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Conserved domains on  [gi|269308251|ref|NP_666145|]
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ankyrin repeat and MYND domain-containing protein 2 [Mus musculus]

Protein Classification

zf-MYND domain-containing protein( domain architecture ID 12790888)

zf-MYND domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-132 2.29e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 2.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVV 109
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         90       100
                 ....*....|....*....|...
gi 269308251 110 NSVGRTAAQMAAFVGQHDCVAII 132
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLL 238
zf-MYND pfam01753
MYND finger;
320-357 1.60e-10

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 1.60e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 269308251  320 CTTCGEKGAS-KRCSVCKMVIYCDQTCQKTHWFAHKKMC 357
Cdd:pfam01753   1 CAVCGKEALKlLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-132 2.29e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 2.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVV 109
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         90       100
                 ....*....|....*....|...
gi 269308251 110 NSVGRTAAQMAAFVGQHDCVAII 132
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-110 3.31e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251   30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHG-ADASChqheHGYTALMFAALSGNKDITWVMLEAGAETDV 108
Cdd:pfam12796  14 KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAdVNLKD----NGRTALHYAARSGHLEIVKLLLEKGADINV 89


                  ..
gi 269308251  109 VN 110
Cdd:pfam12796  90 KD 91
zf-MYND pfam01753
MYND finger;
320-357 1.60e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 1.60e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 269308251  320 CTTCGEKGAS-KRCSVCKMVIYCDQTCQKTHWFAHKKMC 357
Cdd:pfam01753   1 CAVCGKEALKlLRCSRCKSVYYCSKECQKADWPYHKKEC 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-111 2.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  31 LLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADASChQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVN 110
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                 .
gi 269308251 111 S 111
Cdd:PHA03100 256 E 256
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-71 7.38e-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: 42.57  E-value: 7.38e-06
                           10        20
                   ....*....|....*....|....*..
gi 269308251    45 NGMTPLMHAAYKGKLEMCKLLLRHGAD 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 46-115 1.04e-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: 44.62  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  46 GMTPLMHAAYKGKLEMCKLLLRHGADAS----------------CHQHEHgytALMFAALSGNKDITWVMLEAGAETDVV 109
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpknlIYYGEH---PLSFAACVGNEEIVRLLIEHGADIRAQ 165


                 ....*.
gi 269308251 110 NSVGRT 115
Cdd:cd22192  166 DSLGNT 171
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-132 2.29e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 2.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVV 109
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         90       100
                 ....*....|....*....|...
gi 269308251 110 NSVGRTAAQMAAFVGQHDCVAII 132
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-131 4.73e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 4.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  16 LLEVIGKGTVQEAgRLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDI 95
Cdd:COG0666   91 LHAAARNGDLEIV-KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEI 168

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 269308251  96 TWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCVAI 131
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-134 2.46e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  16 LLEVIGKGTVQEAGRLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDI 95
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 269308251  96 TWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCV-------AIINN 134
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVkllleagADVNA 181
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-132 2.06e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVV 109
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                         90       100
                 ....*....|....*....|...
gi 269308251 110 NSVGRTAAQMAAFVGQHDCVAII 132
Cdd:COG0666  249 DKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-110 3.31e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251   30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHG-ADASChqheHGYTALMFAALSGNKDITWVMLEAGAETDV 108
Cdd:pfam12796  14 KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAdVNLKD----NGRTALHYAARSGHLEIVKLLLEKGADINV 89


                  ..
gi 269308251  109 VN 110
Cdd:pfam12796  90 KD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-132 2.26e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251   50 LMHAAYKGKLEMCKLLLRHGADASCHQHEhGYTALMFAALSGNKDITWVMLEaGAETDVVNSvGRTAAQMAAFVGQHDCV 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77


                  ...
gi 269308251  130 AII 132
Cdd:pfam12796  78 KLL 80
zf-MYND pfam01753
MYND finger;
320-357 1.60e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 1.60e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 269308251  320 CTTCGEKGAS-KRCSVCKMVIYCDQTCQKTHWFAHKKMC 357
Cdd:pfam01753   1 CAVCGKEALKlLRCSRCKSVYYCSKECQKADWPYHKKEC 39
Ank_5 pfam13857
Ankyrin repeats (many copies);
31-87 1.75e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 1.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269308251   31 LLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADASCHQhEHGYTALMFA 87
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-131 1.87e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  31 LLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVN 110
Cdd:COG0666   39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                         90       100
                 ....*....|....*....|.
gi 269308251 111 SVGRTAAQMAAFVGQHDCVAI 131
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKL 138
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-95 1.00e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 269308251   46 GMTPLMHAAYKGKLEMCKLLLRHGADASChQHEHGYTALMFAALSGNKDI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEV 49
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-111 2.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  31 LLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADASChQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVN 110
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                 .
gi 269308251 111 S 111
Cdd:PHA03100 256 E 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-145 4.24e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 4.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269308251   84 LMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCV-AIINNFFPRERLDYYT 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKDNGRT 63
Ank_4 pfam13637
Ankyrin repeats (many copies);
27-66 1.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.75e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 269308251   27 EAGRLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLL 66
Cdd:pfam13637  15 ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-71 7.38e-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: 42.57  E-value: 7.38e-06
                           10        20
                   ....*....|....*....|....*..
gi 269308251    45 NGMTPLMHAAYKGKLEMCKLLLRHGAD 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-134 8.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 8.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  13 EKELLEVIGKGTVQEAGRLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADA-------------------- 72
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPdipntdkfsplhlavmmgdi 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269308251  73 ----------SCHQHE--HGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQmaafvgqhdCVAIINN 134
Cdd:PHA02875 149 kgiellidhkACLDIEdcCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL---------CYAIENN 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 45-71 1.91e-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: 41.51  E-value: 1.91e-05
                          10        20
                  ....*....|....*....|....*...
gi 269308251   45 NGMTPLMHAAYK-GKLEMCKLLLRHGAD 71
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGAD 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 45-74 2.75e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 2.75e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 269308251   45 NGMTPLMHAAYKGKLEMCKLLLRHGADASC 74
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-133 8.51e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  30 RLLSSKNVHVNCLDENGMTPL-MHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMfAALSG---NKDITWVMLEAGAE 105
Cdd:PHA03095  67 RLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVN-AKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGAD 144

                         90       100
                 ....*....|....*....|....*....
gi 269308251 106 TDVVNSVGRTAaqMAAFVGQHDC-VAIIN 133
Cdd:PHA03095 145 VNALDLYGMTP--LAVLLKSRNAnVELLR 171
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 46-115 1.04e-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: 44.62  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  46 GMTPLMHAAYKGKLEMCKLLLRHGADAS----------------CHQHEHgytALMFAALSGNKDITWVMLEAGAETDVV 109
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpknlIYYGEH---PLSFAACVGNEEIVRLLIEHGADIRAQ 165


                 ....*.
gi 269308251 110 NSVGRT 115
Cdd:cd22192  166 DSLGNT 171
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-132 1.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.18  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  37 VHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADASChQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTA 116
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                         90
                 ....*....|....*.
gi 269308251 117 AQMAAFVGQHDCVAII 132
Cdd:PHA02874 194 LHNAAEYGDYACIKLL 209
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-112 1.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNK-DITWVMLEAGAETDV 108
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNI 230


                 ....
gi 269308251 109 VNSV 112
Cdd:PHA02875 231 MFMI 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-120 2.90e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269308251   65 LLRHGADASCHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMA 120
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
80-129 8.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 8.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 269308251   80 GYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCV 129
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 50-156 2.26e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  50 LMHAAYKGKLEMCKLLLRHGADASCHQHeHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCV 129
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                         90       100
                 ....*....|....*....|....*...
gi 269308251 130 AIINNFFPRE-RLDYYTKPQGLDKEPKL 156
Cdd:PTZ00322 165 QLLSRHSQCHfELGANAKPDSFTGKPPS 192
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 30-100 2.26e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269308251  30 RLLSSKNVHVNCLDENGMTPLMHAAYKGKLEMCKLLLRHGADASCHQHEhGYTALMFAALSGNKDITWVML 100
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD-GKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-112 7.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 7.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  25 VQEAGRLLSSKNVHVNCLDENGMTPLMHAAYK--GKLEMCKLLLRHGADASCHQHEhGYTALMfAALSGNK---DITWVM 99
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD-GENLLH-LYLESNKidlKILKLL 162

                         90
                 ....*....|...
gi 269308251 100 LEAGAETDVVNSV 112
Cdd:PHA03100 163 IDKGVDINAKNRV 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 38-133 8.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269308251  38 HVNCLDENGMTPLMHA-AYKGKLEMCKLLLRHGADASCHQHEHGYTALMFAALSgnKDITWVMLEAGAETDVVNSVGRTA 116
Cdd:PHA02878 226 STDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303

                         90
                 ....*....|....*..
gi 269308251 117 AQMAafVGQHDCVAIIN 133
Cdd:PHA02878 304 LSSA--VKQYLCINIGR 318
 
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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