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Conserved domains on  [gi|294459971|ref|NP_001170902|]
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transient receptor potential cation channel subfamily V member 4 isoform d [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
69-800 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


:

Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 1540.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  69 PMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPP-PILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLT 147
Cdd:cd22195    1 PMDSLFDYGTYRQHPTENKRRRKKIIEKKPNINSKAPAPDPpPVLKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 148 DEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQG 227
Cdd:cd22195   81 DEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 228 ADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKF 307
Cdd:cd22195  161 ADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPDIVHYLTENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 308 VTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDL 387
Cdd:cd22195  241 VTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGIFQHIIRREIKDEEARHLSRKFKDWAYGPVYSSLYDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 388 SSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYP 467
Cdd:cd22195  321 SSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAYYRPMEGTPPYP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 468 YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFA 547
Cdd:cd22195  401 YRTTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 548 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCR 627
Cdd:cd22195  481 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTVPTYPSCR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 628 DSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTI 707
Cdd:cd22195  561 DSNTFSKFLLDLFKLTIGMGDLEMLNSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTI 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 708 LDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDR 787
Cdd:cd22195  641 LDIERSFPVFLRKAFRSGEMVTVGKNLDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNDTYQYYGFSQTVGRLRRDR 720
                        730
                 ....*....|...
gi 294459971 788 WSSVVPRVVELNK 800
Cdd:cd22195  721 WSTVVPRVVELNK 733
 
Name Accession Description Interval E-value
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
69-800 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 1540.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  69 PMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPP-PILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLT 147
Cdd:cd22195    1 PMDSLFDYGTYRQHPTENKRRRKKIIEKKPNINSKAPAPDPpPVLKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 148 DEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQG 227
Cdd:cd22195   81 DEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 228 ADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKF 307
Cdd:cd22195  161 ADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPDIVHYLTENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 308 VTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDL 387
Cdd:cd22195  241 VTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGIFQHIIRREIKDEEARHLSRKFKDWAYGPVYSSLYDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 388 SSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYP 467
Cdd:cd22195  321 SSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAYYRPMEGTPPYP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 468 YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFA 547
Cdd:cd22195  401 YRTTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 548 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCR 627
Cdd:cd22195  481 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTVPTYPSCR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 628 DSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTI 707
Cdd:cd22195  561 DSNTFSKFLLDLFKLTIGMGDLEMLNSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTI 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 708 LDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDR 787
Cdd:cd22195  641 LDIERSFPVFLRKAFRSGEMVTVGKNLDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNDTYQYYGFSQTVGRLRRDR 720
                        730
                 ....*....|...
gi 294459971 788 WSSVVPRVVELNK 800
Cdd:cd22195  721 WSTVVPRVVELNK 733
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
115-765 9.98e-171

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: 511.93  E-value: 9.98e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  115 FNRPILFDIVSRGSTADLDGLLPFLLthkkrltdeefREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMrEFIN 194
Cdd:TIGR00870  51 LGRSALFVAAIENENLELTELLLNLS-----------CRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPL-ELAN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  195 SPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENP 274
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDP 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  275 HkkaDMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQH 354
Cdd:TIGR00870 199 A---DILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  355 IIRREVTdedtrhlSRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVY---NSKIENRHEMLAVEPINELLRDKWRK 431
Cdd:TIGR00870 276 KLAIKYK-------QKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVfviGLKFPELSDMYLIAPLSRLGQFKWKP 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  432 FGAVSFYINVVSYLCAMVIFTLTAYYQP---------LEGTPPY-PYRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMK 501
Cdd:TIGR00870 349 FIKFIFHSASYLYFLYLIIFTSVAYYRPtrtdlrvtgLQQTPLEmLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDF 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  502 kcpGVNSL----FIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILF 577
Cdd:TIGR00870 429 ---GMNSFylatFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMIL 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  578 KDLFRFLLVYLLFMIGYASALVSLLNPCANMKVcNEDqTNCTVPTypSCRDSETFSTFL---LDLFKLTIGMGDLEMLSS 654
Cdd:TIGR00870 506 GDILRFLFIYAVVLFGFACGLNQLYQYYDELKL-NEC-SNPHARS--CEKQGNAYSTLFetsQELFWAIIGLGDLLANEH 581
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  655 TKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLR-KAFRSGEMVTVG-- 731
Cdd:TIGR00870 582 KFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPpFNIIPGPKSFVGlf 661
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 294459971  732 ---KSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDP 765
Cdd:TIGR00870 662 kriEKHDGKKRQRWCRRVEEVNWTTWERKAETLIEDG 698
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
164-358 4.64e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 4.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 164 ALLNLSNGRNDTIPVLLDIAERTGN---MREFINSPFrDIYYR---GQTALHIAIERRCKHYVELLVAQGADVHAQARGr 237
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDleiVKLLLEAGA-DVNARdkdGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 238 ffqpkdeggyfyfGELPLSLAACTNQPHIVNYLTEnphKKADMRRQDSRGNTVLHAlvAIADNTRENTKfvtkmydLLLL 317
Cdd:COG0666  153 -------------GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHL--AAENGHLEIVK-------LLLE 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 294459971 318 KCArlfpDSNLEavlNNDGLSPLMMAAKTGKIGIFQHIIRR 358
Cdd:COG0666  208 AGA----DVNAK---DNDGKTALDLAAENGNLEIVKLLLEA 241
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
524-696 1.95e-13

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: 70.76  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  524 VLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILfKDLFRFLLVYLLFMIGYASALVSLLN 603
Cdd:pfam00520  74 VVVLPSLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSL-KSLGNLLLLLLLFLFIFAIIGYQLFG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  604 PCANMKV-CNEDQTNCTvpTYPSCrdsetfstfLLDLFKL--TIGMGD-LEMLSSTKYPVVFIILLVTYIILTFVLLLNM 679
Cdd:pfam00520 153 GKLKTWEnPDNGRTNFD--NFPNA---------FLWLFQTmtTEGWGDiMYDTIDGKGEFWAYIYFVSFIILGGFLLLNL 221
                         170
                  ....*....|....*..
gi 294459971  680 LIALMGETVGQVSKESK 696
Cdd:pfam00520 222 FIAVIIDNFQELTERTE 238
 
Name Accession Description Interval E-value
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
69-800 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 1540.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  69 PMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPP-PILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLT 147
Cdd:cd22195    1 PMDSLFDYGTYRQHPTENKRRRKKIIEKKPNINSKAPAPDPpPVLKVFNRPILFDIVSRGSTAELDGLLSFLLSHKKRLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 148 DEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQG 227
Cdd:cd22195   81 DEEFREPSTGKTCLPKALLNLNNGKNDTIPILLDIAEKTGNLREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 228 ADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKF 307
Cdd:cd22195  161 ADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPDIVHYLTENAHKKADLRRQDSRGNTVLHALVAIADNTRENTKF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 308 VTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDL 387
Cdd:cd22195  241 VTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGIFQHIIRREIKDEEARHLSRKFKDWAYGPVYSSLYDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 388 SSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYP 467
Cdd:cd22195  321 SSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAYYRPMEGTPPYP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 468 YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFA 547
Cdd:cd22195  401 YRTTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 548 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCR 627
Cdd:cd22195  481 LVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTVPTYPSCR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 628 DSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTI 707
Cdd:cd22195  561 DSNTFSKFLLDLFKLTIGMGDLEMLNSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTI 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 708 LDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDR 787
Cdd:cd22195  641 LDIERSFPVFLRKAFRSGEMVTVGKNLDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNDTYQYYGFSQTVGRLRRDR 720
                        730
                 ....*....|...
gi 294459971 788 WSSVVPRVVELNK 800
Cdd:cd22195  721 WSTVVPRVVELNK 733
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
129-749 0e+00

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: 990.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 129 TADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTAL 208
Cdd:cd22193    1 LEELLGFLQDLCRRRKDLTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 209 HIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGN 288
Cdd:cd22193   81 HIAIERRQGDIVALLVENGADVHAHAKGRFFQPKYQGEGFYFGELPLSLAACTNQPDIVQYLLENEHQPADIEAQDSRGN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 289 TVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHL 368
Cdd:cd22193  161 TVLHALVTVADNTKENTKFVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQREIKEPELRHL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 369 SRKFKDWAYGPVYSSLYDLSSLDTCGEEaSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAM 448
Cdd:cd22193  241 SRKFTDWAYGPVSSSLYDLSNVDTCEKN-SVLEIIVYNSKIDNRHEMLTLEPLNTLLQDKWDKFAKYMFFFSFCFYLFYM 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 449 VIFTLTAYYQPLEGTPPYP--YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSlFIDGSFQLLYFIYSVLV 526
Cdd:cd22193  320 IIFTLVAYYRPREDEPPPPlaKTTKMDYMRLLGEILVLLGGVYFFVKEIAYFLLRRSDLQSS-FSDSYFEILFFVQAVLV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 527 IVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCA 606
Cdd:cd22193  399 ILSVVLYLFAYKEYLACLVLALALGWANMLYYTRGFQSMGIYSVMIQKVILRDLLRFLFVYLLFLFGFAVALVSLIEKCS 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 607 NMKVCnedqtnctvptypsCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGE 686
Cdd:cd22193  479 SDKKD--------------CSSYGSFSDAVLELFKLTIGMGDLEFQENSTYPAVFLILLLTYVILTFVLLLNMLIALMGE 544
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294459971 687 TVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEV 749
Cdd:cd22193  545 TVNNVSKESKRIWKLQRAITILEFEKSFPECMRKAFRSGRLLKVGLCKDGTPDFRWCFRVDEV 607
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
113-762 0e+00

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: 880.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 113 KVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREF 192
Cdd:cd22196    3 KLYDRRRIFDAVAKGDCKELDGLLEYLMRTKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTISLLLDIAEKTGNLKEF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 193 INSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTE 272
Cdd:cd22196   83 VNAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGEFFKKKKGGPGFYFGELPLSLAACTNQLDIVKFLLE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 273 NPHKKADMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIF 352
Cdd:cd22196  163 NPHSPADISARDSMGNTVLHALVEVADNTPENTKFVTKMYNEILILGAKIRPLLKLEEITNKKGLTPLKLAAKTGKIGIF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 353 QHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDLSSLDTCgEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKF 432
Cdd:cd22196  243 AYILGREIKEPECRHLSRKFTEWAYGPVHSSLYDLSSIDTY-EKNSVLEIIAYSSETPNRHEMLLVEPLNKLLQDKWDKF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 433 GAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYPYR-TTVDYLRLAGEVITLFTGVLFFFTNIKDlFMKKCPGVNSLFI 511
Cdd:cd22196  322 VKRIFYFNFFVYFIYMIIFTLAAYYRPVNKTPPFPIEnTTGEYLRLTGEIISVSGGVYFFFRGIQY-FLQRRPSLKKLIV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 512 DGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFM 591
Cdd:cd22196  401 DSYCEILFFVQSLFLLASTVLYFCGRNEYVAFMVISLALGWANVLYYTRGFQQMGIYSVMIQKMILRDICRFLFVYLVFL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 592 IGYASALVSLL---NPCANMKV-CNEDQTNCTVPTYPScrdseTFSTFlLDLFKLTIGMGDLEMLSSTKYPVVFIILLVT 667
Cdd:cd22196  481 FGFSAALVTLIedgPPKGDVNTsQKECVCKSGYNSYNS-----LYSTC-LELFKFTIGMGDLEFTENYKFKEVFIFLLIS 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 668 YIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVD 747
Cdd:cd22196  555 YVILTYILLLNMLIALMGETVSKIAQESKNIWKLQRAITILDLEKSLLRCLRDRFRSGKSVLVGITPDGKEDYRWCFRVD 634
                        650
                 ....*....|....*
gi 294459971 748 EVNWSHWNQNLGIIN 762
Cdd:cd22196  635 EVNWNKWNTNLGIIN 649
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
112-749 0e+00

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: 707.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 112 LKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMRE 191
Cdd:cd22197    2 PNRFDRDRLFSVVSRGNPEELAGLLEYLRRTSKYLTDSEYTEGSTGKTCLMKAVLNLQDGVNACIMPLLEIDKDSGNPKP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 192 FINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQpKDEGGYFYFGELPLSLAACTNQPHIVNYLT 271
Cdd:cd22197   82 LVNAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQ-KKQGTCFYFGELPLSLAACTKQWDVVNYLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 272 ENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGI 351
Cdd:cd22197  161 ENPHQPASLQAQDSLGNTVLHALVMIADNSPENSALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 352 FQHIIRREVTDEdTRHLSRKFKDWAYGPVYSSLYDLSSLDTcGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRK 431
Cdd:cd22197  241 FRHILQREFSGP-YQHLSRKFTEWCYGPVRVSLYDLSSVDS-WEKNSVLEIIAFHSKSPNRHRMVVLEPLNKLLQEKWDR 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 432 FGAVsFYINVVSYLCAMVIFTLTAYYQPLEGTPPYPYR--TTVDYLRLAGEVITLFTGVLFFFTNIKdLFMKKCPGVNSL 509
Cdd:cd22197  319 LVSR-FYFNFLCYLVYMFIFTVVAYHQPLLDQPPIPPLkaTAGGSMLLLGHILILLGGIYLLLGQLW-YFWRRRLFIWIS 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 510 FIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLL 589
Cdd:cd22197  397 FMDSYFEILFLLQALLTVLSQVLYFMGSEWYLPLLVFSLVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLLVYLV 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 590 FMIGYASALVSLLNPCANMKVcNEDQTNCTVPTYPSCRDSE--TFSTFL---LDLFKLTIGMGDLEMLSSTKYPVVFIIL 664
Cdd:cd22197  477 FLFGFAVALVSLSREAPSPKA-PEDNNSTVTEQPTVGQEEEpaPYRSILdasLELFKFTIGMGELAFQEQLRFRGVVLLL 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 665 LVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCF 744
Cdd:cd22197  556 LLAYVLLTYVLLLNMLIALMSETVNHVADNSWSIWKLQKAISVLEMENGYWWCRRKKQREGRLLTVGTRPDGTPDERWCF 635

                 ....*
gi 294459971 745 RVDEV 749
Cdd:cd22197  636 RVEEM 640
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
116-767 0e+00

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: 706.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 116 NRPI--LFDIVSRGSTADLDGLLP--------FLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAER 185
Cdd:cd22194   43 QRDKkkRLKKVSEAAVEELGELLKelkdlsrrRRKTDVPDFLMHKLTASDTGKTCLMKALLNINENTKEIVRILLAFAEE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 186 TGNMREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPH 265
Cdd:cd22194  123 NGILDRFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFNPKYKHEGFYFGETPLALAACTNQPE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 266 IVNYLTENPHKKADMrrQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCArlfpDSNLEAVLNNDGLSPLMMAAK 345
Cdd:cd22194  203 IVQLLMEKESTDITS--QDSRGNTVLHALVTVAEDSKTQNDFVKRMYDMILLKSE----NKNLETIRNNEGLTPLQLAAK 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 346 TGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDLSSLDTCgEEASVLEILVYNSKIENRHEMLAVEPINELL 425
Cdd:cd22194  277 MGKAEILKYILSREIKEKPNRSLSRKFTDWAYGPVSSSLYDLTNVDTT-TDNSVLEIIVYNTNIDNRHEMLTLEPLHTLL 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 426 RDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGT-PPYPYR--TTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKK 502
Cdd:cd22194  356 HMKWKKFARYMFFISFLFYFFYNITLTLVSYYRPREDEdPPHPLAlsHKMGWLQLLGQMFVLIWATCLSVKEGIAIFLLR 435
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 503 CPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFR 582
Cdd:cd22194  436 PSDLKSILSDAWFHILFFIQAVLVIVSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSLGIYSVMIQKVILNDVLK 515
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 583 FLLVYLLFMIGYASALVSLLNPCanmkvcnedqtnctvPTYPSCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFI 662
Cdd:cd22194  516 FLLVYILFLLGFGVALASLIEDC---------------PDDSECSSYGSFSDAVLELFKLTIGLGDLEIQQNSKYPILFL 580
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 663 ILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSsdgtpDRRW 742
Cdd:cd22194  581 LLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKSLPEWLRKRFRLGELCKVADE-----DFRL 655
                        650       660
                 ....*....|....*....|....*
gi 294459971 743 CFRVDEVNWSHWNQNLGIINEDPGK 767
Cdd:cd22194  656 CLRINEVKWTEWKTHVSCLNEDPGP 680
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
132-749 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 673.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 132 LDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTALHIA 211
Cdd:cd21882    1 LEELLGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQTALHIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 212 IERRCKHYVELLVAQGADVHAQARGRFFQpKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVL 291
Cdd:cd21882   81 IENRNLNLVRLLVENGADVSARATGRFFR-KSPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 292 HALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTdEDTRHLSRK 371
Cdd:cd21882  160 HALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS-GPYQPLSRK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 372 FKDWAYGPVYSSLYDLSSLDTCGEEaSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIF 451
Cdd:cd21882  239 FTEWTYGPVTSSLYDLSEIDSWEKN-SVLELIAFSKKREARHQMLVQEPLNELLQEKWDRYGRPYFCFNFACYLLYMIIF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 452 TLTAYYQPLEGTPPYP--YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKcPGVNSLFIDGSFQLLYFIYSVLVIVS 529
Cdd:cd21882  318 TVCAYYRPLKDRPANQeaKATFGDSIRLVGEILTVLGGVYILLGEIPYFFRRR-LSRWFGFLDSYFEILFITQALLVLLS 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 530 AALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNpcanmk 609
Cdd:cd21882  397 MVLRFMETEGYVVPLVFSLVLGWCNVLYYTRGFQMLGIYTVMIQKMILRDLMRFCWVYLVFLFGFASAFVILFQ------ 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 610 vcNEDqtnctvptYPSCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVG 689
Cdd:cd21882  471 --TED--------PNKLGEFRDYPDALLELFKFTIGMGDLPFNENVDFPFVYLILLLAYVILTYLLLLNMLIALMGETVN 540
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 690 QVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEV 749
Cdd:cd21882  541 RVAQESDEIWKLQKAITTLMLERKYPRCLRKRSREGRLLKVGCGGDGGLDDRWCFRVEEV 600
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
115-765 9.98e-171

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: 511.93  E-value: 9.98e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  115 FNRPILFDIVSRGSTADLDGLLPFLLthkkrltdeefREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMrEFIN 194
Cdd:TIGR00870  51 LGRSALFVAAIENENLELTELLLNLS-----------CRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPL-ELAN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  195 SPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENP 274
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDP 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  275 HkkaDMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQH 354
Cdd:TIGR00870 199 A---DILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  355 IIRREVTdedtrhlSRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVY---NSKIENRHEMLAVEPINELLRDKWRK 431
Cdd:TIGR00870 276 KLAIKYK-------QKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVfviGLKFPELSDMYLIAPLSRLGQFKWKP 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  432 FGAVSFYINVVSYLCAMVIFTLTAYYQP---------LEGTPPY-PYRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMK 501
Cdd:TIGR00870 349 FIKFIFHSASYLYFLYLIIFTSVAYYRPtrtdlrvtgLQQTPLEmLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDF 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  502 kcpGVNSL----FIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILF 577
Cdd:TIGR00870 429 ---GMNSFylatFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMIL 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  578 KDLFRFLLVYLLFMIGYASALVSLLNPCANMKVcNEDqTNCTVPTypSCRDSETFSTFL---LDLFKLTIGMGDLEMLSS 654
Cdd:TIGR00870 506 GDILRFLFIYAVVLFGFACGLNQLYQYYDELKL-NEC-SNPHARS--CEKQGNAYSTLFetsQELFWAIIGLGDLLANEH 581
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  655 TKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLR-KAFRSGEMVTVG-- 731
Cdd:TIGR00870 582 KFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPpFNIIPGPKSFVGlf 661
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 294459971  732 ---KSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDP 765
Cdd:TIGR00870 662 kriEKHDGKKRQRWCRRVEEVNWTTWERKAETLIEDG 698
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
157-750 6.33e-126

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: 391.30  E-value: 6.33e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 157 GKTCLPKALLNlsnGRNDTIPVLLDIAertgnmREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADV-HAQAR 235
Cdd:cd22192   51 GETALHVAALY---DNLEAAVVLMEAA------PELVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvSPRAT 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 236 GRFFQPKdEGGYFYFGELPLSLAACTNQPHIVNYLTENphkKADMRRQDSRGNTVLHALVAIAdntreNTKFVTKMYDLL 315
Cdd:cd22192  122 GTFFRPG-PKNLIYYGEHPLSFAACVGNEEIVRLLIEH---GADIRAQDSLGNTVLHILVLQP-----NKTFACQMYDLI 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 316 LLKCARLFPDSnLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRRevtdedtrhlsRKFKDWAYGPVYSSLYDLSSLDTCGE 395
Cdd:cd22192  193 LSYDKEDDLQP-LDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQWTYGPLTSTLYDLTEIDSWGD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 396 EASVLEILVYNSKIENRHeMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEgtpPYP-------- 467
Cdd:cd22192  261 EQSVLELIVSSKKREARK-ILDVTPVKELVSLKWKRYGRPYFRILALLYLLYIIIFTLCCVYRPLK---PRPenntdprd 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 468 ------------YRTTVDYLRLAGEVITLFTGVLFFFTNIKDLF---MKKCPGVNSLfiDGSFQLLYFIYSVLVIVSAAL 532
Cdd:cd22192  337 itlyvqktlqesYVTPKDYLRLVGELISVLGAIVILLLEIPDILrvgVKRYFGQTVL--GGPFHVIIITYACLVLLTLVL 414
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 533 YLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALvsllnpcanMKVCN 612
Cdd:cd22192  415 RLTSLSGEVVPMSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIFGDLMKFCWLMFVVILGFSSAF---------YMIFQ 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 613 EDQTNCTVPTYPscrdsetFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVS 692
Cdd:cd22192  486 TEDPDSLGHFYD-------FPMTLFSTFELFLGLIDGPANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVA 558
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294459971 693 KESKHIWKLQWATTILDIERSFPVFLRKafRSGemvTVGKsSDGTPDrRWCFRVDEVN 750
Cdd:cd22192  559 HERDELWRAQVVATTLMLERRLPRCLWP--RSG---ICGK-EYGLGD-RWYLRVEDRN 609
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
164-358 4.64e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 4.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 164 ALLNLSNGRNDTIPVLLDIAERTGN---MREFINSPFrDIYYR---GQTALHIAIERRCKHYVELLVAQGADVHAQARGr 237
Cdd:COG0666   75 AAGADINAKDDGGNTLLHAAARNGDleiVKLLLEAGA-DVNARdkdGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 238 ffqpkdeggyfyfGELPLSLAACTNQPHIVNYLTEnphKKADMRRQDSRGNTVLHAlvAIADNTRENTKfvtkmydLLLL 317
Cdd:COG0666  153 -------------GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHL--AAENGHLEIVK-------LLLE 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 294459971 318 KCArlfpDSNLEavlNNDGLSPLMMAAKTGKIGIFQHIIRR 358
Cdd:COG0666  208 AGA----DVNAK---DNDGKTALDLAAENGNLEIVKLLLEA 241
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
524-696 1.95e-13

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: 70.76  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  524 VLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILfKDLFRFLLVYLLFMIGYASALVSLLN 603
Cdd:pfam00520  74 VVVLPSLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSL-KSLGNLLLLLLLFLFIFAIIGYQLFG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  604 PCANMKV-CNEDQTNCTvpTYPSCrdsetfstfLLDLFKL--TIGMGD-LEMLSSTKYPVVFIILLVTYIILTFVLLLNM 679
Cdd:pfam00520 153 GKLKTWEnPDNGRTNFD--NFPNA---------FLWLFQTmtTEGWGDiMYDTIDGKGEFWAYIYFVSFIILGGFLLLNL 221
                         170
                  ....*....|....*..
gi 294459971  680 LIALMGETVGQVSKESK 696
Cdd:pfam00520 222 FIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
203-351 8.42e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 8.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971 203 RGQTALHIAIERRCKHYVELLVAQGADVHAQARgrffqpkdeggyfyFGELPLSLAACTNQPHIVNYLTEnphKKADMRR 282
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDN--------------DGETPLHLAAENGHLEIVKLLLE---AGADVNA 214
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294459971 283 QDSRGNTVLHAlvAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGI 351
Cdd:COG0666  215 KDNDGKTALDL--AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
255-356 1.76e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  255 LSLAACTNQPHIVNYLTENPHkkaDMRRQDSRGNTVLHAlvAIADNTRENTKfvtkmydlLLLKcarlFPDSNLeavlNN 334
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA---DANLQDKNGRTALHL--AAKNGHLEIVK--------LLLE----HADVNL----KD 59
                          90       100
                  ....*....|....*....|..
gi 294459971  335 DGLSPLMMAAKTGKIGIFQHII 356
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-233 3.55e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 3.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 294459971  182 IAERTGN---MREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQ 233
Cdd:pfam12796  36 LAAKNGHleiVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
169-284 9.72e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 9.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  169 SNGRNDTIPVLLDIAERTGNMREFinspfrdiyyrGQTALHIAIERRCKHYVELLVAqgadvHAQARGRffqpkdeggyf 248
Cdd:pfam12796   6 KNGNLELVKLLLENGADANLQDKN-----------GRTALHLAAKNGHLEIVKLLLE-----HADVNLK----------- 58
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 294459971  249 YFGELPLSLAACTNQPHIVNYLTEnphKKADMRRQD 284
Cdd:pfam12796  59 DNGRTALHYAARSGHLEIVKLLLE---KGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
203-233 5.86e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 5.86e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 294459971  203 RGQTALHIAIERR-CKHYVELLVAQGADVHAQ 233
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNAR 32
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-292 2.47e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294459971  208 LHIAIERRCKHYVELLVAQGADVHAQARgrffqpkdeggyfyFGELPLSLAACTNQPHIVNYLTENPHKKAdmrrqDSRG 287
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK--------------NGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNG 61

                  ....*
gi 294459971  288 NTVLH 292
Cdd:pfam12796  62 RTALH 66
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
203-232 4.75e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 4.75e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 294459971  203 RGQTALHIAIERRCKHYVELLVAQGADVHA 232
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
 
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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