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Conserved domains on  [gi|281500804|pdb|3JXI|D]
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Chain D, Vanilloid receptor-related osmotically activated channel protein

Protein Classification

transient-receptor-potential channel family protein( domain architecture ID 1750128)

transient-receptor-potential ion channel protein conducts cations such as calcium into cells; belongs to the Transient Receptor Family (TC. 1.A.4)

Gene Ontology:  GO:0070588|GO:0005262|GO:0070679
PubMed:  20025796|18535090|20861159
SCOP:  4000366
TCDB:  1.A.4

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1-251 0e+00

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).


The actual alignment was detected with superfamily member cd22195:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 733  Bit Score: 552.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        1 MKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMRE 80
Cdd:cd22195  45 LKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLTDEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLRE 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       81 FINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLT 160
Cdd:cd22195 125 FINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPDIVHYLT 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      161 ENGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGI 240
Cdd:cd22195 205 ENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGI 284

                       250
                ....*....|.
3JXI_D      241 FQHIIRREIAD 251
Cdd:cd22195 285 FQHIIRREIKD 295
 
Name Accession Description Interval E-value
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 1-251 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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 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.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 552.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        1 MKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMRE 80
Cdd:cd22195  45 LKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLTDEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLRE 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       81 FINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLT 160
Cdd:cd22195 125 FINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPDIVHYLT 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      161 ENGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGI 240
Cdd:cd22195 205 ENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGI 284

                       250
                ....*....|.
3JXI_D      241 FQHIIRREIAD 251
Cdd:cd22195 285 FQHIIRREIKD 295
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 4-249 1.62e-64

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]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 214.17  E-value: 1.62e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D          4 FNRPILFDIVSRGSPDGLEGLLSFLLthkkrltdeefREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMrEFIN 83
Cdd:TIGR00870  51 LGRSALFVAAIENENLELTELLLNLS-----------CRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPL-ELAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D         84 SPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENG 163
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        164 HkqaDLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQH 243
Cdd:TIGR00870 199 A---DILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275


                  ....*.
3JXI_D        244 IIRREI 249
Cdd:TIGR00870 276 KLAIKY 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-251 5.87e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 5.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       92 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGrffqpkdeggyfyfGELPLSLAACTNQPHIVHYLTENGhkqADLRR 171
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND--------------GNTPLHLAAANGNLEIVKLLLEAG---ADVNA 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      172 QDSRGNTVLHAlvAIADNTRENTKfvtkmydLLLIKCAklfpDTNLEallNNDGLSPLMMAAKTGKIGIFQHIIRREIAD 251
Cdd:COG0666 182 RDNDGETPLHL--AAENGHLEIVK-------LLLEAGA----DVNAK---DNDGKTALDLAAENGNLEIVKLLLEAGADL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-122 7.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 7.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
3JXI_D         71 IAEKTGN---MREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQ 122
Cdd:pfam12796  36 LAAKNGHleiVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-235 2.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        56 NLSAGRNDTIPILLDIAEKTGNMREFI------NSPFRDVYYRGQTALHIAIERRC--KHYVELLVEKGADVHAQARGRF 127
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKKSNSYSIVeylldnGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       128 F-------QPKDEGGYFyfgelPLSLAACTNQPHIVHYLTEnghKQADLRRQDSRGNTVLHalVAIADNTRENTKFVTKM 200
Cdd:PHA03100 178 LlsygvpiNIKDVYGFT-----PLHYAVYNNNPEFVKYLLD---LGANPNLVNKYGDTPLH--IAILNNNKEIFKLLLNN 247

                        170       180       190
                 ....*....|....*....|....*....|....*..
3JXI_D       201 YDLL--LIKCAKLFPDTNLEALLNNDGLSPLMMAAKT 235
Cdd:PHA03100 248 GPSIktIIETLLYFKDKDLNTITKIKMLKKSIMYMFL 284
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 92-121 2.93e-03

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.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 2.93e-03
                           10        20        30
                   ....*....|....*....|....*....|
3JXI_D          92 RGQTALHIAIERRCKHYVELLVEKGADVHA 121
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 1-251 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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 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.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 552.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        1 MKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMRE 80
Cdd:cd22195  45 LKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLTDEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLRE 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       81 FINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLT 160
Cdd:cd22195 125 FINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPDIVHYLT 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      161 ENGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGI 240
Cdd:cd22195 205 ENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGI 284

                       250
                ....*....|.
3JXI_D      241 FQHIIRREIAD 251
Cdd:cd22195 285 FQHIIRREIKD 295
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 18-251 9.75e-140

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.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 405.72  E-value: 9.75e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       18 PDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYRGQTAL 97
Cdd:cd22193   1 LEELLGFLQDLCRRRKDLTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       98 HIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENGHKQADLRRQDSRGN 177
Cdd:cd22193  81 HIAIERRQGDIVALLVENGADVHAHAKGRFFQPKYQGEGFYFGELPLSLAACTNQPDIVQYLLENEHQPADIEAQDSRGN 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3JXI_D      178 TVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQHIIRREIAD 251
Cdd:cd22193 161 TVLHALVTVADNTKENTKFVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQREIKE 234
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 2-251 7.95e-128

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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 376.45  E-value: 7.95e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        2 KVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREF 81
Cdd:cd22196   3 KLYDRRRIFDAVAKGDCKELDGLLEYLMRTKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTISLLLDIAEKTGNLKEF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       82 INSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTE 161
Cdd:cd22196  83 VNAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGEFFKKKKGGPGFYFGELPLSLAACTNQLDIVKFLLE 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      162 NGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIF 241
Cdd:cd22196 163 NPHSPADISARDSMGNTVLHALVEVADNTPENTKFVTKMYNEILILGAKIRPLLKLEEITNKKGLTPLKLAAKTGKIGIF 242

                       250
                ....*....|
3JXI_D      242 QHIIRREIAD 251
Cdd:cd22196 243 AYILGREIKE 252
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 3-251 4.85e-104

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 315.26  E-value: 4.85e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        3 VFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFI 82
Cdd:cd22197   4 RFDRDRLFSVVSRGNPEELAGLLEYLRRTSKYLTDSEYTEGSTGKTCLMKAVLNLQDGVNACIMPLLEIDKDSGNPKPLV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       83 NSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQpKDEGGYFYFGELPLSLAACTNQPHIVHYLTEN 162
Cdd:cd22197  84 NAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQ-KKQGTCFYFGELPLSLAACTKQWDVVNYLLEN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      163 GHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQ 242
Cdd:cd22197 163 PHQPASLQAQDSLGNTVLHALVMIADNSPENSALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEIFR 242


                ....*....
3JXI_D      243 HIIRREIAD 251
Cdd:cd22197 243 HILQREFSG 251
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 21-249 3.24e-90

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).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 278.30  E-value: 3.24e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       21 LEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYRGQTALHIA 100
Cdd:cd21882   1 LEELLGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQTALHIA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      101 IERRCKHYVELLVEKGADVHAQARGRFFQpKDEGGYFYFGELPLSLAACTNQPHIVHYLTENGHKQADLRRQDSRGNTVL 180
Cdd:cd21882  81 IENRNLNLVRLLVENGADVSARATGRFFR-KSPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3JXI_D      181 HALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQHIIRREI 249
Cdd:cd21882 160 HALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREF 228
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 5-251 9.99e-85

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.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 266.24  E-value: 9.99e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        5 NRPI--LFDIVSRGSPDGLEGLLS--------FLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEK 74
Cdd:cd22194  43 QRDKkkRLKKVSEAAVEELGELLKelkdlsrrRRKTDVPDFLMHKLTASDTGKTCLMKALLNINENTKEIVRILLAFAEE 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       75 TGNMREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPH 154
Cdd:cd22194 123 NGILDRFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFNPKYKHEGFYFGETPLALAACTNQPE 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      155 IVHYLTENGHKqaDLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAklfpDTNLEALLNNDGLSPLMMAAK 234
Cdd:cd22194 203 IVQLLMEKEST--DITSQDSRGNTVLHALVTVAEDSKTQNDFVKRMYDMILLKSE----NKNLETIRNNEGLTPLQLAAK 276

                       250
                ....*....|....*..
3JXI_D      235 TGKIGIFQHIIRREIAD 251
Cdd:cd22194 277 MGKAEILKYILSREIKE 293
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 4-249 1.62e-64

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]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 214.17  E-value: 1.62e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D          4 FNRPILFDIVSRGSPDGLEGLLSFLLthkkrltdeefREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMrEFIN 83
Cdd:TIGR00870  51 LGRSALFVAAIENENLELTELLLNLS-----------CRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPL-ELAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D         84 SPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENG 163
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        164 HkqaDLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQH 243
Cdd:TIGR00870 199 A---DILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275


                  ....*.
3JXI_D        244 IIRREI 249
Cdd:TIGR00870 276 KLAIKY 281
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 46-248 2.00e-43

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.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 155.17  E-value: 2.00e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       46 GKTCLPKALLNlsaGRNDTIPILLDIAektgnmREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADV-HAQAR 124
Cdd:cd22192  51 GETALHVAALY---DNLEAAVVLMEAA------PELVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvSPRAT 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      125 GRFFQPKdEGGYFYFGELPLSLAACTNQPHIVHYLTENGhkqADLRRQDSRGNTVLHALVAIAdntreNTKFVTKMYDLL 204
Cdd:cd22192 122 GTFFRPG-PKNLIYYGEHPLSFAACVGNEEIVRLLIEHG---ADIRAQDSLGNTVLHILVLQP-----NKTFACQMYDLI 192

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
3JXI_D      205 LIKCAKLFPDTnLEALLNNDGLSPLMMAAKTGKIGIFQHIIRRE 248
Cdd:cd22192 193 LSYDKEDDLQP-LDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-251 5.87e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 5.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       92 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGrffqpkdeggyfyfGELPLSLAACTNQPHIVHYLTENGhkqADLRR 171
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND--------------GNTPLHLAAANGNLEIVKLLLEAG---ADVNA 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      172 QDSRGNTVLHAlvAIADNTRENTKfvtkmydLLLIKCAklfpDTNLEallNNDGLSPLMMAAKTGKIGIFQHIIRREIAD 251
Cdd:COG0666 182 RDNDGETPLHL--AAENGHLEIVK-------LLLEAGA----DVNAK---DNDGKTALDLAAENGNLEIVKLLLEAGADL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-247 3.70e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 3.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       50 LPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYR---GQTALHIAIERRCKHYVELLVEKGADVHAQARGr 126
Cdd:COG0666  41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKddgGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD- 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D      127 ffqpkdeggyfyfGELPLSLAACTNQPHIVHYLTENGhkqADLRRQDSRGNTVLHAlvAIADNtreNTKFVtkmyDLLLI 206
Cdd:COG0666 120 -------------GETPLHLAAYNGNLEIVKLLLEAG---ADVNAQDNDGNTPLHL--AAANG---NLEIV----KLLLE 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3JXI_D      207 KCAklfpDTNleaLLNNDGLSPLMMAAKTGKIGIFQHIIRR 247
Cdd:COG0666 175 AGA----DVN---ARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-240 8.18e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 8.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       92 RGQTALHIAIERRCKHYVELLVEKGADVHAQARgrffqpkdeggyfyFGELPLSLAACTNQPHIVHYLTENGhkqADLRR 171
Cdd:COG0666 152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDN--------------DGETPLHLAAENGHLEIVKLLLEAG---ADVNA 214

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3JXI_D      172 QDSRGNTVLHAlvAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGI 240
Cdd:COG0666 215 KDNDGKTALDL--AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-122 7.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 7.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
3JXI_D         71 IAEKTGN---MREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQ 122
Cdd:pfam12796  36 LAAKNGHleiVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-249 3.87e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.25  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        144 LSLAACTNQPHIVHYLTENGHkqaDLRRQDSRGNTVLHAlvAIADNTRENTKfvtkmydlLLIKcaklFPDTNLeallNN 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA---DANLQDKNGRTALHL--AAKNGHLEIVK--------LLLE----HADVNL----KD 59

                          90       100
                  ....*....|....*....|....*.
3JXI_D        224 DGLSPLMMAAKTGKIGIFQHIIRREI 249
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEKGA 85
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 92-122 2.49e-04

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.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 2.49e-04
                          10        20        30
                  ....*....|....*....|....*....|..
3JXI_D         92 RGQTALHIAIERR-CKHYVELLVEKGADVHAQ 122
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNAR 32
Ank_2 pfam12796
Ankyrin repeats (3 copies);
97-181 1.14e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D         97 LHIAIERRCKHYVELLVEKGADVHAQARgrffqpkdeggyfyFGELPLSLAACTNQPHIVHYLTENghkqADLRRQDSrG 176
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK--------------NGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-G 61


                  ....*
3JXI_D        177 NTVLH 181
Cdd:pfam12796  62 RTALH 66
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 92-121 1.25e-03

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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 1.25e-03
                          10        20        30
                  ....*....|....*....|....*....|
3JXI_D         92 RGQTALHIAIERRCKHYVELLVEKGADVHA 121
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-235 2.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        56 NLSAGRNDTIPILLDIAEKTGNMREFI------NSPFRDVYYRGQTALHIAIERRC--KHYVELLVEKGADVHAQARGRF 127
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKKSNSYSIVeylldnGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       128 F-------QPKDEGGYFyfgelPLSLAACTNQPHIVHYLTEnghKQADLRRQDSRGNTVLHalVAIADNTRENTKFVTKM 200
Cdd:PHA03100 178 LlsygvpiNIKDVYGFT-----PLHYAVYNNNPEFVKYLLD---LGANPNLVNKYGDTPLH--IAILNNNKEIFKLLLNN 247

                        170       180       190
                 ....*....|....*....|....*....|....*..
3JXI_D       201 YDLL--LIKCAKLFPDTNLEALLNNDGLSPLMMAAKT 235
Cdd:PHA03100 248 GPSIktIIETLLYFKDKDLNTITKIKMLKKSIMYMFL 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
 88-229 2.44e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        88 DVYYRG---QTALHIAIERRCKHY---VELLVEKGADVHAQARgrffqpkdeggyfyFGELPLSLAACTNQ-PHIVHYLT 160
Cdd:PHA03095  39 DVNFRGeygKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPER--------------CGFTPLHLYLYNATtLDVIKLLI 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3JXI_D       161 ENGhkqADLRRQDSRGNTVLHALVaiadnTRENTKFvtKMYDLLLIKCAklfpdtNLEAlLNNDGLSPL 229
Cdd:PHA03095 105 KAG---ADVNAKDKVGRTPLHVYL-----SGFNINP--KVIRLLLRKGA------DVNA-LDLYGMTPL 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 92-121 2.93e-03

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.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 2.93e-03
                           10        20        30
                   ....*....|....*....|....*....|
3JXI_D          92 RGQTALHIAIERRCKHYVELLVEKGADVHA 121
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-232 7.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.25  E-value: 7.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D        48 TCLPKALLN-LSAGRNDTIPILLDIAEKTGNM------REFINSPFR---DVYYRG---QTALHIAIERRCKHYVELLVE 114
Cdd:PHA02874  66 TKIPHPLLTaIKIGAHDIIKLLIDNGVDTSILpipcieKDMIKTILDcgiDVNIKDaelKTFLHYAIKKGDLESIKMLFE 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3JXI_D       115 KGADVHAQargrffqpKDEGGYfyfgelPLSLAACTNQPHIVHYLTENGhkqADLRRQDSRGNTVLHALVAIADntRENT 194
Cdd:PHA02874 146 YGADVNIE--------DDNGCY------PIHIAIKHNFFDIIKLLLEKG---AYANVKDNNGESPLHNAAEYGD--YACI 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
3JXI_D       195 KFVTKMYDLLLIKC---------AKLFPDTNLEALLNN--------DGLSPLMMA 232
Cdd:PHA02874 207 KLLIDHGNHIMNKCkngftplhnAIIHNRSAIELLINNasindqdiDGSTPLHHA 261
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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