Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565 117 ANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRgGARVDALDRaGRTPLHLAksklniLQEGHSQC 196
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYA------ARSGHLEI 76

                  ..
gi 1821619565 197 LE 198
Cdd:pfam12796  77 VK 78

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821619565 123 ETVQLLLDHGADPNQQDGLGNTPLH-LAACTNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLAKSKLNI 188
Cdd:cd22192   150 EIVRLLIEHGADIRAQDSLGNTVLHiLVLQPNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLAAKEGNI 225

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        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821619565 120 NDVETVQLLLDHGADPN------------QQDGL--GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAK 183
Cdd:TIGR00870 139 QNYEIVKLLLERGASVParacgdffvksqGVDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821619565 117 ANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLN 187
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN 231

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565 117 ANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRgGARVDALDRaGRTPLHLAksklniLQEGHSQC 196
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYA------ARSGHLEI 76

                  ..
gi 1821619565 197 LE 198
Cdd:pfam12796  77 VK 78

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821619565 117 ANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 182
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565 113 LRDSANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEG 192
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA------AYNG 131

                          90
                  ....*....|
gi 1821619565 193 HsqcLEAVRL 202
Cdd:COG0666   132 N---LEIVKL 138

ankyrin repeat protein; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821619565 120 NDVETVQLLLDHGADPNQQDGLGNTPLHLAACT--NHVPVITTLLRGGARVDALDRAGRTPLHLA----KSKLNILQ 190
Cdd:PHA03100   84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnKIDLKILK 160

ankyrin-like protein; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1821619565 128 LLDHGADPNQQDGLGNTPLHLAA--CTNHVPVITTLLRGGARVDALDRAGRTPLHLA 182
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYA 264

Ankyrin repeats (many copies);

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1821619565 117 ANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLL 162
Cdd:pfam13637   9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54

ankyrin repeat protein; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821619565 116 SANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTN-HVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNIL 189
Cdd:PHA02876  315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389

Ankyrin repeats (3 copies);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1821619565 116 SANANDVETVQLLLDHgADPNQQDGlGNTPLHLAACTNHVPVITTLLRGGARVDALD 172
Cdd:pfam12796  37 AAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91

ankyrin repeat protein; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1821619565 116 SANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDR 173
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256

ankyrin-like protein; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1821619565 125 VQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 182
Cdd:PHA03095  240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297

ankyrin repeat protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565  98 RRLGPTGKEVHALKRL------RDSANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL 171
Cdd:PHA02876  325 RTLIMLGADVNAADRLyitplhQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                          90
                  ....*....|.
gi 1821619565 172 DRAGRTPLHLA 182
Cdd:PHA02876  405 SQKIGTALHFA 415

ankyin-like protein; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565 121 DVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 180
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110

Ankyrin repeats (3 copies);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1821619565 146 LHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHSQCLEA 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA------AKNGHLEIVKL 48

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821619565 125 VQLLLDHGADPN------------QQDGL--GNTPLHLAACTNHVPVITTLLRG---GARVDALDRAGRTPLH 180
Cdd:cd22196   110 VELLVQNGADVHarasgeffkkkkGGPGFyfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLH 182

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 1821619565 142 GNTPLHLAAC-TNHVPVITTLLRGGARVDALDR 173
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34

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 1821619565 120 NDVETVQLLLDHGADPNQ-----------QDGL---GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH----- 180
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlq 179

                          90       100
                  ....*....|....*....|....*....
gi 1821619565 181 ----LAKSKLNIL----QEGHSQCLEAVR 201
Cdd:cd22192   180 pnktFACQMYDLIlsydKEDDLQPLDLVP 208

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 1821619565 106 EVHAL--KRLRDS-----ANANDVETVQ-LLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD----- 172
Cdd:cd22192     7 ELHLLqqKRISESplllaAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPmtsdl 86

                          90
                  ....*....|....*.
gi 1821619565 173 RAGRTPLHLAKSKLNI 188
Cdd:cd22192    87 YQGETALHIAVVNQNL 102

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        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565 116 SANANDVETVQLLLDHGADP---NQQDGLGNTPLH-LAACTNHVPVITT--------LLRGGARVDAL-------DRAGR 176
Cdd:cd21882   126 AACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHaLVLQADNTPENSAfvcqmynlLLSYGAHLDPTqqleeipNHQGL 205

                          90
                  ....*....|..
gi 1821619565 177 TPLHLAKSKLNI 188
Cdd:cd21882   206 TPLKLAAVEGKI 217

ankyrin repeat protein; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1821619565 121 DVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAG 175
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201

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 1821619565  142 GNTPLHLAACTNHVPVITTLLRGGARVDA 170
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30

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        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821619565 120 NDVETVQLLLDHGADPN------------QQDGL--GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAK 183
Cdd:TIGR00870 139 QNYEIVKLLLERGASVParacgdffvksqGVDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216

ankyin-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565  97 HRRLGPTGKEVHALKRLRDSANANDVETVQLLLDHGADPNQQDGLGNTPLHLAACTNH--VPVITTLLRGGARV-DALDR 173
Cdd:PHA02946   60 HRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSVDE 139

                  ....*.
gi 1821619565 174 AGRTPL 179
Cdd:PHA02946  140 EGCGPL 145

ankyrin repeat protein; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821619565 121 DVETVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARV-DALDRAGRTPLHLA 182
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLA 109

Voltage-dependent potassium channel; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821619565 128 LLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE----------G 192
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfasisdphaaG 623

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821619565 193 HSQCLEAVRLEVKqiihMLREYLeRLGRHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--QMQSMEKR 266
Cdd:PLN03192  624 DLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddDFSPTELR 696

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        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821619565 123 ETVQLLLDHGADPN------------QQDGL--GNTPLHLAACTNHVPVITTLL-RGGARVDALDRAGRTPLH 180
Cdd:cd22194   155 DIVKLLIAKGADVNahakgvffnpkyKHEGFyfGETPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLH 227

Ankyrin repeats (many copies);

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1821619565 117 ANANDVETVQLLLDHGADPNQQDGLGNTPLHLA 149
Cdd:pfam13857  24 AKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56