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PR00824

Identifier
HEPLIPASE  [View Relations]  [View Alignment]  
Accession
PR00824
No. of Motifs
9
Creation Date
18-FEB-1998  (UPDATE 07-JUN-1999)
Title
Hepatic lipase signature
Database References
PRINTS; PR00821 TAGLIPASE
PROSITE; PS00120 LIPASE_SER
BLOCKS; BL00120
INTERPRO; IPR002333
Literature References
1. CHAPUS, C., ROVERY, M., SARDA, L. AND VERGER, R.
Minireview on pancreatic lipase and colipase.
BIOCHIMIE 70 1223-1234 (1988).
 
2. PERSSON, B., BENGTSSON-OLIVECRONA, G., ENERBACK, S., OLIVECRONA, T.
AND JOERNVALL, H.
Structural features of lipoprotein-lipase - lipase family relationships,
binding interactions, non-equivalence of lipase cofactors, vitellogenin 
similarities and functional subdivision of lipoprotein-lipase.
EUR.J.BIOCHEMISTRY 179 39-45 (1989).
 
3. HEGELE, R.A., TU, L. AND CONNELLY, P.W.
Human hepatic lipase mutations and polymorphisms. 
HUM.MUTAT. 1 320-324 (1992). 
 
4. CAI, S.J., WONG, D.M., CHEN, S.H. AND CHAN, L.
Structure of the human hepatic triglyceride lipase gene. 
BIOCHEMISTRY 28 8966-8971 (1989). 
 
5. WION, K.L., KIRCHGESSNER, T.G., LUSIS, A.J., SCHOTZ, M.C. AND LAWN, R.M.
Human lipoprotein lipase complementary DNA sequence.
SCIENCE 235 1638-1641 (1987). 

Documentation
Triglyceride lipases (EC 3.1.1.3) are lipolytic enzymes that hydrolyse
ester linkages of triglycerides [1]. Lipases are widely distributed in
animals, plants and prokaryotes. At least three tissue-specific isozymes
exist in higher vertebrates: pancreatic, hepatic and gastric/lingual. These
lipases are closely related to each other and to lipoprotein lipase
(EC 3.1.1.34), which hydrolyses triglycerides of chylomicrons and very
low density lipoproteins (VLDL) [2].
 
Familial human hepatic lipase deficiency is a rare recessive disorder that
results from mutation in position 405 of the mature protein. The disease is
characterised by premature atherosclerosis and abnormal circulating 
lipoproteins [3].
 
The structure of the human hepatic triglyceride lipase gene has been
determined [4]. The hepatic lipase gene spans ~60 kb, and contains 8 introns
and 9 exons: exon 1 encodes the signal peptide; exon 4, a region that binds
to the lipoprotein substrate; exon 5, an evolutionarily highly-conserved 
region of potential catalytic function; and exons 6 and 9 encode sequences
rich in basic amino acids, thought to be important in anchoring the enzyme
to the endothelial surface by interacting with acidic domains of surface
glycosaminoglycans [4]. The human lipoprotein lipase gene has an identical
exon-intron organisation, with analogous structural domains, supporting the
common evolutionary origin of these two lipolytic enzymes [5]. 
 
HEPLIPASE is a 9-element fingerprint that provides a signature for hepatic
triacylglycerol lipases. The fingerprint was derived from an initial
alignment of 4 sequences: the motifs were drawn from conserved sections
spanning the full alignment length, focusing on those regions that
characterise the hepatic lipases but distinguish them from the rest of the
lipase family - motif 5 lies in a potential heparin binding domain. A single
iteration on OWL30.0 was required to reach convergence, no further sequences
being identified beyond the starting set.
 
An update on SPTR37_9f identified a true set of 5 sequences.
Summary Information
5 codes involving  9 elements
0 codes involving 8 elements
0 codes involving 7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
9555555555
8000000000
7000000000
6000000000
5000000000
4000000000
3000000000
2000000000
123456789
True Positives
LIPH_HUMAN    LIPH_MOUSE    LIPH_RAT      O46559        
Q99465
Sequence Titles
LIPH_HUMAN  TRIACYLGLYCEROL LIPASE, HEPATIC PRECURSOR (EC 3.1.1.3) (HEPATIC LIPASE) (HL) - HOMO SAPIENS (HUMAN). 
LIPH_MOUSE TRIACYLGLYCEROL LIPASE, HEPATIC PRECURSOR (EC 3.1.1.3) (HEPATIC LIPASE) (HL) - MUS MUSCULUS (MOUSE).
LIPH_RAT TRIACYLGLYCEROL LIPASE, HEPATIC PRECURSOR (EC 3.1.1.3) (HEPATIC LIPASE) (HL) - RATTUS NORVEGICUS (RAT).
O46559 HEPATIC LIPASE - ORYCTOLAGUS CUNICULUS (RABBIT).
Q99465 HEPATIC TRIGLYCERIDE LIPASE PRECURSOR - HOMO SAPIENS (HUMAN).
Scan History
OWL30_0    1  40   NSINGLE    
SPTR37_9f 2 7 NSINGLE
Initial Motifs
Motif 1  width=19
Element Seqn Id St Int Rpt
LQISVSLVLCIFIQSSACG RATHLP 5 5 -
LQISVSLVLCIFIQSSACG LIPH_RAT 5 5 -
LCFSILLVLCIFIQSSALG LIPH_HUMAN 6 6 -
LQISIFLVFCIFIQSSACG LIPH_MOUSE 5 5 -

Motif 2 width=17
Element Seqn Id St Int Rpt
GQSLKPEPFGRRAQAVE LIPH_HUMAN 24 -1 -
GQGVGTEPFGRNLGATE LIPH_RAT 23 -1 -
GQGVGTEPFGRNLGATE RATHLP 23 -1 -
GQGVGTEPFGRSLGATE LIPH_MOUSE 23 -1 -

Motif 3 width=14
Element Seqn Id St Int Rpt
GCQLRPQHPETLQE RATHLP 62 22 -
GCQLRPQHPETLQE LIPH_RAT 62 22 -
GCRLRPQHPETLQE LIPH_MOUSE 62 22 -
GCQIRINHPDTLQE LIPH_HUMAN 61 20 -

Motif 4 width=13
Element Seqn Id St Int Rpt
LKSQPAQPVNVGL LIPH_HUMAN 107 32 -
LKSRQSQPVNVGL RATHLP 108 32 -
LKSRQSQPVNVGL LIPH_RAT 108 32 -
LKSRQSQPVNVGL LIPH_MOUSE 108 32 -

Motif 5 width=15
Element Seqn Id St Int Rpt
VSGFAGSSMGGKRKI RATHLP 174 53 -
VSGFAGSSIGGTHKI LIPH_HUMAN 173 53 -
VSGFAGSSMGGKRKI LIPH_RAT 174 53 -
VSGFAGSSMDGKNKI LIPH_MOUSE 174 53 -

Motif 6 width=19
Element Seqn Id St Int Rpt
HSNLQNTGFQCSNMDSFSQ LIPH_RAT 293 104 -
HSNLQNTGFHCSNMDTFSQ RATHLP 293 104 -
HSDLQSIGFQCSDMGSFSQ LIPH_MOUSE 293 104 -
HAGTQSMAYPCGDMNSFSQ LIPH_HUMAN 292 104 -

Motif 7 width=19
Element Seqn Id St Int Rpt
TKEEIKKIPITLGEGITSN RATHLP 380 68 -
TKEKMQKIPITLGKGIASN LIPH_HUMAN 379 68 -
TKEEIKKIPITLGEGITSN LIPH_RAT 380 68 -
TKEEIKRIPITLGEGITSN LIPH_MOUSE 380 68 -

Motif 8 width=20
Element Seqn Id St Int Rpt
WENSAVWANVWNTVQTIMLW LIPH_MOUSE 421 22 -
WENSAVWANVWNTVQTIMLW RATHLP 421 22 -
WENSAVWANVWDTVQTIIPW LIPH_HUMAN 420 22 -
WENSAVWANVWNTVQTIMLW LIPH_RAT 421 22 -

Motif 9 width=16
Element Seqn Id St Int Rpt
CSENTDDLLLRPTQEK LIPH_HUMAN 467 27 -
CPENLDDLQLHPSQEK LIPH_MOUSE 468 27 -
CPDNVDDLQLHPTQEK LIPH_RAT 468 27 -
CPDNVDDLQLHPTQEK RATHLP 468 27 -
Final Motifs
Motif 1  width=19
Element Seqn Id St Int Rpt
LCFSILLVLCIFIQSSALG LIPH_HUMAN 6 6 -
LCFSILLVLCIFIQSSALG Q99465 6 6 -
LQISVSLVLCIFIQSSACG LIPH_RAT 5 5 -
LQISIFLVFCIFIQSSACG LIPH_MOUSE 5 5 -
LCVPIFLAVCILIQSSTHG O46559 5 5 -

Motif 2 width=17
Element Seqn Id St Int Rpt
GQSLKPEPFGRRAQAVE LIPH_HUMAN 24 -1 -
GQSLKPEPFGRRAQAVE Q99465 24 -1 -
GQGVGTEPFGRNLGATE LIPH_RAT 23 -1 -
GQGVGTEPFGRSLGATE LIPH_MOUSE 23 -1 -
GQSLRPEPFGRRARVTA O46559 23 -1 -

Motif 3 width=14
Element Seqn Id St Int Rpt
GCQIRINHPDTLQE LIPH_HUMAN 61 20 -
GCQIRINHPDTLQE Q99465 61 20 -
GCQLRPQHPETLQE LIPH_RAT 62 22 -
GCRLRPQHPETLQE LIPH_MOUSE 62 22 -
GCQIRLHHADTLQE O46559 61 21 -

Motif 4 width=13
Element Seqn Id St Int Rpt
LKSQPAQPVNVGL LIPH_HUMAN 107 32 -
LKSQPAQPVNVGL Q99465 107 32 -
LKSRQSQPVNVGL LIPH_RAT 108 32 -
LKSRQSQPVNVGL LIPH_MOUSE 108 32 -
LKSQPARPVNVGL O46559 107 32 -

Motif 5 width=15
Element Seqn Id St Int Rpt
VSGFAGSSIGGTHKI LIPH_HUMAN 173 53 -
VSGFAGSSIGGTHKI Q99465 173 53 -
VSGFAGSSMGGKRKI LIPH_RAT 174 53 -
VSGFAGSSMDGKNKI LIPH_MOUSE 174 53 -
VAGFAGSYISGKHKI O46559 173 53 -

Motif 6 width=19
Element Seqn Id St Int Rpt
HAGTQSMAYPCGDMNSFSQ LIPH_HUMAN 292 104 -
HAGTQSMAYPCGDMNSFSQ Q99465 292 104 -
HSNLQNTGFQCSNMDSFSQ LIPH_RAT 293 104 -
HSDLQSIGFQCSDMGSFSQ LIPH_MOUSE 293 104 -
HPSMQSTAYQCSDMDSFSQ O46559 292 104 -

Motif 7 width=19
Element Seqn Id St Int Rpt
TKEKMQKIPITLGKGIASN LIPH_HUMAN 379 68 -
TKEKMQKIPITLGKGIASN Q99465 379 68 -
TKEEIKKIPITLGEGITSN LIPH_RAT 380 68 -
TKEEIKRIPITLGEGITSN LIPH_MOUSE 380 68 -
TKEEMQKIPITLGEGITSN O46559 379 68 -

Motif 8 width=20
Element Seqn Id St Int Rpt
WENSAVWANVWDTVQTIIPW LIPH_HUMAN 420 22 -
WENSAVWANVWDTVQTIIPW Q99465 420 22 -
WENSAVWANVWNTVQTIMLW LIPH_RAT 421 22 -
WENSAVWANVWNTVQTIMLW LIPH_MOUSE 421 22 -
WENSAVWANVWNTVQTIIPW O46559 420 22 -

Motif 9 width=16
Element Seqn Id St Int Rpt
CSENTDDLLLRPTQEK LIPH_HUMAN 467 27 -
CSENTDDLLLRPTQEK Q99465 467 27 -
CPDNVDDLQLHPTQEK LIPH_RAT 468 27 -
CPENLDDLQLHPSQEK LIPH_MOUSE 468 27 -
CSENMDDLQLHPTQEK O46559 467 27 -