NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1480771384|ref|NP_001353075|]
View 

transient receptor potential cation channel subfamily M member 3 isoform n [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
 153-418 6.68e-174

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


:

Pssm-ID: 465665  Cd Length: 266  Bit Score: 516.36  E-value: 6.68e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  153 AMYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVG 232
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  233 DALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQ 312
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  313 LEKHISLQKINTRIGQGVPVVALIVEGGPNVISIVLEYLRDTPPVPVVVCDGSGRASDILAFGHKYSEEGGLINESLRDQ 392
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPPVPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240

                          250       260
                   ....*....|....*....|....*.
gi 1480771384  393 LLVTIQKTFTYTRTQAQHLFIILMEC 418
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
 1227-1282 2.90e-24

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


:

Pssm-ID: 465156  Cd Length: 56  Bit Score: 96.63  E-value: 2.90e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1480771384 1227 DERIRVTSERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERL 1282
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 881-1199 1.81e-18

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 TIGR00870:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 743  Bit Score: 91.30  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  881 PIVKFWFYTLAYIGYLMLF------NYIVLVKMERWPSTQ----EWIVISYIftLGIEKMREILMsepgkLLQKVKVWLQ 950
Cdd:TIGR00870  348 PFIKFIFHSASYLYFLYLIiftsvaYYRPTRTDLRVTGLQqtplEMLIVTWV--DGLRLGEEKLI-----WLGGIFEYIH 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  951 EYWNVTDLIAILLFSVGMILR-------------LQDQPFRSDGRVIYCV-----NIIYWyIRLLDIFGVNKYLGPYVMM 1012
Cdd:TIGR00870  421 QLWNILDFGMNSFYLATFLDRpfailfvtqaflvLREHWLRFDPTLIEEAlfafaLVLSW-LNLLYIFRGNQHLGPLQIM 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1013 IGKMMI-DMMYFVIIMLVVLMSFGVARQAILF---PNEEPSWKLAKNIFYMPYWMIYGEVFA----------DQIDPPCG 1078
Cdd:TIGR00870  500 IGRMILgDILRFLFIYAVVLFGFACGLNQLYQyydELKLNECSNPHARSCEKQGNAYSTLFEtsqelfwaiiGLGDLLAN 579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1079 QNE-TREDGKIiqlppcktgawivpaIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIM-TFHERPVL 1156
Cdd:TIGR00870  580 EHKfTEFVGLL---------------LFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMsYEREGGTC 644

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1480771384 1157 PPPLIIFS-------HMTMIFQHLC---CRWRKHESDPDERDYGLKLFITDDE 1199
Cdd:TIGR00870  645 PPPFNIIPgpksfvgLFKRIEKHDGkkrQRWCRRVEEVNWTTWERKAETLIED 697
 
Name Accession Description Interval E-value
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
 153-418 6.68e-174

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


Pssm-ID: 465665  Cd Length: 266  Bit Score: 516.36  E-value: 6.68e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  153 AMYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVG 232
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  233 DALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQ 312
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  313 LEKHISLQKINTRIGQGVPVVALIVEGGPNVISIVLEYLRDTPPVPVVVCDGSGRASDILAFGHKYSEEGGLINESLRDQ 392
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPPVPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240

                          250       260
                   ....*....|....*....|....*.
gi 1480771384  393 LLVTIQKTFTYTRTQAQHLFIILMEC 418
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
 1227-1282 2.90e-24

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


Pssm-ID: 465156  Cd Length: 56  Bit Score: 96.63  E-value: 2.90e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1480771384 1227 DERIRVTSERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERL 1282
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 881-1199 1.81e-18

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: 91.30  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  881 PIVKFWFYTLAYIGYLMLF------NYIVLVKMERWPSTQ----EWIVISYIftLGIEKMREILMsepgkLLQKVKVWLQ 950
Cdd:TIGR00870  348 PFIKFIFHSASYLYFLYLIiftsvaYYRPTRTDLRVTGLQqtplEMLIVTWV--DGLRLGEEKLI-----WLGGIFEYIH 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  951 EYWNVTDLIAILLFSVGMILR-------------LQDQPFRSDGRVIYCV-----NIIYWyIRLLDIFGVNKYLGPYVMM 1012
Cdd:TIGR00870  421 QLWNILDFGMNSFYLATFLDRpfailfvtqaflvLREHWLRFDPTLIEEAlfafaLVLSW-LNLLYIFRGNQHLGPLQIM 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1013 IGKMMI-DMMYFVIIMLVVLMSFGVARQAILF---PNEEPSWKLAKNIFYMPYWMIYGEVFA----------DQIDPPCG 1078
Cdd:TIGR00870  500 IGRMILgDILRFLFIYAVVLFGFACGLNQLYQyydELKLNECSNPHARSCEKQGNAYSTLFEtsqelfwaiiGLGDLLAN 579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1079 QNE-TREDGKIiqlppcktgawivpaIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIM-TFHERPVL 1156
Cdd:TIGR00870  580 EHKfTEFVGLL---------------LFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMsYEREGGTC 644

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1480771384 1157 PPPLIIFS-------HMTMIFQHLC---CRWRKHESDPDERDYGLKLFITDDE 1199
Cdd:TIGR00870  645 PPPFNIIPgpksfvgLFKRIEKHDGkkrQRWCRRVEEVNWTTWERKAETLIED 697
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 888-1133 1.33e-15

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 77.69  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  888 YTLAYIGYLMLFNYIVLVKMERWPSTQEW---------IVISYIFTLgiekmrEILMsepgKLLQ--KVKVWLQEYWNVT 956
Cdd:pfam00520    2 RYFELFILLLILLNTIFLALETYFQPEEPlttvleildYVFTGIFTL------EMLL----KIIAagFKKRYFRSPWNIL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  957 DLIAILLFSVGMILRLQDQPFrsdgrVIYCVNIIYWyIRLLDIFGVNKYLGPYVMMIGKMMIDMMYFVIIMLVVLMSFGV 1036
Cdd:pfam00520   72 DFVVVLPSLISLVLSSVGSLS-----GLRVLRLLRL-LRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1037 ARQaILFPNEEPSWKLA-------KNIFYMPYWMI-------YGEVFADQIDppcgqnetredgkiiqlppcKTGAWIVP 1102
Cdd:pfam00520  146 IGY-QLFGGKLKTWENPdngrtnfDNFPNAFLWLFqtmttegWGDIMYDTID--------------------GKGEFWAY 204

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1480771384 1103 AIMACYLLVANILLVNLLIAVFNNTFFEVKS 1133
Cdd:pfam00520  205 IYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1004-1142 1.77e-09

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: 61.95  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1004 KYLGPYVMMIGKMMI-DMMYFVIIMLVVLMSFGVARQaILFPNEEPSWKLAKNIFYMPYWMIYgEVFADQIDPPCGQNet 1082
Cdd:cd22192    445 QMLGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAFY-MIFQTEDPDSLGHFYDFPMTLFSTF-ELFLGLIDGPANYT-- 520

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1083 redgkiIQLPPcktgawIVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQ 1142
Cdd:cd22192    521 ------VDLPF------MYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWRAQ 568
 
Name Accession Description Interval E-value
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
 153-418 6.68e-174

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


Pssm-ID: 465665  Cd Length: 266  Bit Score: 516.36  E-value: 6.68e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  153 AMYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVG 232
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  233 DALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQ 312
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  313 LEKHISLQKINTRIGQGVPVVALIVEGGPNVISIVLEYLRDTPPVPVVVCDGSGRASDILAFGHKYSEEGGLINESLRDQ 392
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPPVPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240

                          250       260
                   ....*....|....*....|....*.
gi 1480771384  393 LLVTIQKTFTYTRTQAQHLFIILMEC 418
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
 1227-1282 2.90e-24

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


Pssm-ID: 465156  Cd Length: 56  Bit Score: 96.63  E-value: 2.90e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1480771384 1227 DERIRVTSERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERL 1282
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 881-1199 1.81e-18

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: 91.30  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  881 PIVKFWFYTLAYIGYLMLF------NYIVLVKMERWPSTQ----EWIVISYIftLGIEKMREILMsepgkLLQKVKVWLQ 950
Cdd:TIGR00870  348 PFIKFIFHSASYLYFLYLIiftsvaYYRPTRTDLRVTGLQqtplEMLIVTWV--DGLRLGEEKLI-----WLGGIFEYIH 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  951 EYWNVTDLIAILLFSVGMILR-------------LQDQPFRSDGRVIYCV-----NIIYWyIRLLDIFGVNKYLGPYVMM 1012
Cdd:TIGR00870  421 QLWNILDFGMNSFYLATFLDRpfailfvtqaflvLREHWLRFDPTLIEEAlfafaLVLSW-LNLLYIFRGNQHLGPLQIM 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1013 IGKMMI-DMMYFVIIMLVVLMSFGVARQAILF---PNEEPSWKLAKNIFYMPYWMIYGEVFA----------DQIDPPCG 1078
Cdd:TIGR00870  500 IGRMILgDILRFLFIYAVVLFGFACGLNQLYQyydELKLNECSNPHARSCEKQGNAYSTLFEtsqelfwaiiGLGDLLAN 579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1079 QNE-TREDGKIiqlppcktgawivpaIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIM-TFHERPVL 1156
Cdd:TIGR00870  580 EHKfTEFVGLL---------------LFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMsYEREGGTC 644

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1480771384 1157 PPPLIIFS-------HMTMIFQHLC---CRWRKHESDPDERDYGLKLFITDDE 1199
Cdd:TIGR00870  645 PPPFNIIPgpksfvgLFKRIEKHDGkkrQRWCRRVEEVNWTTWERKAETLIED 697
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 888-1133 1.33e-15

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 77.69  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  888 YTLAYIGYLMLFNYIVLVKMERWPSTQEW---------IVISYIFTLgiekmrEILMsepgKLLQ--KVKVWLQEYWNVT 956
Cdd:pfam00520    2 RYFELFILLLILLNTIFLALETYFQPEEPlttvleildYVFTGIFTL------EMLL----KIIAagFKKRYFRSPWNIL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  957 DLIAILLFSVGMILRLQDQPFrsdgrVIYCVNIIYWyIRLLDIFGVNKYLGPYVMMIGKMMIDMMYFVIIMLVVLMSFGV 1036
Cdd:pfam00520   72 DFVVVLPSLISLVLSSVGSLS-----GLRVLRLLRL-LRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1037 ARQaILFPNEEPSWKLA-------KNIFYMPYWMI-------YGEVFADQIDppcgqnetredgkiiqlppcKTGAWIVP 1102
Cdd:pfam00520  146 IGY-QLFGGKLKTWENPdngrtnfDNFPNAFLWLFqtmttegWGDIMYDTID--------------------GKGEFWAY 204

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1480771384 1103 AIMACYLLVANILLVNLLIAVFNNTFFEVKS 1133
Cdd:pfam00520  205 IYFVSFIILGGFLLLNLFIAVIIDNFQELTE 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1004-1142 1.77e-09

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: 61.95  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1004 KYLGPYVMMIGKMMI-DMMYFVIIMLVVLMSFGVARQaILFPNEEPSWKLAKNIFYMPYWMIYgEVFADQIDPPCGQNet 1082
Cdd:cd22192    445 QMLGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAFY-MIFQTEDPDSLGHFYDFPMTLFSTF-ELFLGLIDGPANYT-- 520

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1083 redgkiIQLPPcktgawIVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQ 1142
Cdd:cd22192    521 ------VDLPF------MYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWRAQ 568
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1004-1143 2.61e-08

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: 58.35  E-value: 2.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1004 KYLGPYVMMIGKMMI-DMMYFVIIMLVVLMSFGVARqAILFPNEEPSWKLAKNIFYMPYWMIYgEVFADQIDPPCGQNet 1082
Cdd:cd21882    430 QMLGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAF-VILFQTEDPNKLGEFRDYPDALLELF-KFTIGMGDLPFNEN-- 505

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1480771384 1083 redgkiIQLPpcktgaWIVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQR 1143
Cdd:cd21882    506 ------VDFP------FVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 988-1160 1.07e-03

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: 43.59  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384  988 NIIYwYIRLLDIFGVnkylgpYVMMIGKMMI-DMMYFVIIMLVVLMSFGVARQAILfpNEEPSWKLAKNifYMPYWMIYG 1066
Cdd:cd22194    487 NMLY-YTRGFQSLGI------YSVMIQKVILnDVLKFLLVYILFLLGFGVALASLI--EDCPDDSECSS--YGSFSDAVL 555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480771384 1067 EVFADQIDppCGQNETREDGKIIQLppcktgawiVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQL 1146
Cdd:cd22194    556 ELFKLTIG--LGDLEIQQNSKYPIL---------FLLLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRART 624

                          170
                   ....*....|....
gi 1480771384 1147 IMTFHERpvLPPPL 1160
Cdd:cd22194    625 ILEFEKS--LPEWL 636
RNase_Y_N pfam12072
RNase Y N-terminal region;
1235-1293 3.01e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 3.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1480771384 1235 ERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERLTGLERAESNKI 1293
Cdd:pfam12072   96 RKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELERISGLTSEEAKEI 154
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH