Cplx1 complexin 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Cplx1provided by RGD
Official Full Name: complexin 1provided by RGD
Primary source: RGD:70944
See related: EnsemblRapid:ENSRNOG00000090522 AllianceGenome:RGD:70944
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables syntaxin-1 binding activity. Involved in synaptic vesicle exocytosis. Located in dendrite; neuronal cell body; and synapse. Part of synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex. Is active in postsynapse and presynapse. Human ortholog(s) of this gene implicated in developmental and epileptic encephalopathy 63. Orthologous to human CPLX1 (complexin 1). [provided by Alliance of Genome Resources, Oct 2024]
Expression: Restricted expression toward (RPKM 725.8) See more
Orthologs: human mouse all
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Genomic context

Location:: 14p22

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	14	NC_086032.1 (1329073..1360781)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	14	NC_051349.1 (1184677..1216392)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	14	NC_005113.4 (2194895..2226610)

Chromosome 14 - NC_086032.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages 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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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Involvement of miR-135a-5p Downregulation in Acute and Chronic Stress Response in the Prefrontal Cortex of Rats.
Title: Involvement of miR-135a-5p Downregulation in Acute and Chronic Stress Response in the Prefrontal Cortex of Rats.
Complexin I knockout rats exhibit a complex neurobehavioral phenotype including profound ataxia and marked deficits in lifespan.
Title: Complexin I knockout rats exhibit a complex neurobehavioral phenotype including profound ataxia and marked deficits in lifespan.
complexin-1 competes with alphaSNAP binding to the SNARE complex.
Title: NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin.
actively drives SNARE complexes into linker-open conformation
Title: Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension.
Results suggest that the C-terminal domain of Cplx1 plays a role in preferential membrane localization of Cpx to synaptic vesicles and find it as an important regulator for synaptic vesicle fusion through promoting Ca2+ in conjunction with SNAREs and synaptotagmins.
Title: C-terminal domain of mammalian complexin-1 localizes to highly curved membranes.
Munc18a does not alter synaptic fusion rates mediated by neuronal SNAREs, synaptotagmin-1, and complexin-1.
Title: Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexin.
Complexin-1 inhibits spontaneous release and synchronizes Ca2+-triggered synaptic vesicle fusion by distinct mechanisms.
Title: Complexin inhibits spontaneous release and synchronizes Ca2+-triggered synaptic vesicle fusion by distinct mechanisms.
Data show direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1.
Title: Direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1.
Results indicate that distinct functional domains of copmplexin I differentially regulate synaptic exocytosis, and that CplxI carries out a crucial role in fine-tuning Ca2+-triggered fast neurotransmitter release.
Title: Distinct domains of complexin I differentially regulate neurotransmitter release.
Transient increases in the levels of complexin I and complexin II proteins were detected in the injured cerebral cortex 6 h following TBI. This increase was followed by a decrease of complexin I in the injured cortex and hippocampus.
Title: Early, transient increase in complexin I and complexin II in the cerebral cortex following traumatic brain injury is attenuated by N-acetylcysteine.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables SNARE binding	IBA Inferred from Biological aspect of Ancestor more info
enables SNARE binding	IDA Inferred from Direct Assay more info	PubMed
enables neurotransmitter transmembrane transporter activity	ISO Inferred from Sequence Orthology more info
enables syntaxin-1 binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in insulin secretion	ISO Inferred from Sequence Orthology more info
involved_in modulation of chemical synaptic transmission	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of exocytic insertion of neurotransmitter receptor to postsynaptic membrane	ISO Inferred from Sequence Orthology more info
involved_in regulation of synaptic vesicle fusion to presynaptic active zone membrane	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of synaptic vesicle fusion to presynaptic active zone membrane	ISO Inferred from Sequence Orthology more info
involved_in synaptic vesicle exocytosis	IBA Inferred from Biological aspect of Ancestor more info
involved_in synaptic vesicle exocytosis	IDA Inferred from Direct Assay more info	PubMed
involved_in synaptic vesicle exocytosis	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
part_of SNARE complex	IBA Inferred from Biological aspect of Ancestor more info
part_of SNARE complex	ISO Inferred from Sequence Orthology more info
is_active_in Schaffer collateral - CA1 synapse	ISO Inferred from Sequence Orthology more info
is_active_in calyx of Held	ISO Inferred from Sequence Orthology more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in dendrite	IDA Inferred from Direct Assay more info	PubMed
is_active_in glutamatergic synapse	ISO Inferred from Sequence Orthology more info
located_in neuronal cell body	IDA Inferred from Direct Assay more info	PubMed
located_in perikaryon	IEA Inferred from Electronic Annotation more info
is_active_in postsynapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in postsynapse	ISO Inferred from Sequence Orthology more info
is_active_in presynapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in presynapse	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed
located_in synapse	IDA Inferred from Direct Assay more info	PubMed
part_of synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex	IDA Inferred from Direct Assay more info	PubMed
located_in terminal bouton	HDA more info	PubMed
is_active_in terminal bouton	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: complexin-1

Names: CPX I; complexin I; synaphin-2

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.