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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207177244   1 MCCLAYLGKSEEMEAWKAAGVSFNVADAHGRTPLHVAVCTDQPEMVKFCIHNGSDPEQRDGFNNRPIDDAERLGLQHMVE 80
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                          90
                  ....*....|....*
gi 1207177244  81 LLTYQAHQPTSSGHR 95
Cdd:PTZ00322  166 LLSRHSQCHFELGAN 180

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 1207177244  29 HGRTPLHVAVC-TDQPEMVKFCIHNGSDPEQRD 60
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1207177244  29 HGRTPLHVAVCTDQPEMVKFCIHNGSDPEQRDGFNN 64
Cdd:TIGR00870 174 HGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207177244   5 AYLGKSEEMEAWKAAGVSFNVADAHGRTPLHVAVCTDQPEMVKFCIHNGSDPEQRDGFNNRPIDDAERLGLQHMVELL 82
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207177244   4 LAYLGKSEEMEAWKAAGVSFNVADAHGRTPLHVAVCTDQPEMVKFCIHNGSDPEQRDGFNNRPIDDAERLGLQHMVELL 82
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207177244  17 KAAGVSFNVADAH-----GRTPLHVAVCTDQPEMVKFCIHNGSDP-EQRDGFNN 64
Cdd:cd22194   170 HAKGVFFNPKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDiTSQDSRGN 223

Ankyrin repeats (3 copies);

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1207177244  29 HGRTPLHVAVCTDQPEMVKFCIHNGSDPEQRD 60
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91

ankyrin repeat protein; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207177244  20 GVSFNVADAHGRTPLHVAVCTDQPEMVKFCIHNGSDPEQRDGFNNRPI 67
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207177244   5 AYLGKSEEMEAWKAAGVSFNVADAHGRTPLHVAVCTDQPEMVKFCI-HNGSDpEQRDGFNnrPIDDAERLGLQHMVELL 82
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLeHADVN-LKDNGRT--ALHYAARSGHLEIVKLL 80

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 1207177244  29 HGRTPLHVAVCTDQPEMVKFCIHNGSDP 56
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207177244  17 KAAGVSFNVADAH-----GRTPLHVAVCTDQPEMVKFCIHNGSDP---EQRDGFNN 64
Cdd:cd22193   105 HAKGRFFQPKYQGegfyfGELPLSLAACTNQPDIVQYLLENEHQPadiEAQDSRGN 160

Ankyrin repeats (many copies);

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207177244   1 MCCLAYLGKSEEMEAWKAAGVSFNVADAHGRTPLHVAVCTDQPEMVKF 48
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1207177244  30 GRTPLHVAVCTDQPEMVKFCIHNGSDP---EQRDGFNN 64
Cdd:cd21882   119 GELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGN 156

ankyrin repeat protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207177244   4 LAYLGKSEEMEAWKAA---GVSFNVADAHGRTPLHVAVCTDQPEMVKFCIHNGSDPEQRDGFNNRPIDDAERLGLQHMVE 80
Cdd:PHA02874  128 LHYAIKKGDLESIKMLfeyGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                  ..
gi 1207177244  81 LL 82
Cdd:PHA02874  208 LL 209