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 170 (02 Jun 2021)
Sequence version 2 (24 Jan 2006)
Previous versions | rss
Add a publicationFeedback
Protein

Hormone-sensitive lipase

Gene

Lipe

Organism
Mus musculus (Mouse)
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

Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (PubMed:15550674, PubMed:20625037, PubMed:21454566, PubMed:23066022, PubMed:23291629).

Shows a preferential hydrolysis of DAGs over TAGs and MAGs and of the fatty acid (FA) esters at the sn-1 and sn-2 positions of the glycerol backbone in TAGs (By similarity).

Preferentially hydrolyzes FA esters at the sn-3 position of the glycerol backbone in DAGs (PubMed:23066022).

Catalyzes the hydrolysis of 2-arachidonoylglycerol, an endocannabinoid and of 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (PubMed:20625037, PubMed:21454566).

In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production (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 '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=0.25 µM for 1-(9Z-octadecenoyl)-glycerol1 Publication
  2. KM=0.26 µM for 2-(9Z-octadecenoyl)-glycerol1 Publication
  3. KM=0.27 µM for 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: triacylglycerol degradation

    This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway triacylglycerol degradation and in Glycerolipid metabolism.

    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 sitei423PROSITE-ProRule annotationBy similarity1
    Active sitei694By similarity1
    Active sitei724By similarity1

    <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 functionHydrolase
    Biological processCholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.1.79, 3474

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00256

    Protein family/group databases

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

    More...
    ESTHERi
    mouse-hslip, Hormone-sensitive_lipase_like

    MEROPS protease database

    More...
    MEROPSi
    S09.993

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000313
    SLP:000000314

    <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:
    Hormone-sensitive lipase (EC:3.1.1.793 Publications)
    Short name:
    HSL
    Alternative name(s):
    Monoacylglycerol lipase LIPE (EC:3.1.1.231 Publication)
    Retinyl ester hydrolase1 Publication
    Short name:
    REH
    <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:Lipe
    <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>OrganismiMus musculus (Mouse)
    <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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    <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
    • UP000000589 <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: Chromosome 7

    Organism-specific databases

    Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

    More...
    MGIi
    MGI:96790, Lipe

    <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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Lipid droplet, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Total acylglycerol levels are unaltered whereas diacylglycerol concentrations are drastically increased in white adipose tissue of knockout mice when compared to wild-type littermates.1 Publication

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5935

    <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 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_00000715481 – 759Hormone-sensitive lipaseAdd BLAST759

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei557PhosphoserineBy similarity1
    Modified residuei559Phosphoserine; by AMPKCombined sources1 Publication1
    Modified residuei574PhosphothreonineCombined sources1
    Modified residuei597PhosphoserineBy similarity1
    Modified residuei618PhosphoserineBy similarity1
    Modified residuei650PhosphoserineBy similarity1
    Modified residuei651PhosphoserineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylation by AMPK reduces its translocation towards the lipid droplets.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P54310

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P54310

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

    More...
    PaxDbi
    P54310

    PeptideAtlas

    More...
    PeptideAtlasi
    P54310

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P54310

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    292097 [P54310-1]
    292098 [P54310-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P54310

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P54310

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000003123, Expressed in white adipose tissue and 176 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P54310, MM

    <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

    Monomer and homodimer (By similarity).

    Interacts with CAVIN1 in the adipocyte cytoplasm (By similarity).

    Interacts with PLIN5 (PubMed:19717842).

    By similarity1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000003207

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P54310, protein

    <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
    P54310

    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

    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>Regioni534 – 553DisorderedSequence analysisAdd BLAST20
    Regioni583 – 604DisorderedSequence analysisAdd BLAST22

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi349 – 351Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity3

    <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 'GDXG' lipolytic enzyme family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG4388, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00730000111056

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_010288_1_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P54310

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF314423

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1820, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058, AB_hydrolase
    IPR013094, AB_hydrolase_3
    IPR010468, HSL_N
    IPR002168, Lipase_GDXG_HIS_AS
    IPR033140, Lipase_GDXG_put_SER_AS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07859, Abhydrolase_3, 2 hits
    PF06350, HSL_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53474, SSF53474, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01173, LIPASE_GDXG_HIS, 1 hit
    PS01174, LIPASE_GDXG_SER, 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>Sequences (2+)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.

    This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P54310-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MDLRTMTQSL VTLAEDNMAF FSSQGPGETA RRLSNVFAGV REQALGLEPT
    60 70 80 90 100
    LGQLLGVAHH FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRKSI
    110 120 130 140 150
    FFRASHNLAE LEAYLAALTQ LRAMAYYAQR LLTINRPGVL FFEGDEGLTA
    160 170 180 190 200
    DFLQEYVTLH KGCFYGRCLG FQFTPAIRPF LQTLSIGLVS FGEHYKRNET
    210 220 230 240 250
    GLSVTASSLF TGGRFAIDPE LRGAEFERII QNLDVHFWKA FWNITEIEVL
    260 270 280 290 300
    SSLANMASTT VRVSRLLSLP PEAFEMPLTS DPRLTVTISP PLAHTGPAPV
    310 320 330 340 350
    LARLISYDLR EGQDSKVLNS LAKSEGPRLE LRPRPHQAPR SRALVVHIHG
    360 370 380 390 400
    GGFVAQTSKS HEPYLKNWAQ ELGVPIFSID YSLAPEAPFP RALEECFFAY
    410 420 430 440 450
    CWAVKHCDLL GSTGERICLA GDSAGGNLCI TVSLRAAAYG VRVPDGIMAA
    460 470 480 490 500
    YPVTTLQSSA SPSRLLSLMD PLLPLSVLSK CVSAYSGTEA EDHFDSDQKA
    510 520 530 540 550
    LGVMGLVQRD TSLFLRDLRL GASSWLNSFL ELSGRKPQKT TSPTAESVRP
    560 570 580 590 600
    TESMRRSVSE AALAQPEGLL GTDTLKKLTI KDLSNSEPSD SPEMSQSMET
    610 620 630 640 650
    LGPSTPSDVN FFLRPGNSQE EAEAKDEVRP MDGVPRVRAA FPEGFHPRRS
    660 670 680 690 700
    SQGVLHMPLY TSPIVKNPFM SPLLAPDSML KTLPPVHLVA CALDPMLDDS
    710 720 730 740 750
    VMFARRLRDL GQPVTLKVVE DLPHGFLSLA ALCRETRQAT EFCVQRIRLI

    LTPPAAPLN
    Length:759
    Mass (Da):83,348
    Last modified:January 24, 2006 - 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:i3419AF52F6C85FF4
    GO
    Isoform 2 (identifier: P54310-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEPAVESAPVGAQASKQGKEGSKNRSRRRWRKGKIKASAFSHSM

    Show »
    Length:802
    Mass (Da):88,027
    Checksum:i3D0D4870E898AE5B
    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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E9Q4M2E9Q4M2_MOUSE
    Hormone-sensitive lipase
    Lipe
    1,072Annotation 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>
    A0A0U1RNR0A0A0U1RNR0_MOUSE
    Hormone-sensitive lipase
    Lipe
    180Annotation 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>
    Q9D4C4Q9D4C4_MOUSE
    Hormone-sensitive lipase
    Lipe
    334Annotation score:

    Annotation score:1 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>
    A0A0U1RPJ0A0A0U1RPJ0_MOUSE
    Hormone-sensitive lipase
    Lipe
    24Annotation score:

    Annotation score:1 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 conflicti113A → T in BAE41414 (PubMed:16141072).Curated1
    Sequence conflicti311E → D in BAE41414 (PubMed:16141072).Curated1
    Sequence conflicti330 – 331EL → DV in AAC52163 (PubMed:7698747).Curated2
    Sequence conflicti530L → P in AAC52163 (PubMed:7698747).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0533351M → MEPAVESAPVGAQASKQGKE GSKNRSRRRWRKGKIKASAF SHSM in isoform 2. 1 Publication1

    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
    U08188 mRNA Translation: AAC52163.1
    AF179427 Genomic DNA Translation: AAC53069.1
    AC162443 Genomic DNA No translation available.
    AC169209 Genomic DNA No translation available.
    AK029984 mRNA Translation: BAC26716.1
    AK169858 mRNA Translation: BAE41414.1
    BC021642 mRNA Translation: AAH21642.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS20981.1 [P54310-2]
    CCDS20982.1 [P54310-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I49007

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001034596.1, NM_001039507.2 [P54310-1]
    NP_034849.2, NM_010719.5 [P54310-2]
    XP_006539634.1, XM_006539571.2
    XP_006539635.1, XM_006539572.3 [P54310-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000003207; ENSMUSP00000003207; ENSMUSG00000003123 [P54310-2]
    ENSMUST00000054301; ENSMUSP00000050935; ENSMUSG00000003123 [P54310-1]
    ENSMUST00000206861; ENSMUSP00000145665; ENSMUSG00000003123 [P54310-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    16890

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:16890

    UCSC genome browser

    More...
    UCSCi
    uc009fsp.1, mouse [P54310-1]
    uc009fsr.1, mouse [P54310-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    U08188 mRNA Translation: AAC52163.1
    AF179427 Genomic DNA Translation: AAC53069.1
    AC162443 Genomic DNA No translation available.
    AC169209 Genomic DNA No translation available.
    AK029984 mRNA Translation: BAC26716.1
    AK169858 mRNA Translation: BAE41414.1
    BC021642 mRNA Translation: AAH21642.1
    CCDSiCCDS20981.1 [P54310-2]
    CCDS20982.1 [P54310-1]
    PIRiI49007
    RefSeqiNP_001034596.1, NM_001039507.2 [P54310-1]
    NP_034849.2, NM_010719.5 [P54310-2]
    XP_006539634.1, XM_006539571.2
    XP_006539635.1, XM_006539572.3 [P54310-1]

    3D structure databases

    SMRiP54310
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000003207

    Chemistry databases

    ChEMBLiCHEMBL5935
    SwissLipidsiSLP:000000313
    SLP:000000314

    Protein family/group databases

    ESTHERimouse-hslip, Hormone-sensitive_lipase_like
    MEROPSiS09.993

    PTM databases

    iPTMnetiP54310
    PhosphoSitePlusiP54310

    Proteomic databases

    jPOSTiP54310
    MaxQBiP54310
    PaxDbiP54310
    PeptideAtlasiP54310
    PRIDEiP54310
    ProteomicsDBi292097 [P54310-1]
    292098 [P54310-2]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    4327, 483 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    16890

    Genome annotation databases

    EnsembliENSMUST00000003207; ENSMUSP00000003207; ENSMUSG00000003123 [P54310-2]
    ENSMUST00000054301; ENSMUSP00000050935; ENSMUSG00000003123 [P54310-1]
    ENSMUST00000206861; ENSMUSP00000145665; ENSMUSG00000003123 [P54310-1]
    GeneIDi16890
    KEGGimmu:16890
    UCSCiuc009fsp.1, mouse [P54310-1]
    uc009fsr.1, mouse [P54310-2]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    3991
    MGIiMGI:96790, Lipe

    Phylogenomic databases

    eggNOGiKOG4388, Eukaryota
    GeneTreeiENSGT00730000111056
    HOGENOMiCLU_010288_1_0_1
    InParanoidiP54310
    TreeFamiTF314423

    Enzyme and pathway databases

    UniPathwayiUPA00256
    BRENDAi3.1.1.79, 3474

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    16890, 2 hits in 53 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    Lipe, mouse

    Protein Ontology

    More...
    PROi
    PR:P54310
    RNActiP54310, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000003123, Expressed in white adipose tissue and 176 other tissues
    GenevisibleiP54310, MM

    Family and domain databases

    Gene3Di3.40.50.1820, 2 hits
    InterProiView protein in InterPro
    IPR029058, AB_hydrolase
    IPR013094, AB_hydrolase_3
    IPR010468, HSL_N
    IPR002168, Lipase_GDXG_HIS_AS
    IPR033140, Lipase_GDXG_put_SER_AS
    PfamiView protein in Pfam
    PF07859, Abhydrolase_3, 2 hits
    PF06350, HSL_N, 1 hit
    SUPFAMiSSF53474, SSF53474, 1 hit
    PROSITEiView protein in PROSITE
    PS01173, LIPASE_GDXG_HIS, 1 hit
    PS01174, LIPASE_GDXG_SER, 1 hit

    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 nameiLIPS_MOUSE
    <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: P54310
    Secondary accession number(s): P97866
    , Q3TE34, Q6GU16, Q8CDI9
    <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: October 1, 1996
    Last sequence update: January 24, 2006
    Last modified: June 2, 2021
    This is version 170 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. 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