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Conserved domains on  [gi|1039777411|ref|XP_006539633|]
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hormone-sensitive lipase isoform X1 [Mus musculus]

Protein Classification

hormone-sensitive lipase( domain architecture ID 10533829)

hormone-sensitive lipase displays broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters; belongs to the alpha/beta hydrolase superfamily

EC:  3.1.1.-
Gene Symbol:  LIPE
Gene Ontology:  GO:0016787|GO:0016298

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
304-612 1.64e-155

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


:

Pssm-ID: 461882  Cd Length: 306  Bit Score: 462.88  E-value: 1.64e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  304 MTQSLVTLAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 383
Cdd:pfam06350    1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  384 LLHKSRYVASNRKSIFFRASHNLAELEAYLAALTQLRAMAYYAQRLLTINRPGVLFFEGDeGLTADFLQEYVTLHKGCFY 463
Cdd:pfam06350   80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  464 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 543
Cdd:pfam06350  159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777411  544 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPRLTVTISPPLAHTGPAPVLARLISYDLREGQD 612
Cdd:pfam06350  239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
632-762 7.83e-38

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 140.78  E-value: 7.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  632 RPHQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGST 711
Cdd:COG0657      5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039777411  712 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 762
Cdd:COG0657     85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
16-188 7.21e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411   16 ETQERPIIKPDPGPE-----TTLTDHPGSKMLQESGTPQKQSLPNEPTAQQEAEFQqeqgIQQSALL--QKFLTPFA--F 86
Cdd:pfam03154  175 QAQSGAASPPSPPPPgttqaATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL----IQQTPTLhpQRLPSPHPplQ 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411   87 PAPQQSSPSQkVHLDQQEAISPNGPGAgkvyTTPQEPQLGEEHMgmtkSGPAEPPPATEAETTSTAQAVSGPDKKPSTQT 166
Cdd:pfam03154  251 PMTQPPPPSQ-VSPQPLPQPSLHGQMP----PMPHSLQTGPSHM----QHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQS 321
                          170       180
                   ....*....|....*....|..
gi 1039777411  167 NLVSQEGPEQSDPTAQQTPLVQ 188
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPREQ 343
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
304-612 1.64e-155

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 462.88  E-value: 1.64e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  304 MTQSLVTLAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 383
Cdd:pfam06350    1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  384 LLHKSRYVASNRKSIFFRASHNLAELEAYLAALTQLRAMAYYAQRLLTINRPGVLFFEGDeGLTADFLQEYVTLHKGCFY 463
Cdd:pfam06350   80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  464 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 543
Cdd:pfam06350  159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777411  544 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPRLTVTISPPLAHTGPAPVLARLISYDLREGQD 612
Cdd:pfam06350  239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
632-762 7.83e-38

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 140.78  E-value: 7.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  632 RPHQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGST 711
Cdd:COG0657      5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039777411  712 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 762
Cdd:COG0657     85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
643-791 8.99e-36

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 135.03  E-value: 8.99e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  643 VVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGSTGERICLAGDSA 722
Cdd:pfam07859    1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777411  723 GGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqSSASPSRLLSLM--DPLLPLSVLSKCVSAYSGTEAEDH 791
Cdd:pfam07859   81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
PRK10162 PRK10162
acetyl esterase;
630-732 5.25e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 89.39  E-value: 5.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  630 RPRPHqaprSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLG 709
Cdd:PRK10162    75 YPQPD----SQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYG 150
                           90       100
                   ....*....|....*....|...
gi 1039777411  710 STGERICLAGDSAGGNLCITVSL 732
Cdd:PRK10162   151 INMSRIGFAGDSAGAMLALASAL 173
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
16-188 7.21e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411   16 ETQERPIIKPDPGPE-----TTLTDHPGSKMLQESGTPQKQSLPNEPTAQQEAEFQqeqgIQQSALL--QKFLTPFA--F 86
Cdd:pfam03154  175 QAQSGAASPPSPPPPgttqaATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL----IQQTPTLhpQRLPSPHPplQ 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411   87 PAPQQSSPSQkVHLDQQEAISPNGPGAgkvyTTPQEPQLGEEHMgmtkSGPAEPPPATEAETTSTAQAVSGPDKKPSTQT 166
Cdd:pfam03154  251 PMTQPPPPSQ-VSPQPLPQPSLHGQMP----PMPHSLQTGPSHM----QHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQS 321
                          170       180
                   ....*....|....*....|..
gi 1039777411  167 NLVSQEGPEQSDPTAQQTPLVQ 188
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPREQ 343
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
304-612 1.64e-155

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 462.88  E-value: 1.64e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  304 MTQSLVTLAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 383
Cdd:pfam06350    1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  384 LLHKSRYVASNRKSIFFRASHNLAELEAYLAALTQLRAMAYYAQRLLTINRPGVLFFEGDeGLTADFLQEYVTLHKGCFY 463
Cdd:pfam06350   80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  464 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 543
Cdd:pfam06350  159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777411  544 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPRLTVTISPPLAHTGPAPVLARLISYDLREGQD 612
Cdd:pfam06350  239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
632-762 7.83e-38

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 140.78  E-value: 7.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  632 RPHQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGST 711
Cdd:COG0657      5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039777411  712 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 762
Cdd:COG0657     85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
643-791 8.99e-36

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 135.03  E-value: 8.99e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  643 VVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGSTGERICLAGDSA 722
Cdd:pfam07859    1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777411  723 GGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqSSASPSRLLSLM--DPLLPLSVLSKCVSAYSGTEAEDH 791
Cdd:pfam07859   81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
PRK10162 PRK10162
acetyl esterase;
630-732 5.25e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 89.39  E-value: 5.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  630 RPRPHqaprSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLG 709
Cdd:PRK10162    75 YPQPD----SQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYG 150
                           90       100
                   ....*....|....*....|...
gi 1039777411  710 STGERICLAGDSAGGNLCITVSL 732
Cdd:PRK10162   151 INMSRIGFAGDSAGAMLALASAL 173
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
642-726 1.20e-12

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 68.36  E-value: 1.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  642 LVVHIHGGGFVAQTSKSHEPYLKNWAQEL---GVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGSTGERICLA 718
Cdd:pfam20434   15 VVIWIHGGGWNSGDKEADMGFMTNTVKALlkaGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYGIDTNKIALM 94

                   ....*...
gi 1039777411  719 GDSAGGNL 726
Cdd:pfam20434   95 GFSAGGHL 102
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
16-188 7.21e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411   16 ETQERPIIKPDPGPE-----TTLTDHPGSKMLQESGTPQKQSLPNEPTAQQEAEFQqeqgIQQSALL--QKFLTPFA--F 86
Cdd:pfam03154  175 QAQSGAASPPSPPPPgttqaATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL----IQQTPTLhpQRLPSPHPplQ 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411   87 PAPQQSSPSQkVHLDQQEAISPNGPGAgkvyTTPQEPQLGEEHMgmtkSGPAEPPPATEAETTSTAQAVSGPDKKPSTQT 166
Cdd:pfam03154  251 PMTQPPPPSQ-VSPQPLPQPSLHGQMP----PMPHSLQTGPSHM----QHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQS 321
                          170       180
                   ....*....|....*....|..
gi 1039777411  167 NLVSQEGPEQSDPTAQQTPLVQ 188
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPREQ 343
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
593-726 1.28e-03

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 42.52  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777411  593 TGPAPVLARLISYDLREGQDSKVLNSLAKSEGPRLE---LRPRPHQ-APRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQ 668
Cdd:pfam10340   71 TGSSPTRYNLPSEDLLPNYGEIFTHKYLNQDMIDSTkfwLRKVPETfDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGK 150
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039777411  669 ELG-VPIFSIDYSLAPEAP----FPRALEECFFAYCWAVKhcdLLGSTgeRICLAGDSAGGNL 726
Cdd:pfam10340  151 YFPdMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYLTL---TKGCK--NVTLMGDSAGGNL 208
 
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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