ced-12 Cell death abnormality protein 12;ELMO domain-containing protein [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: ced-12
Official Full Name: Cell death abnormality protein 12;ELMO domain-containing protein
Primary source: WormBase:WBGene00000426
Locus tag: CELE_Y106G6E.5
See related: AllianceGenome:WB:WBGene00000426
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: Enables phosphatidylinositol phosphate binding activity; proline-rich region binding activity; and small GTPase binding activity. Involved in several processes, including cytoskeleton organization; engulfment of apoptotic cell; and left/right axis specification. Located in cytoplasm and plasma membrane. Part of guanyl-nucleotide exchange factor complex. Is expressed in intestine; nervous system; reproductive system; and tail. Orthologous to human ELMO1 (engulfment and cell motility 1); ELMO2 (engulfment and cell motility 2); and ELMO3 (engulfment and cell motility 3). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See ced-12 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 8

Sequence:: Chromosome: I; NC_003279.8 (10222881..10227009, 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?

CED-5/CED-12 (DOCK/ELMO) can promote and inhibit F-actin formation via distinct motifs that may target different GTPases.
Title: CED-5/CED-12 (DOCK/ELMO) can promote and inhibit F-actin formation via distinct motifs that may target different GTPases.
Epistatic analyses place mtm-1 upstream of the ternary GEF complex, which consists of ced-2, ced-5 and ced-12, and parallel to mig-2.
Title: The phosphoinositide phosphatase MTM-1 regulates apoptotic cell corpse clearance through CED-5-CED-12 in C. elegans.
findings suggest that PSR-1 is likely an upstream receptor for the signaling pathway containing CED-2, CED-5, CED-10, and CED-12 proteins and plays an important role in recognizing phosphatidylserine during phagocytosis
Title: Cell corpse engulfment mediated by C. elegans phosphatidylserine receptor through CED-5 and CED-12.
Rac activation by the ELMO.Dock180 complex at discrete intracellular locations mediated by the N-terminal 330 amino acids of ELMO1 plays a role in cell migration
Title: Dock180 and ELMO1 proteins cooperate to promote evolutionarily conserved Rac-dependent cell migration.
the PH domain of ELMO binds the Dock180-Rac complex in trans and stabilizes Rac in the nucleotide-free transition state
Title: PH domain of ELMO functions in trans to regulate Rac activation via Dock180.

Submit: New GeneRIF Correction

Pathways from PubChem

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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

Y106G6E.5 (e-PCR)
- UniSTS:312974

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables SH3 domain binding	IEA Inferred from Electronic Annotation more info
enables SH3 domain binding	TAS Traceable Author Statement more info	PubMed
enables enzyme binding	IPI Inferred from Physical Interaction more info	PubMed
contributes_to guanyl-nucleotide exchange factor activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables lipid binding	IEA Inferred from Electronic Annotation more info
enables phosphatidylinositol-3,4,5-trisphosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidylinositol-3,5-bisphosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidylinositol-4-phosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables proline-rich region binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	IPI Inferred from Physical Interaction more info	PubMed
enables small GTPase binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in actin cytoskeleton organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in actin filament organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in actin filament organization	IDA Inferred from Direct Assay more info	PubMed
involved_in apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in apoptotic process involved in development	IGI Inferred from Genetic Interaction more info	PubMed
involved_in apoptotic process involved in development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cell migration	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cell motility	IBA Inferred from Biological aspect of Ancestor more info
involved_in cytoskeletal rearrangement involved in phagocytosis, engulfment	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in engulfment of apoptotic cell	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in establishment of mitotic spindle orientation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in gonad morphogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in left/right axis specification	IGI Inferred from Genetic Interaction more info	PubMed
involved_in phagocytosis	IEA Inferred from Electronic Annotation more info
involved_in phagocytosis, engulfment	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of distal tip cell migration	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of engulfment of apoptotic cell	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of cell migration	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
part_of guanyl-nucleotide exchange factor complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Cell death abnormality protein 12;ELMO domain-containing protein

NP_001293276.1

Confirmed by transcript evidence

NP_492693.1

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

10222881..10227009 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_060292.7 → NP_492693.1 Cell death abnormality protein 12 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_492693.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q8STE5

Conserved Domains (3) summary

pfam04727
Location:370 → 465

ELMO_CED12; ELMO/CED-12 family

pfam11841
Location:156 → 304

DUF3361; Domain of unknown function (DUF3361)

cl17171
Location:544 → 679

PH-like; Pleckstrin homology-like domain
NM_001306347.3 → NP_001293276.1 ELMO domain-containing protein [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_001293276.1

Status: REVIEWED

UniProtKB/TrEMBL

V5Z1T2

Conserved Domains (3) summary

pfam04727
Location:377 → 472

ELMO_CED12; ELMO/CED-12 family

pfam11841
Location:163 → 311

DUF3361; Domain of unknown function (DUF3361)

pfam16457
Location:551 → 686

PH_12; Pleckstrin homology domain