UniProtKB - P07867 (LIPC_RAT)
Protein
Hepatic triacylglycerol lipase
Gene
Lipc
Organism
Rattus norvegicus (Rat)
Status
Functioni
Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (PubMed:7074125, PubMed:6747460, PubMed:1770315, PubMed:1865764, PubMed:1531641). Also exhibits lysophospholipase activity (PubMed:1531641). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (PubMed:1865764). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (By similarity).By similarity5 Publications
Catalytic activityi
- EC:3.1.1.34 Publications
- a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H+ + sn-glycerol 3-phosphocholine1 PublicationEC:3.1.1.51 Publication
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+4 PublicationsEC:3.1.1.324 Publications
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H+2 PublicationsThis reaction proceeds in the forward1 Publication direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H+ + sn-glycero-3-phospho-L-serine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine1 PublicationThis reaction proceeds in the forward1 Publication direction.
Activity regulationi
Phospholipase A1 and lysophospholipase activities are inhibited by annexin II.1 Publication
Kineticsi
- KM=0.82 mM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol1 Publication
- KM=0.16 mM for 1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine1 Publication
- Vmax=144 µmol/min/mg enzyme with 1-oleoyl-sn-glycerol as substrate1 Publication
- Vmax=163 µmol/min/mg enzyme with 1,2-dioleoyl-sn-glycerol as substrate1 Publication
- Vmax=145 µmol/min/mg enzyme with 1,3-dioleoyl-sn-glycerol as substrate1 Publication
- Vmax=67 µmol/min/mg enzyme with phosphatidic acid as substrate1 Publication
- Vmax=50 µmol/min/mg enzyme with phosphatidylethanolamine as substrate1 Publication
- Vmax=4 µmol/min/mg enzyme with phosphatidylcholine as substrate1 Publication
pH dependencei
Optimum pH is 8-9.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 169 | NucleophileBy similarity | 1 | |
Active sitei | 195 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 280 | Charge relay systemPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- 1-acyl-2-lysophosphatidylserine acylhydrolase activity Source: UniProtKB-EC
- acylglycerol lipase activity Source: RGD
- apolipoprotein binding Source: RGD
- carboxylic ester hydrolase activity Source: RGD
- chylomicron binding Source: BHF-UCL
- heparan sulfate proteoglycan binding Source: RGD
- heparin binding Source: RGD
- identical protein binding Source: RGD
- lipase activity Source: RGD
- lipid binding Source: RGD
- lipoprotein lipase activity Source: GO_Central
- low-density lipoprotein particle binding Source: BHF-UCL
- lysophospholipase activity Source: RGD
- phosphatidyl phospholipase B activity Source: UniProtKB-EC
- phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC
- phospholipase A1 activity Source: UniProtKB
- phospholipase activity Source: GO_Central
- transferase activity, transferring acyl groups Source: RGD
- triglyceride lipase activity Source: UniProtKB
GO - Biological processi
- cellular response to hormone stimulus Source: RGD
- cholesterol homeostasis Source: RGD
- cholesterol metabolic process Source: RGD
- cholesterol transport Source: RGD
- chylomicron remnant clearance Source: RGD
- chylomicron remodeling Source: RGD
- circadian rhythm Source: RGD
- developmental growth Source: RGD
- fatty acid biosynthetic process Source: RGD
- fatty acid metabolic process Source: RGD
- glycerophospholipid catabolic process Source: RGD
- heparan sulfate proteoglycan biosynthetic process Source: RGD
- high-density lipoprotein particle remodeling Source: RGD
- lipid catabolic process Source: GO_Central
- liver development Source: RGD
- low-density lipoprotein particle clearance Source: RGD
- low-density lipoprotein particle remodeling Source: BHF-UCL
- neutral lipid catabolic process Source: RGD
- phosphatidic acid metabolic process Source: RGD
- phosphatidylcholine metabolic process Source: RGD
- phosphatidylethanolamine metabolic process Source: RGD
- phosphatidylserine metabolic process Source: RGD
- regulation of plasma lipoprotein particle levels Source: RGD
- response to acetate Source: RGD
- response to amino acid Source: RGD
- response to calcium ion Source: RGD
- response to carbohydrate Source: RGD
- response to copper ion Source: RGD
- response to drug Source: RGD
- response to fatty acid Source: RGD
- response to glucocorticoid Source: RGD
- response to hormone Source: RGD
- response to hypoxia Source: RGD
- response to inorganic substance Source: RGD
- response to lipid Source: RGD
- response to magnesium ion Source: RGD
- response to nutrient levels Source: RGD
- response to organic cyclic compound Source: RGD
- response to peptide hormone Source: RGD
- triglyceride catabolic process Source: RGD
- triglyceride homeostasis Source: RGD
- triglyceride metabolic process Source: RGD
- very-low-density lipoprotein particle remodeling Source: RGD
Keywordsi
Molecular function | Heparin-binding, Hydrolase |
Biological process | Lipid degradation, Lipid metabolism |
Enzyme and pathway databases
Reactomei | R-RNO-8963889, Assembly of active LPL and LIPC lipase complexes R-RNO-8964026, Chylomicron clearance |
Protein family/group databases
ESTHERi | ratno-1hlip, Hepatic_Lipase |
Chemistry databases
SwissLipidsi | SLP:000000571 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Lipc |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3009, Lipc |
Subcellular locationi
Extracellular region or secreted
- Secreted By similarity
Endosome
- early endosome Source: RGD
- late endosome Source: RGD
Extracellular region or secreted
- extracellular space Source: RGD
- high-density lipoprotein particle Source: UniProtKB-KW
Other locations
- cell surface Source: RGD
- microvillus Source: RGD
Keywords - Cellular componenti
HDL, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | By similarityAdd BLAST | 21 | |
ChainiPRO_0000017771 | 22 – 494 | Hepatic triacylglycerol lipaseAdd BLAST | 473 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 79 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 398 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
GlycoproteinProteomic databases
PaxDbi | P07867 |
PeptideAtlasi | P07867 |
PTM databases
GlyGeni | P07867, 2 sites |
Interactioni
Subunit structurei
Homodimer.
By similarityGO - Molecular functioni
- apolipoprotein binding Source: RGD
- heparan sulfate proteoglycan binding Source: RGD
- identical protein binding Source: RGD
Protein-protein interaction databases
IntActi | P07867, 1 interactor |
STRINGi | 10116.ENSRNOP00000047403 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 353 – 487 | PLATPROSITE-ProRule annotationAdd BLAST | 135 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 255 – 278 | Essential for determining substrate specificityBy similarityAdd BLAST | 24 |
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG502QVTG, Eukaryota |
InParanoidi | P07867 |
PhylomeDBi | P07867 |
Family and domain databases
CDDi | cd00707, Pancreat_lipase_like, 1 hit |
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR013818, Lipase/vitellogenin IPR002333, Lipase_hep IPR016272, Lipase_LIPH IPR033906, Lipase_N IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR000734, TAG_lipase |
PANTHERi | PTHR11610, PTHR11610, 1 hit PTHR11610:SF2, PTHR11610:SF2, 1 hit |
Pfami | View protein in Pfam PF00151, Lipase, 1 hit PF01477, PLAT, 1 hit |
PIRSFi | PIRSF000865, Lipoprotein_lipase_LIPH, 1 hit |
PRINTSi | PR00824, HEPLIPASE PR00821, TAGLIPASE |
SMARTi | View protein in SMART SM00308, LH2, 1 hit |
SUPFAMi | SSF49723, SSF49723, 1 hit SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00120, LIPASE_SER, 1 hit PS50095, PLAT, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
P07867-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGNHLQISVS LVLCIFIQSS ACGQGVGTEP FGRNLGATEE RKPLQKPEIR
60 70 80 90 100
FLLFKDESDR LGCQLRPQHP ETLQECGFNS SHPLVMIIHG WSVDGLLETW
110 120 130 140 150
IWKIVGALKS RQSQPVNVGL VDWISLAYQH YAIAVRNTRV VGQEVAALLL
160 170 180 190 200
WLEESMKFSR SKVHLIGYSL GAHVSGFAGS SMGGKRKIGR ITGLDPAGPM
210 220 230 240 250
FEGTSPNERL SPDDANFVDA IHTFTREHMG LSVGIKQPIA HYDFYPNGGS
260 270 280 290 300
FQPGCHFLEL YKHIAEHGLN AITQTINCAH ERSVHLFIDS LQHSNLQNTG
310 320 330 340 350
FQCSNMDSFS QGLCLNCKKG RCNSLGYDIR RIGHVKSKTL FLITRAQSPF
360 370 380 390 400
KVYHYQFKIQ FINQMEKPME PTFTMTLLGT KEEIKKIPIT LGEGITSNKT
410 420 430 440 450
YSLLITLNKD IGELIMLKFK WENSAVWANV WNTVQTIMLW DTEPHYAGLI
460 470 480 490
VKTIWVKAGE TQQRMTFCPD NVDDLQLHPT QEKVFVKCDL KSKD
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0G2K6S7 | A0A0G2K6S7_RAT | Hepatic triacylglycerol lipase | Lipc | 510 | Annotation score: | ||
Q5M895 | Q5M895_RAT | Hepatic triacylglycerol lipase | Lipc rCG_56713 | 494 | Annotation score: | ||
A0A0G2JY79 | A0A0G2JY79_RAT | Hepatic triacylglycerol lipase | Lipc | 492 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 277 | N → K in AAA41335 (PubMed:3470738).Curated | 1 | |
Sequence conflicti | 302 | Q → H in AAA41335 (PubMed:3470738).Curated | 1 | |
Sequence conflicti | 308 | S → T in AAA41335 (PubMed:3470738).Curated | 1 | |
Sequence conflicti | 335 | V → A in AAA41335 (PubMed:3470738).Curated | 1 | |
Sequence conflicti | 369 | M → I in AAA41335 (PubMed:3470738).Curated | 1 | |
Sequence conflicti | 408 | N → D in AAA41335 (PubMed:3470738).Curated | 1 | |
Sequence conflicti | 451 | V → L in AAA41335 (PubMed:3470738).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X17366 mRNA Translation: CAA35241.1 X17367 Genomic DNA Translation: CAA35242.1 M16235 mRNA Translation: AAA41335.1 |
PIRi | A27442 |
Genome annotation databases
UCSCi | RGD:3009, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X17366 mRNA Translation: CAA35241.1 X17367 Genomic DNA Translation: CAA35242.1 M16235 mRNA Translation: AAA41335.1 |
PIRi | A27442 |
3D structure databases
SMRi | P07867 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | P07867, 1 interactor |
STRINGi | 10116.ENSRNOP00000047403 |
Chemistry databases
SwissLipidsi | SLP:000000571 |
Protein family/group databases
ESTHERi | ratno-1hlip, Hepatic_Lipase |
PTM databases
GlyGeni | P07867, 2 sites |
Proteomic databases
PaxDbi | P07867 |
PeptideAtlasi | P07867 |
Genome annotation databases
UCSCi | RGD:3009, rat |
Organism-specific databases
RGDi | 3009, Lipc |
Phylogenomic databases
eggNOGi | ENOG502QVTG, Eukaryota |
InParanoidi | P07867 |
PhylomeDBi | P07867 |
Enzyme and pathway databases
Reactomei | R-RNO-8963889, Assembly of active LPL and LIPC lipase complexes R-RNO-8964026, Chylomicron clearance |
Miscellaneous databases
PROi | PR:P07867 |
Family and domain databases
CDDi | cd00707, Pancreat_lipase_like, 1 hit |
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR013818, Lipase/vitellogenin IPR002333, Lipase_hep IPR016272, Lipase_LIPH IPR033906, Lipase_N IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR000734, TAG_lipase |
PANTHERi | PTHR11610, PTHR11610, 1 hit PTHR11610:SF2, PTHR11610:SF2, 1 hit |
Pfami | View protein in Pfam PF00151, Lipase, 1 hit PF01477, PLAT, 1 hit |
PIRSFi | PIRSF000865, Lipoprotein_lipase_LIPH, 1 hit |
PRINTSi | PR00824, HEPLIPASE PR00821, TAGLIPASE |
SMARTi | View protein in SMART SM00308, LH2, 1 hit |
SUPFAMi | SSF49723, SSF49723, 1 hit SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00120, LIPASE_SER, 1 hit PS50095, PLAT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LIPC_RAT | |
Accessioni | P07867Primary (citable) accession number: P07867 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | August 1, 1990 | |
Last modified: | December 2, 2020 | |
This is version 153 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families