Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294 152 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 231
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569004294 232 HCFRVP-KNSVQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 275
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125

Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294 152 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 231
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569004294 232 HCFRVP-KNSVQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 275
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   10 LHHA-RNGNAEEVRKLLaamarmEVVADIDCKgrskSNLGWTPLHLACYFGHKQVVEdLLKAGAKVNMlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLL------ENGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 569004294   89 AFTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   161 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDSCLFSIRCFDDTVHC 233
Cdd:smart00233   3 KEGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLL 81

                           90       100
                   ....*....|....*....|....
gi 569004294   234 FRVPKnsvQQSREKWLEAIEEHSA 257
Cdd:smart00233  82 LQAES---EEEREKWVEALRKAIA 102

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   9 LLHHARNGNAEEVRKLLaamarmeVVADIDCKGRSKsnLGWTPLHLACYFGHKQVVEDLLKAGAK-VN--MLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-------KCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                         90       100
                 ....*....|....*....|...
gi 569004294  84 PLHRAAFTGRKELVLLLLEYDAD 106
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGAD 114

Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294 152 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 231
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569004294 232 HCFRVP-KNSVQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 275
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125

Ankyrin repeat [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   9 LLHHA-RNGNAEEVRKLLAAmarmevVADIDCKGrsksNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHR 87
Cdd:COG0666  123 PLHLAaYNGNLEIVKLLLEA------GADVNAQD----NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004294  88 AAFTGRKELVLLLLEYDADSTVVNGSGQT----AKEATHDKEIRNMLEDQKPLDLAQGAEMKHILVGNKVVHKALKRYE 162
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   10 LHHA-RNGNAEEVRKLLaamarmEVVADIDCKgrskSNLGWTPLHLACYFGHKQVVEdLLKAGAKVNMlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLL------ENGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 569004294   89 AFTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004294   52 LHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEY-DADstvVNGSGQTA 117
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHaDVN---LKDNGRTA 64

Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 is proposed to function in regulation of Akt phosphorylation. ORP9 has 2 forms, a long (ORP9L) and a short (ORP9S). ORP9L contains an N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains a FFAT motif and an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294 162 EGPLWKSSRFF-GWKLFWVVLEH--GVLSWYRKQpDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTVHcFRVpK 238
Cdd:cd13290    2 EGPLSKWTNVMkGWQYRWFVLDDnaGLLSYYTSK-EKMMRGSRRGCVRLKGAVVGIDDEDDSTFTITVDQKTFH-FQA-R 78

                         90
                 ....*....|....*..
gi 569004294 239 NSvqQSREKWLEAIEEH 255
Cdd:cd13290   79 DA--EERERWIRALEDT 93

ankyrin repeat protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   9 LLHHARNGNAEEVRKLLaamarMEVVADIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:PHA03100 162 LIDKGVDINAKNRVNYL-----LSYGVPIN----IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232

                         90
                 ....*....|....*...
gi 569004294  89 AFTGRKELVLLLLEYDAD 106
Cdd:PHA03100 233 ILNNNKEIFKLLLNNGPS 250

Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called Collagen type IV alpha-3-binding protein/hCERT; START domain-containing protein 11/StARD11; StAR-related lipid transfer protein 11) is a kinase that phosphorylates an N-terminal region of the alpha 3 chain of type IV collagen, which is commonly known as the goodpasture antigen. Its splice variant the ceramide transporter (CERT) mediates the cytosolic transport of ceramide. There have been additional splice variants identified, but all of them function as ceramide transport proteins. GPBP and CERT both contain an N-terminal PH domain, followed by a serine rich domain, and a C-terminal START domain. However, GPBP has an additional serine rich domain just upstream of its START domain. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294 173 GWKLFWVVLEHGVLSWYRKQPDAVHnsyrqGCK---HLTQAVCTVKPTDSCLFSIrCFDDTVHCFRVpknSVQQSREKWL 249
Cdd:cd13283   14 GWQDRYFVLKDGTLSYYKSESEKEY-----GCRgsiSLSKAVIKPHEFDECRFDV-SVNDSVWYLRA---ESPEERQRWI 84

                         90
                 ....*....|
gi 569004294 250 EAIEEHSAYS 259
Cdd:cd13283   85 DALESHKAAS 94

ankyrin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   8 QLLHHARNGNAEEVRKLLAAMArmevvaDIDCKGRSksnlGWTPLHlaCYFGHKQ---VVEDLLKAGAKVNMLNDMGDTP 84
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGA------DVNAPERC----GFTPLH--LYLYNATtldVIKLLIKAGADVNAKDKVGRTP 120

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 569004294  85 LHR--AAFTGRKELVLLLLEYDADSTVVNGSGQTA 117
Cdd:PHA03095 121 LHVylSGFNINPKVIRLLLRKGADVNALDLYGMTP 155

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 569004294   48 GWTPLHLACY-FGHKQVVEDLLKAGAKVNMLND 79
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294 161 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQ-GCKHLTQAVCTVKPTDSCLFSIRCFDDTVHCFRVP 237
Cdd:cd00821    1 KEGYLLKrgGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSiPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQAD 80

                         90
                 ....*....|....*
gi 569004294 238 KnsvQQSREKWLEAI 252
Cdd:cd00821   81 S---EEERQEWLKAL 92

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.

                           10        20
                   ....*....|....*....|....*....
gi 569004294    48 GWTPLHLACYFGHKQVVEDLLKAGAKVNM 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30

Ankyrin repeats (many copies);

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569004294   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.

                          10        20
                  ....*....|....*....|....*....
gi 569004294   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNM 76
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004294  67 LLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAKEATHDKEIRNMLE 131
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.

                           10        20
                   ....*....|....*....|....*..
gi 569004294    80 MGDTPLHRAAFTGRKELVLLLLEYDAD 106
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27

Voltage-dependent potassium channel; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569004294  59 GHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTA 117
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   9 LLHHARNGNAEEVRKLLaamarmeVVADIDCKGRSKsnLGWTPLHLACYFGHKQVVEDLLKAGAK-VN--MLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-------KCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                         90       100
                 ....*....|....*....|...
gi 569004294  84 PLHRAAFTGRKELVLLLLEYDAD 106
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGAD 114

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.

                          10        20
                  ....*....|....*....|....*.
gi 569004294   81 GDTPLHRAAFTGRKELVLLLLEYDAD 106
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27

ankyrin repeat protein; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569004294  63 VVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAKE 119
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216

ankyrin repeat protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294  48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTA---KEATHDK 124
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPliiAMAKGDI 181

                 ....*...
gi 569004294 125 EIRNMLED 132
Cdd:PHA02875 182 AICKMLLD 189

Voltage-dependent potassium channel; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004294   2 NTEAEQQLLHHARNGNAEEVRKLLAAmarmEVVADI-DCKGRsksnlgwTPLHLACYFGHKQVVEDLLKAGAKVNMLNDM 80
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKA----KLDPDIgDSKGR-------TPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                         90       100
                 ....*....|....*....|....*..
gi 569004294  81 GDTPLHRAAFTGRKELVLLLLEYDADS 107
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRILYHFASIS 617