RRFNDFLKLHTDLKKL-----FPKKKLPAAPPKgllrmknraLLEERRHSLEEWMGKLL 120