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[1]
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NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND FUNCTION IN HIBERNATION.
TISSUE=Heart;
DOI=10.1073/pnas.95.14.8392; PubMed=9653197 [NCBI, ExPASy, EBI, Israel, Japan]
Andrews M.T.,
Squire T.L.,
Bowen C.M.,
Rollins M.B.;
"Low-temperature carbon utilization is regulated by novel gene activity in the heart of a hibernating mammal.";
Proc. Natl. Acad. Sci. U.S.A. 95:8392-8397(1998).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
DOI=10.1152/physiolgenomics.00167.2002; PubMed=14583598 [NCBI, ExPASy, EBI, Israel, Japan]
Squire T.L.,
Andrews M.T.;
"Pancreatic triacylglycerol lipase in a hibernating mammal. I. Novel genomic organization.";
Physiol. Genomics 16:119-130(2003).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=White adipose tissue;
Bauer V.W.,
Andrews M.T.;
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
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[4]
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TISSUE SPECIFICITY.
DOI=10.1152/physiolgenomics.00168.2002; PubMed=14583599 [NCBI, ExPASy, EBI, Israel, Japan]
Squire T.L.,
Lowe M.E.,
Bauer V.W.,
Andrews M.T.;
"Pancreatic triacylglycerol lipase in a hibernating mammal. II. Cold-adapted function and differential expression.";
Physiol. Genomics 16:131-140(2003).
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- FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones (By similarity). Play a role in hibernation as a key enzyme that shows high activity at low temperatures. When expressed in the hibernating heart it liberates fatty acids from triglycerides at temperatures as low as 0 degrees Celsius.
- CATALYTIC ACTIVITY: Triacylglycerol + H2O = diacylglycerol + a carboxylate.
- SUBCELLULAR LOCATION: Secreted (By similarity).
- TISSUE SPECIFICITY: Expressed in many tissues with highest expression in liver. During hibernation there is a significant increases in expression in heart, white adipose tissue (WAT), and testis; but not in pancreas.
- INDUCTION: Up-regulated during hibernation.
- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
- SIMILARITY: Contains 1 PLAT domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 465 AA [This is the length of the unprocessed precursor] |
Molecular weight: 51227 Da [This is the MW of the unprocessed precursor] |
CRC64: A152FB00CD01169B [This is a checksum on the sequence] |
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10 20 30 40 50 60
MLLVWSLALL LGAVAGKEVC YDRLGCFSDD SPWSGIVERP LKVLPWSPAD VNTRFLLYTN
70 80 90 100 110 120
ENQDNYQQIT ADSSRIQSSN FKTNRKTRFI IHGFIDKGEE SWLANMCKKM FQVESVNCIC
130 140 150 160 170 180
VDWKGGSRTG YTQASQNIRI VGAEVAYFVD FLRTQLGYSP SNVHVIGHSL GSHAAGEAGR
190 200 210 220 230 240
RTNGAIGRIT GLDPAEPCFE GTPELVRLDP SDAQFVDAIH TDGAPIVPNL GFGMSQTVGH
250 260 270 280 290 300
LDFFPNGGIE MPGCQKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPTGFAAF
310 320 330 340 350 360
SCASYSVFSA NKCFPCPSGG CPQMGHYADR YSGKTNGVGQ KFYLNTGDKS NFSRWRYKVS
370 380 390 400 410 420
VTLSGQKVTG HILVSLFGNA GNSKQYEIYK GSLHPGYTHS NEFDSDVDVG DLQRVKFIWY
430 440 450 460
NNVINPSLPR VGASSISVER NDGRVFKFCS AETVREDVLL TLNAC
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O88354 in FASTA format |
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