Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 153 (02 Dec 2020)
Sequence version 2 (01 Aug 1990)
Previous versions | rss
Add a publicationFeedback
Protein

Hepatic triacylglycerol lipase

Gene

Lipc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phospholipase A1 and lysophospholipase activities are inhibited by annexin II.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.82 mM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol1 Publication
  2. KM=0.16 mM for 1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine1 Publication
  1. Vmax=144 µmol/min/mg enzyme with 1-oleoyl-sn-glycerol as substrate1 Publication
  2. Vmax=163 µmol/min/mg enzyme with 1,2-dioleoyl-sn-glycerol as substrate1 Publication
  3. Vmax=145 µmol/min/mg enzyme with 1,3-dioleoyl-sn-glycerol as substrate1 Publication
  4. Vmax=67 µmol/min/mg enzyme with phosphatidic acid as substrate1 Publication
  5. Vmax=50 µmol/min/mg enzyme with phosphatidylethanolamine as substrate1 Publication
  6. Vmax=4 µmol/min/mg enzyme with phosphatidylcholine as substrate1 Publication

pH dependencei

Optimum pH is 8-9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei169NucleophileBy similarity1
Active sitei195Charge relay systemPROSITE-ProRule annotation1
Active sitei280Charge relay systemPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-8963889, Assembly of active LPL and LIPC lipase complexes
R-RNO-8964026, Chylomicron clearance

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
ratno-1hlip, Hepatic_Lipase

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000571

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Hepatic triacylglycerol lipase (EC:3.1.1.34 Publications)
Short name:
HL
Short name:
Hepatic lipase
Alternative name(s):
Lipase member C
Lysophospholipase (EC:3.1.1.51 Publication)
Phospholipase A1 (EC:3.1.1.324 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Lipc
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3009, Lipc

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

HDL, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21By similarityAdd BLAST21
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001777122 – 494Hepatic triacylglycerol lipaseAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi398N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P07867

PeptideAtlas

More...
PeptideAtlasi
P07867

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P07867, 2 sites

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P07867, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000047403

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P07867

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini353 – 487PLATPROSITE-ProRule annotationAdd BLAST135

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni255 – 278Essential for determining substrate specificityBy similarityAdd BLAST24

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QVTG, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07867

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07867

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00707, Pancreat_lipase_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

More...
PANTHERi
PTHR11610, PTHR11610, 1 hit
PTHR11610:SF2, PTHR11610:SF2, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00151, Lipase, 1 hit
PF01477, PLAT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000865, Lipoprotein_lipase_LIPH, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00824, HEPLIPASE
PR00821, TAGLIPASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00308, LH2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49723, SSF49723, 1 hit
SSF53474, SSF53474, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00120, LIPASE_SER, 1 hit
PS50095, PLAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P07867-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:494
Mass (Da):55,623
Last modified:August 1, 1990 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2A9461B1F80845EA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K6S7A0A0G2K6S7_RAT
Hepatic triacylglycerol lipase
Lipc
510Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5M895Q5M895_RAT
Hepatic triacylglycerol lipase
Lipc rCG_56713
494Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2JY79A0A0G2JY79_RAT
Hepatic triacylglycerol lipase
Lipc
492Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti277N → K in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti302Q → H in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti308S → T in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti335V → A in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti369M → I in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti408N → D in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti451V → L in AAA41335 (PubMed:3470738).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X17366 mRNA Translation: CAA35241.1
X17367 Genomic DNA Translation: CAA35242.1
M16235 mRNA Translation: AAA41335.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A27442

Genome annotation databases

UCSC genome browser

More...
UCSCi
RGD:3009, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiA27442

3D structure databases

SMRiP07867
ModBaseiSearch...

Protein-protein interaction databases

IntActiP07867, 1 interactor
STRINGi10116.ENSRNOP00000047403

Chemistry databases

SwissLipidsiSLP:000000571

Protein family/group databases

ESTHERiratno-1hlip, Hepatic_Lipase

PTM databases

GlyGeniP07867, 2 sites

Proteomic databases

PaxDbiP07867
PeptideAtlasiP07867

Genome annotation databases

UCSCiRGD:3009, rat

Organism-specific databases

RGDi3009, Lipc

Phylogenomic databases

eggNOGiENOG502QVTG, Eukaryota
InParanoidiP07867
PhylomeDBiP07867

Enzyme and pathway databases

ReactomeiR-RNO-8963889, Assembly of active LPL and LIPC lipase complexes
R-RNO-8964026, Chylomicron clearance

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P07867

Family and domain databases

CDDicd00707, Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView 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
PANTHERiPTHR11610, PTHR11610, 1 hit
PTHR11610:SF2, PTHR11610:SF2, 1 hit
PfamiView protein in Pfam
PF00151, Lipase, 1 hit
PF01477, PLAT, 1 hit
PIRSFiPIRSF000865, Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00824, HEPLIPASE
PR00821, TAGLIPASE
SMARTiView protein in SMART
SM00308, LH2, 1 hit
SUPFAMiSSF49723, SSF49723, 1 hit
SSF53474, SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120, LIPASE_SER, 1 hit
PS50095, PLAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLIPC_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07867
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again