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Plb1 phospholipase B1 [ Cricetulus griseus (Chinese hamster) ]

Gene ID: 100761810, updated on 8-Mar-2024

Summary

Gene symbol
Plb1
Gene description
phospholipase B1
Locus tag
I79_002010
See related
Ensembl:ENSCGRG00015024870
Gene type
protein coding
RefSeq status
MODEL
Organism
Cricetulus griseus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Cricetidae; Cricetinae; Cricetulus
Orthologs
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Genomic context

Location:
chromosome: 7
Exon count:
51
Annotation release Status Assembly Chr Location
104 current CriGri_1.0 (GCF_000223135.1) Unplaced Scaffold NW_003613628.1 (2087953..2182145, complement)
104 current CriGri-PICRH-1.0 (GCF_003668045.3) 7 NC_048600.1 (12112958..12206867, complement)

NW_003613628.1Genomic Context describing neighboring genes Neighboring gene tRNA methyltransferase 61B Neighboring gene speedy/RINGO cell cycle regulator family member A Neighboring gene host cell factor C1 regulator 1-like Neighboring gene protein phosphatase 1 catalytic subunit beta Neighboring gene uncharacterized LOC118239166 Neighboring gene partner of Y14 and mago-like

Genomic regions, transcripts, and products

General gene information

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables lysophospholipase activity IEA
Inferred from Electronic Annotation
more info
PubMed 
enables phospholipase A2 activity IEA
Inferred from Electronic Annotation
more info
PubMed 
enables retinyl-palmitate esterase activity IEA
Inferred from Electronic Annotation
more info
PubMed 
Process Evidence Code Pubs
involved_in phospholipid metabolic process IEA
Inferred from Electronic Annotation
more info
PubMed 
Component Evidence Code Pubs
located_in brush border membrane IEA
Inferred from Electronic Annotation
more info
PubMed 

General protein information

Preferred Names
phospholipase B1, membrane-associated

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Cricetulus griseus Annotation Release 104 details...Open this link in a new tab

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

Reference CriGri_1.0 Primary Assembly

Genomic

  1. NW_003613628.1 Reference CriGri_1.0 Primary Assembly

    Range
    2087953..2182145 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_027442777.2XP_027298578.2  phospholipase B1, membrane-associated

    UniProtKB/TrEMBL
    A0A8C2LHJ2, A0A9J7G9Q8
    Conserved Domains (2) summary
    cd01824
    Location:237531
    Phospholipase_B_like; Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and ...
    cl01053
    Location:2172
    SGNH_hydrolase; or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical ...

Alternate CriGri-PICRH-1.0

Genomic

  1. NC_048600.1 Alternate CriGri-PICRH-1.0

    Range
    12112958..12206867 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_027424423.2XP_027280224.2  phospholipase B1, membrane-associated

    UniProtKB/TrEMBL
    A0A8C2LHJ2, A0A9J7G9Q8
    Related
    ENSCGRP00015033159.2, ENSCGRT00015040442.2
    Conserved Domains (2) summary
    cd01824
    Location:237531
    Phospholipase_B_like; Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and ...
    cl01053
    Location:2172
    SGNH_hydrolase; or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical ...