NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18204921|gb|AAH21642|]
View 

Lipase, hormone sensitive [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
6-314 5.32e-157

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: 457.49  E-value: 5.32e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921     6 MTQSLVTLAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 85
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921    86 LLHKSRYVASNRKSIFFRASHNLAELEAYLAALTQLRAMAYYAQRLLTINRPGVLFFEGDeGLTADFLQEYVTLHKGCFY 165
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921   166 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 245
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18204921   246 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPRLTVTISPPLAHTGPAPVLARLISYDLREGQD 314
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
334-464 1.09e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 136.93  E-value: 1.09e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921 334 RPHQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGST 413
Cdd:COG0657   5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18204921 414 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 464
Cdd:COG0657  85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314 5.32e-157

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: 457.49  E-value: 5.32e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921     6 MTQSLVTLAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 85
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921    86 LLHKSRYVASNRKSIFFRASHNLAELEAYLAALTQLRAMAYYAQRLLTINRPGVLFFEGDeGLTADFLQEYVTLHKGCFY 165
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921   166 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 245
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18204921   246 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPRLTVTISPPLAHTGPAPVLARLISYDLREGQD 314
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
334-464 1.09e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 136.93  E-value: 1.09e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921 334 RPHQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGST 413
Cdd:COG0657   5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18204921 414 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 464
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.
345-493 7.85e-35

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: 131.56  E-value: 7.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921   345 VVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGSTGERICLAGDSA 424
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18204921   425 GGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqSSASPSRLLSLM--DPLLPLSVLSKCVSAYSGTEAEDH 493
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
PRK10162 PRK10162
acetyl esterase;
332-434 4.93e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 88.62  E-value: 4.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921  332 RPRPHqaprSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLG 411
Cdd:PRK10162  75 YPQPD----SQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYG 150
                         90       100
                 ....*....|....*....|...
gi 18204921  412 STGERICLAGDSAGGNLCITVSL 434
Cdd:PRK10162 151 INMSRIGFAGDSAGAMLALASAL 173
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314 5.32e-157

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: 457.49  E-value: 5.32e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921     6 MTQSLVTLAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 85
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921    86 LLHKSRYVASNRKSIFFRASHNLAELEAYLAALTQLRAMAYYAQRLLTINRPGVLFFEGDeGLTADFLQEYVTLHKGCFY 165
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921   166 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 245
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18204921   246 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPRLTVTISPPLAHTGPAPVLARLISYDLREGQD 314
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
334-464 1.09e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 136.93  E-value: 1.09e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921 334 RPHQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGST 413
Cdd:COG0657   5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18204921 414 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 464
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.
345-493 7.85e-35

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: 131.56  E-value: 7.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921   345 VVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGSTGERICLAGDSA 424
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18204921   425 GGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqSSASPSRLLSLM--DPLLPLSVLSKCVSAYSGTEAEDH 493
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
PRK10162 PRK10162
acetyl esterase;
332-434 4.93e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 88.62  E-value: 4.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921  332 RPRPHqaprSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLG 411
Cdd:PRK10162  75 YPQPD----SQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYG 150
                         90       100
                 ....*....|....*....|...
gi 18204921  412 STGERICLAGDSAGGNLCITVSL 434
Cdd:PRK10162 151 INMSRIGFAGDSAGAMLALASAL 173
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
344-428 8.12e-13

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: 8.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921   344 LVVHIHGGGFVAQTSKSHEPYLKNWAQEL---GVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGSTGERICLA 420
Cdd:pfam20434  15 VVIWIHGGGWNSGDKEADMGFMTNTVKALlkaGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYGIDTNKIALM 94

                  ....*...
gi 18204921   421 GDSAGGNL 428
Cdd:pfam20434  95 GFSAGGHL 102
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
295-428 8.58e-04

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: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18204921   295 TGPAPVLARLISYDLREGQDSKVLNSLAKSEGPRLE---LRPRPHQ-APRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQ 370
Cdd:pfam10340  71 TGSSPTRYNLPSEDLLPNYGEIFTHKYLNQDMIDSTkfwLRKVPETfDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGK 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18204921   371 ELG-VPIFSIDYSLAPEAP----FPRALEECFFAYCWAVKhcdLLGSTgeRICLAGDSAGGNL 428
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH