lrk-1 Leucine-rich repeat serine/threonine-protein kinase 1 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: lrk-1
Official Full Name: Leucine-rich repeat serine/threonine-protein kinase 1
Primary source: WormBase:WBGene00003068
Locus tag: CELE_T27C10.6
See related: AllianceGenome:WB:WBGene00003068
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable metal ion binding activity; protein kinase activity; and purine ribonucleoside triphosphate binding activity. Involved in several processes, including axon extension involved in axon guidance; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; and synaptic vesicle transport. Located in Golgi apparatus and neuronal cell body. Is expressed in several structures, including hermaphrodite distal tip cell; intestine; neurons; pharynx; and vulva. Used to study Parkinson's disease. Human ortholog(s) of this gene implicated in osteosclerotic metaphyseal dysplasia. Orthologous to human LRRK1 (leucine rich repeat kinase 1). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See lrk-1 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 20

Sequence:: Chromosome: I; NC_003279.8 (10879769..10894237, complement)

Chromosome I - NC_003279.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003279.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

UNC-16 interacts with LRK-1 and WDFY-3 to regulate the termination of axon growth.
Title: UNC-16 interacts with LRK-1 and WDFY-3 to regulate the termination of axon growth.
LRRK2 functions together with a second Parkinson's disease-associated gene, RAB7L1, within an evolutionarily conserved genetic module in diverse cellular contexts.
Title: LRRK2 and RAB7L1 coordinately regulate axonal morphology and lysosome integrity in diverse cellular contexts.
Study investigated the role of UNC-23 and HSP-1 on LRK-1 function in C. elegans; results suggest that the UNC-23-HSP-1 chaperone complex regulates LRK-1 localization to the Golgi apparatus and consequently determines the polarized sorting of synaptic vesicle proteins to the axons.
Title: Chaperone complex BAG2-HSC70 regulates localization of Caenorhabditis elegans leucine-rich repeat kinase LRK-1 to the Golgi.
Lack of Grx1 homolog exacerbates LRRK2-mediated dopaminergic neurodegeneration in Caenorhabditis elegans.
Title: Glutaredoxin deficiency exacerbates neurodegeneration in C. elegans models of Parkinson's disease.
Findings establish a critical functional link between LRRK2 and ER stress.
Title: Dysregulated LRRK2 signaling in response to endoplasmic reticulum stress leads to dopaminergic neuron degeneration in C. elegans.
Due to the similarity of the C. elegans proteins to human LRRK2 and PINK1, we suggest a common role of both factors in cellular functions including stress response and regulation of neurite outgrowth
Title: Caenorhabditits elegans LRK-1 and PINK-1 act antagonistically in stress response and neurite outgrowth.
LRRK2 can regulate the mitochondrial physiology of Caenorhabditis elegans, possibly via the worm lrk-1 pathway.
Title: Investigating convergent actions of genes linked to familial Parkinson's disease.
Study identified a novel protein kinase LRK-1, a C. elegans homolog of the familial Parkinsonism gene PARK8/LRRK2 that is required for polarized localization of synaptic vesicle proteins.
Title: LRK-1, a C. elegans PARK8-related kinase, regulates axonal-dendritic polarity of SV proteins.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

T27C10.3 (e-PCR)
- UniSTS:318545

T27C10.5 (e-PCR)
- UniSTS:312785

T27C10.6 (e-PCR)
- UniSTS:312786

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables GTP binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein kinase activity	IEA Inferred from Electronic Annotation more info
enables protein serine kinase activity	IEA Inferred from Electronic Annotation more info
enables protein serine/threonine kinase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in axon extension involved in axon guidance	IGI Inferred from Genetic Interaction more info	PubMed
involved_in negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein phosphorylation	IEA Inferred from Electronic Annotation more info
involved_in regulation of signal transduction	IEA Inferred from Electronic Annotation more info
involved_in response to endoplasmic reticulum stress	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to oxidative stress	IGI Inferred from Genetic Interaction more info	PubMed
involved_in synaptic vesicle transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in synaptic vesicle transport	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in neuronal cell body	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Leucine-rich repeat serine/threonine-protein kinase 1

NP_492839.4

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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

Reference assembly

Genomic

NC_003279.8 Reference assembly

Range

10879769..10894237 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_060438.8 → NP_492839.4 Leucine-rich repeat serine/threonine-protein kinase 1 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_492839.4

Status: REVIEWED

UniProtKB/Swiss-Prot

A3KFB1, Q9TZM3

Conserved Domains (10) summary

smart00220
Location:1698 → 1983

S_TKc; Serine/Threonine protein kinases, catalytic domain

cd00116
Location:512 → 639

LRR_RI; Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond ...

cd00204
Location:51 → 218

ANK; ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other ...

sd00033
Location:534 → 555

LRR_RI; leucine-rich repeat [structural motif]

pfam12796
Location:29 → 121

Ank_2; Ankyrin repeats (3 copies)

pfam13855
Location:554 → 615

LRR_8; Leucine rich repeat

pfam16095
Location:1239 → 1336

COR; C-terminal of Roc, COR, domain

sd00045
Location:56 → 88

ANK; ANK repeat [structural motif]

cl21453
Location:1699 → 1990

PKc_like; Protein Kinases, catalytic domain

cl21455
Location:977 → 1160

P-loop_NTPase; P-loop containing Nucleoside Triphosphate Hydrolases