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Conserved domains on  [gi|85566768|gb|AAI12095|]
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Dysferlin interacting protein 1 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-147 2.82e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 2.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  33 LFLDHIRQGDLEQVGRFIRtRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDI 112
Cdd:COG0666  90 LLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 85566768 113 ARYLISLGADRDATNDDGDLPSDL-IDPDYKELVEL 147
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLaAENGHLEIVKL 204
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-147 2.82e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 2.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  33 LFLDHIRQGDLEQVGRFIRtRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDI 112
Cdd:COG0666  90 LLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 85566768 113 ARYLISLGADRDATNDDGDLPSDL-IDPDYKELVEL 147
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLaAENGHLEIVKL 204
Ank_2 pfam12796
Ankyrin repeats (3 copies);
68-129 7.88e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 7.88e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85566768    68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISlGADRDATNDD 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG 61
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-148 1.50e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   62 PSGLAALHEAVLSG--NLECVKLLVKYGADIHQ----------------RDEAGWTPLHIACSDGYPDIARYLISLGADR 123
Cdd:PHA03100 139 SDGENLLHLYLESNkiDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218

                         90       100
                 ....*....|....*....|....*.
gi 85566768  124 DATNDDGDLPSDL-IDPDYKELVELF 148
Cdd:PHA03100 219 NLVNKYGDTPLHIaILNNNKEIFKLL 244
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 97-122 8.21e-06

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: 40.65  E-value: 8.21e-06
                           10        20
                   ....*....|....*....|....*.
gi 85566768     97 GWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 64-122 1.52e-05

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: 43.72  E-value: 1.52e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85566768  64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEA-------------GWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ 144
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 64-122 6.17e-04

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: 38.91  E-value: 6.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85566768    64 GLAALHEAVLSGNLECVKLLVKYGADIHQR---DEA-----------GWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgDFFvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD 200
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-147 2.82e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 2.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  33 LFLDHIRQGDLEQVGRFIRtRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDI 112
Cdd:COG0666  90 LLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 85566768 113 ARYLISLGADRDATNDDGDLPSDL-IDPDYKELVEL 147
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLaAENGHLEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-149 3.82e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 3.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  38 IRQGDLEQVGRFIRtRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLI 117
Cdd:COG0666 128 AYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90       100       110
                ....*....|....*....|....*....|...
gi 85566768 118 SLGADRDATNDDGDLPSDL-IDPDYKELVELFK 149
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLaAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-133 4.45e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.85  E-value: 4.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  20 MLADRSVRFPNDVLFLDHIRQGDLEQVGRFIRTRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWT 99
Cdd:COG0666  43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122

                        90       100       110
                ....*....|....*....|....*....|....
gi 85566768 100 PLHIACSDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
68-129 7.88e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 7.88e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85566768    68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISlGADRDATNDD 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG 61
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-137 3.31e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 3.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  38 IRQGDLEQVGRFIRtRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLI 117
Cdd:COG0666 161 AANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                        90       100
                ....*....|....*....|
gi 85566768 118 SLGADRDATNDDGDLPSDLI 137
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLA 259
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-127 4.00e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768    38 IRQGDLEQVgRFIRTRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYgADIHQRDEaGWTPLHIACSDGYPDIARYLI 117
Cdd:pfam12796   5 AKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 85566768   118 SLGADRDATN 127
Cdd:pfam12796  82 EKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
64-117 5.38e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 5.38e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 85566768    64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLI 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-148 1.50e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   62 PSGLAALHEAVLSG--NLECVKLLVKYGADIHQ----------------RDEAGWTPLHIACSDGYPDIARYLISLGADR 123
Cdd:PHA03100 139 SDGENLLHLYLESNkiDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218

                         90       100
                 ....*....|....*....|....*.
gi 85566768  124 DATNDDGDLPSDL-IDPDYKELVELF 148
Cdd:PHA03100 219 NLVNKYGDTPLHIaILNNNKEIFKLL 244
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 74-150 3.49e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 3.49e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85566768   74 SGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLPSDL-IDPDYKELVELFKG 150
Cdd:PTZ00322  92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELaEENGFREVVQLLSR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-148 5.78e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 5.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  30 NDVLFLDHIRQGDLEQVGRFIRTRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGY 109
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 85566768 110 PDIARYLISLGADRDATNDDGDLPSDL-IDPDYKELVELF 148
Cdd:COG0666 100 LEIVKLLLEAGADVNARDKDGETPLHLaAYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-135 1.93e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 1.93e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85566768   63 SGLAALHEAVLSGN-LECVKLLVKYGADIHQRDEAGWTPLHIACSDGY--PDIARYLISLGADRDATNDDGDLPSD 135
Cdd:PHA03095  82 CGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 68-133 2.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 2.09e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85566768   68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
Ank_5 pfam13857
Ankyrin repeats (many copies);
82-136 3.05e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 85566768    82 LLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLPSDL 136
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 68-134 5.64e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 5.64e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85566768   68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLPS 134
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSP 692
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-149 1.50e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLPSDLiDPDYKE 143
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETLLYFKDK-DLNTIT 270


                 ....*.
gi 85566768  144 LVELFK 149
Cdd:PHA03100 271 KIKMLK 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-130 2.24e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 2.24e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85566768   62 PSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSD--GYPDIARYLISLGADRDATNDDG 130
Cdd:PHA03100  71 PLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDG 141
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 97-128 8.05e-07

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: 43.43  E-value: 8.05e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 85566768    97 GWTPLHIAC-SDGYPDIARYLISLGADRDATND 128
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-104 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.52e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 85566768    67 ALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIA 104
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 68-132 3.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 3.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85566768   68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDL 132
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCV 203
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-127 5.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   20 MLADRSVRFPNDVLFLDHIRQGDLEqVGRFIRTRKVSLATIHPSGLAALHEAVLSGNL-ECVKLLVKYGADIHQRDEAGW 98
Cdd:PHA02876 230 IIDNRSNINKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGE 308

                         90       100       110
                 ....*....|....*....|....*....|
gi 85566768   99 TPLHIACSDGY-PDIARYLISLGADRDATN 127
Cdd:PHA02876 309 TPLYLMAKNGYdTENIRTLIMLGADVNAAD 338
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-129 5.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 5.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85566768   61 HPSGLAALHEAVLSGNLECVKLLV---KYGADIHQRDeaGWTPLHIACSDGYPDIARYLISLGADRDATNDD 129
Cdd:PHA02875  65 YPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 97-125 5.55e-06

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: 41.09  E-value: 5.55e-06
                          10        20
                  ....*....|....*....|....*....
gi 85566768    97 GWTPLHIACSDGYPDIARYLISLGADRDA 125
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-133 8.08e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 8.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85566768   77 LECVKLLVKYGADIHQRDEAGWTPLHI----ACSDgYPDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLylhySSEK-VKDIVRLLLEAGADVNAPERCGFTP 86
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 97-122 8.21e-06

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: 40.65  E-value: 8.21e-06
                           10        20
                   ....*....|....*....|....*.
gi 85566768     97 GWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-95 1.27e-05

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: 39.97  E-value: 1.27e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 85566768    64 GLAALHEAVLS-GNLECVKLLVKYGADIHQRDE 95
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 64-122 1.52e-05

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: 43.72  E-value: 1.52e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85566768  64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEA-------------GWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ 144
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-133 1.54e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   30 NDVLFLDHIRQGDLEQVGRFIRTRK----------VSLATIHPSGLAALHEAVLSGNLECVKL--LVKYGADIHQRDEAG 97
Cdd:PHA03095 178 ADVYAVDDRFRSLLHHHLQSFKPRArivreliragCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 85566768   98 WTPLHIACSDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 29-122 1.98e-05

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: 43.08  E-value: 1.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  29 PNDVLFLDHIRQGDLEQVGRFIRTRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYG---------ADIHQrdeaGWT 99
Cdd:cd22192  16 ISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQ----GET 91

                        90       100
                ....*....|....*....|...
gi 85566768 100 PLHIACSDGYPDIARYLISLGAD 122
Cdd:cd22192  92 ALHIAVVNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 67-91 2.12e-05

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: 39.49  E-value: 2.12e-05
                           10        20
                   ....*....|....*....|....*
gi 85566768     67 ALHEAVLSGNLECVKLLVKYGADIH 91
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 68-127 2.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 2.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATN 127
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY 100
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-104 3.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 3.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85566768   36 DHIRQGDLEQVGRFIRTRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIA 104
Cdd:PHA02875  74 DAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 78-122 3.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 3.99e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 85566768   78 ECVKLLVKYGADIHQRDE-AGWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:PHA02878 148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGAN 193
Ank_4 pfam13637
Ankyrin repeats (many copies);
97-133 5.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 85566768    97 GWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-122 5.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   38 IRQGDLEQVGRFIRTRKVSLATIHPSGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLI 117
Cdd:PHA02874   9 IYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88


                 ....*
gi 85566768  118 SLGAD 122
Cdd:PHA02874  89 DNGVD 93
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-133 9.05e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 9.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 85566768   77 LECVKLLVKYGADIHQRDEAGWTPLHI-ACSDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA03095  63 KDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTP 120
PHA03095 PHA03095
ankyrin-like protein; Provisional
 76-133 1.08e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   76 NLECVKLLVKYGADIHQRDEAGWTPLHIAC--SDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTP 225
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 68-125 1.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 1.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSD--GYpDIARYLISLGADRDA 125
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYckDY-DILKLLLEHGVDVNA 263
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 71-103 1.27e-04

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: 40.77  E-value: 1.27e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 85566768  71 AVLSGNLECVKLLVKYGADIHQRDEAGWTPLHI 103
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 64-117 1.48e-04

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: 40.61  E-value: 1.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85566768  64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEA-------------GWTPLHIACSDGYPDIARYLI 117
Cdd:cd22197  94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLL 160
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 64-118 2.09e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 85566768   64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLIS 118
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 64-122 2.66e-04

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: 40.00  E-value: 2.66e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 85566768  64 GLAALHEAVLSGNLECVKLLVKYGADIhQRDEA---------------GWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD 161
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 67-148 2.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   67 ALHEAVLSGN-LECVKLLVKYGADIHQRDEAGWTPLHIACSDG-YPDIARYLISLGADRDATNDDGDLPSdLIDPDYKEL 144
Cdd:PHA02876 411 ALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL-LIALEYHGI 489


                 ....
gi 85566768  145 VELF 148
Cdd:PHA02876 490 VNIL 493
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 68-133 3.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 3.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85566768   68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGY-----PDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITP 109
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-91 3.77e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 3.77e-04
                          10        20
                  ....*....|....*....|....*...
gi 85566768    64 GLAALHEAVLSGNLECVKLLVKYGADIH 91
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-133 4.50e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 4.50e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 85566768   101 LHIACSDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-132 5.64e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 38.78  E-value: 5.64e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  63 SGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDL 132
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 64-122 6.17e-04

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: 38.91  E-value: 6.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85566768    64 GLAALHEAVLSGNLECVKLLVKYGADIHQR---DEA-----------GWTPLHIACSDGYPDIARYLISLGAD 122
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgDFFvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD 200
PHA02798 PHA02798
ankyrin-like protein; Provisional
 77-130 7.31e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 7.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 85566768   77 LECVKLLVKYGADIHQRDEAGWTPLHIACSDGY---PDIARYLISLGADRDATNDDG 130
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDG 145
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 64-117 7.87e-04

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: 38.62  E-value: 7.87e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85566768  64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEA--------------GWTPLHIACSDGYPDIARYLI 117
Cdd:cd22193  76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLL 143
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 64-133 9.76e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 38.35  E-value: 9.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   64 GLAALHEAVLSGNL--ECVKLLVKYGADIHQRDEAGWTPLHIACS--------------DGYPDIARYLISLGADRDATN 127
Cdd:PHA02716 317 GRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVN 396


                 ....*.
gi 85566768  128 DDGDLP 133
Cdd:PHA02716 397 CLGYTP 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-120 1.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   38 IRQGDLEQVGRFIRTR-KVSLATIHpsGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYL 116
Cdd:PHA02874 132 IKKGDLESIKMLFEYGaDVNIEDDN--GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209


                 ....
gi 85566768  117 ISLG 120
Cdd:PHA02874 210 IDHG 213
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-133 2.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.17  E-value: 2.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85566768   64 GLAALHEAVLS-GNLECVKLLVKYGADIHQRDEA-GWTPLHIACSDgyPDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA02878 234 GNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
PHA02795 PHA02795
ankyrin-like protein; Provisional
 77-130 3.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 36.51  E-value: 3.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 85566768   77 LECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDG 130
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNG 254
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 64-116 3.69e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 36.77  E-value: 3.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 85566768   64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYL 116
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 64-131 6.77e-03

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: 35.94  E-value: 6.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768  64 GLAALHEAVLSGNLECVKLLVKYGADIHQRDEA--------------GWTPLHIACSDGYPDIARYLIS---LGADRDAT 126
Cdd:cd22196  94 GQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADISAR 173


                ....*
gi 85566768 127 NDDGD 131
Cdd:cd22196 174 DSMGN 178
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 64-117 6.85e-03

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: 35.98  E-value: 6.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85566768  64 GLAALHEAVLSGNLECVKLLVKYGADIHQ---------RDEAGW-----TPLHIACSDGYPDIARYLI 117
Cdd:cd22195 137 GQTALHIAIERRCKHYVELLVEKGADVHAqargrffqpKDEGGYfyfgeLPLSLAACTNQPDIVHYLT 204
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 68-104 6.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 35.71  E-value: 6.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 85566768   68 LHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIA 104
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 63-133 6.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 35.63  E-value: 6.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 85566768   63 SGLAALHEAVLSGNLECVKLLVKYGADIHQRDEAGWTPLHIACSDGYPDIARYLISLGADRDATNDDGDLP 133
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 76-127 9.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 35.18  E-value: 9.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85566768   76 NLECVKLLVKYGADIHQRDEAGWTPLHI---ACSDGYpDIARYLISLGA-----DRDATN 127
Cdd:PHA02859 102 EPEILKILIDSGSSITEEDEDGKNLLHMymcNFNVRI-NVIKLLIDSGVsflnkDFDNNN 160
 
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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