liph lipase, member H [Xenopus tropicalis (tropical clawed frog)] - Gene

Summary

Official Symbol: liphprovided by Xenbase
Official Full Name: lipase, member Hprovided by Xenbase
Primary source: Xenbase:XB-GENE-5847665
See related: Ensembl:ENSXETG00000005849 AllianceGenome:Xenbase:XB-GENE-5847665
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Xenopus tropicalis
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana
Also known as: lipi; lpdl; lpdlr; pla1b; pred5; liph-a; liph-b; mpa-pla1
Summary: Predicted to enable phospholipase activity. Predicted to be involved in lipid catabolic process. Predicted to act upstream of or within lipid metabolic process. Predicted to be located in extracellular region and 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]
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: chromosome: 2

Exon count:: 10

Annotation release	Status	Assembly	Chr	Location
104	current	UCB_Xtro_10.0 (GCF_000004195.4)	2	NC_030678.2 (26553049..26572007)
103	previous assembly	Xenopus_tropicalis_v9.1 (GCF_000004195.3)	2	NC_030678.1 (22383143..22401069)

Chromosome 2 - NC_030678.2 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Submit: New GeneRIF Correction

General gene information

Go to the top of the page Help

Gene Ontology Provided by Xenbase

Function	Evidence Code	Pubs
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables lipase activity	IEA Inferred from Electronic Annotation more info
enables phospholipase activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in lipid catabolic process	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within lipid catabolic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within 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 plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: lipase member H

Names: lipase I; lipase, member I

NP_001011098.1

EC 2.7.11.30

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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)

NM_001011098.1 → NP_001011098.1 lipase member H precursor

See identical proteins and their annotated locations for NP_001011098.1

Status: PROVISIONAL

Source sequence(s)

BC084493

UniProtKB/Swiss-Prot

Q5XGE9

UniProtKB/TrEMBL

F7BXT5

Related

ENSXETP00000012870.4, ENSXETT00000012870.5

Conserved Domains (1) summary

cd00707
Location:45 → 312

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 ...