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    Liph lipase H [ Rattus norvegicus (Norway rat) ]

    Gene ID: 681694, updated on 27-Nov-2024

    Summary

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    Official Symbol
    Liphprovided by RGD
    Official Full Name
    lipase Hprovided by RGD
    Primary source
    RGD:1592849
    See related
    EnsemblRapid:ENSRNOG00000047894 AllianceGenome:RGD:1592849
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Rattus norvegicus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
    Summary
    Predicted to enable heparin binding activity and phospholipase activity. Predicted to be involved in lipid catabolic process. Predicted to be located in plasma membrane. Predicted to be active in extracellular space. Human ortholog(s) of this gene implicated in hypotrichosis 7. Orthologous to human LIPH (lipase H). [provided by Alliance of Genome Resources, Nov 2024]
    Expression
    Biased expression in Lung (RPKM 40.0), Kidney (RPKM 27.8) and 3 other tissues See more
    Orthologs
    human mouse all
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    Genomic context

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    See Liph in Genome Data Viewer
    Location:
    11q23
    Exon count:
    12
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCr8 (GCF_036323735.1) 11 NC_086029.1 (92536724..92586117)
    RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 11 NC_051346.1 (79032229..79081625)
    106 previous assembly Rnor_6.0 (GCF_000001895.5) 11 NC_005110.4 (82680167..82732145)

    Chromosome 11 - NC_086029.1Genomic Context describing neighboring genes Neighboring gene insulin-like growth factor 2 mRNA binding protein 2 Neighboring gene uncharacterized LOC134481028 Neighboring gene SUMO specific peptidase 2 Neighboring gene transmembrane protein 41a Neighboring gene mitogen-activated protein kinase kinase kinase 13 Neighboring gene small ubiquitin-related modifier 2-like

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
    • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
    • BioProject: PRJNA238328
    • Publication: PMID 24510058
    • Analysis date: Mon Jun 6 17:44:12 2016

    Bibliography

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    Related articles in PubMed

    1. Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta. Hiramatsu T, et al. J Biol Chem, 2003 Dec 5. PMID 12963729
    2. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, et al. Genome Res, 2004 Oct. PMID 15489334, Free PMC Article
    3. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, et al. Proc Natl Acad Sci U S A, 2002 Dec 24. PMID 12477932, Free PMC Article
    4. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, et al. Brief Bioinform, 2011 Sep. PMID 21873635, Free PMC Article

    GeneRIFs: Gene References Into Functions

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RGD

    Function Evidence Code Pubs
    enables heparin binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables heparin binding ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables lipase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phospholipase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables phospholipase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phospholipase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    Process Evidence Code Pubs
    involved_in lipid catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in lipid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipid catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in lipid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in extracellular region IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in extracellular space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in extracellular space IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in extracellular space ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane ISO
    Inferred from Sequence Orthology
    more info
    		  

    General protein information

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    Preferred Names
    lipase member H
    Names
    lipase, member H
    NP_001037744.1
    XP_038944552.1
    XP_038944553.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001044279.1 → NP_001037744.1  lipase member H precursor

      See identical proteins and their annotated locations for NP_001037744.1

      Status: PROVISIONAL

      Source sequence(s)
      BC107932
      UniProtKB/Swiss-Prot
      Q32PY2, Q6P6S8
      UniProtKB/TrEMBL
      A0A0G2JUG3
      Related
      ENSRNOP00000080503.1, ENSRNOT00000094527.2
      Conserved Domains (1) summary
      cd00707
      Location:41 → 310
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...

    RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCr8

    Genomic

    1. NC_086029.1 Reference GRCr8

      Range
      92536724..92586117
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_039088625.2 → XP_038944553.1  lipase member H isoform X2

      UniProtKB/TrEMBL
      A0A8I6G4M3
      Conserved Domains (1) summary
      cd00707
      Location:78 → 347
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...

    2. XM_039088624.2 → XP_038944552.1  lipase member H isoform X1

      UniProtKB/TrEMBL
      A0A8I6G4M3
      Related
      ENSRNOP00000111170.1, ENSRNOT00000149579.1
      Conserved Domains (1) summary
      cd00707
      Location:78 → 347
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q32PY2.1 GenPept UniProtKB/Swiss-Prot:Q32PY2

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
    Molecular Biology Databases
    Research Materials
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