Git1 GIT ArfGAP 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Git1provided by RGD
Official Full Name: GIT ArfGAP 1provided by RGD
Primary source: RGD:69331
See related: EnsemblRapid:ENSRNOG00000061270 AllianceGenome:RGD:69331
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 several functions, including GTPase activator activity; enzyme binding activity; and scaffold protein binding activity. A structural constituent of postsynaptic specialization. Involved in several processes, including cellular response to epidermal growth factor stimulus; neurotransmitter receptor localization to postsynaptic specialization membrane; and regulation of signal transduction. Acts upstream of or within dendritic spine development and immunological synapse formation. Located in several cellular components, including excitatory synapse; growth cone; and inhibitory synapse. Is active in GABA-ergic synapse; glutamatergic synapse; and postsynapse. Human ortholog(s) of this gene implicated in attention deficit hyperactivity disorder. Orthologous to human GIT1 (GIT ArfGAP 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Testes (RPKM 490.5), Brain (RPKM 254.3) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 10q24

Exon count:: 21

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	10	NC_086028.1 (62840165..62854508)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	10	NC_051345.1 (62342082..62356379)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	10	NC_005109.4 (62656000..62664467, complement)

Chromosome 10 - NC_086028.1 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

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

beta-PIX cooperates with GIT1 to regulate endothelial nitric oxide synthase in sinusoidal endothelial cells.
Title: β-PIX cooperates with GIT1 to regulate endothelial nitric oxide synthase in sinusoidal endothelial cells.
Kinesin-1-dependent transport of the betaPIX/GIT complex in neuronal cells.
Title: Kinesin-1-dependent transport of the βPIX/GIT complex in neuronal cells.
Inhibition of micro RNA miR-122-5p prevents lipopolysaccharide-induced myocardial injury by inhibiting oxidative stress, inflammation and apoptosis via targeting GIT1.
Title: Inhibition of micro RNA miR-122-5p prevents lipopolysaccharide-induced myocardial injury by inhibiting oxidative stress, inflammation and apoptosis via targeting GIT1.
Exosomes derived from GIT1-overexpressing bone marrow mesenchymal stem cells promote traumatic spinal cord injury recovery in a rat model.
Title: Exosomes derived from GIT1-overexpressing bone marrow mesenchymal stem cells promote traumatic spinal cord injury recovery in a rat model.
Induced association of beta-PIX with GIT1 is essential for the stimulation of intestinal epithelial restitution by activating Rac1, and this signaling pathway is tightly regulated by cellular polyamines.
Title: β-PIX plays an important role in regulation of intestinal epithelial restitution by interacting with GIT1 and Rac1 after wounding.
Integrin-beta1 regulates chondrocyte proliferation and apoptosis through the upregulation of GIT1 expression
Title: Integrin-β1 regulates chondrocyte proliferation and apoptosis through the upregulation of GIT1 expression.
PDGF activates the GIT1PLCG1mediated ERK1/2 pathway to control chondrocyte proliferation.
Title: PDGF regulates chondrocyte proliferation through activation of the GIT1- and PLCγ1-mediated ERK1/2 signaling pathway.
Plateletderived growth factor inhibits osteoblast apoptosis through upregulating GIT1 expression.
Title: Platelet‑derived growth factor promotes osteoblast proliferation by activating G‑protein‑coupled receptor kinase interactor‑1.
GIT1-eNOS complex is formed and regulated. GIT1 was phosphorylated on tyrosine by Src.
Title: Endothelial nitric-oxide synthase (eNOS) is activated through G-protein-coupled receptor kinase-interacting protein 1 (GIT1) tyrosine phosphorylation and Src protein.
binding of GluN3A to GIT1 is regulated by synaptic activity, a response that might restrict the negative regulatory effects of GluN3A on actin signaling to inactive synapses.
Title: GluN3A expression restricts spine maturation via inhibition of GIT1/Rac1 signaling.

Submit: New GeneRIF Correction See all GeneRIFs (21)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH128287 (e-PCR)
- UniSTS:211595

GIT1_9564 (e-PCR)
- UniSTS:468439

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables GTPase activator activity	IBA Inferred from Biological aspect of Ancestor more info
enables GTPase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables GTPase activator activity	IEA Inferred from Electronic Annotation more info
enables gamma-tubulin binding	IEA Inferred from Electronic Annotation more info
enables gamma-tubulin binding	ISO Inferred from Sequence Orthology more info
enables gamma-tubulin binding	ISS Inferred from Sequence or Structural Similarity more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein phosphatase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein tyrosine kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	IEA Inferred from Electronic Annotation more info
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables scaffold protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables small GTPase binding	IBA Inferred from Biological aspect of Ancestor more info
enables small GTPase binding	IDA Inferred from Direct Assay more info	PubMed
enables structural constituent of postsynaptic specialization	IDA Inferred from Direct Assay more info	PubMed
enables structural constituent of postsynaptic specialization	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in brain development	IBA Inferred from Biological aspect of Ancestor more info
involved_in brain development	IEA Inferred from Electronic Annotation more info
involved_in brain development	ISO Inferred from Sequence Orthology more info
involved_in cell redox homeostasis	IEA Inferred from Electronic Annotation more info
involved_in cell redox homeostasis	ISO Inferred from Sequence Orthology more info
involved_in cell redox homeostasis	ISS Inferred from Sequence or Structural Similarity more info
involved_in cellular response to epidermal growth factor stimulus	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular response to lipopolysaccharide	IEA Inferred from Electronic Annotation more info
involved_in cellular response to lipopolysaccharide	ISO Inferred from Sequence Orthology more info
involved_in cellular response to lipopolysaccharide	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within dendritic spine development	IGI Inferred from Genetic Interaction more info	PubMed
involved_in ephrin receptor signaling pathway	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within ephrin receptor signaling pathway	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within immunological synapse formation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in intramembranous ossification	IEA Inferred from Electronic Annotation more info
involved_in intramembranous ossification	ISO Inferred from Sequence Orthology more info
involved_in intramembranous ossification	ISS Inferred from Sequence or Structural Similarity more info
involved_in locomotory behavior	IEA Inferred from Electronic Annotation more info
involved_in locomotory behavior	ISO Inferred from Sequence Orthology more info
involved_in maintenance of postsynaptic specialization structure	IEA Inferred from Electronic Annotation more info
involved_in motor learning	IEA Inferred from Electronic Annotation more info
involved_in motor learning	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of ARF protein signal transduction	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of glycolytic process	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of glycolytic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of glycolytic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of inflammatory response to wounding	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of inflammatory response to wounding	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of inflammatory response to wounding	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of interleukin-1 beta production	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of interleukin-1 beta production	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of interleukin-1 beta production	ISS Inferred from Sequence or Structural Similarity more info
involved_in neuron development	IEA Inferred from Electronic Annotation more info
involved_in neuron development	ISO Inferred from Sequence Orthology more info
involved_in neurotransmitter receptor localization to postsynaptic specialization membrane	IDA Inferred from Direct Assay more info	PubMed
involved_in neurotransmitter receptor localization to postsynaptic specialization membrane	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of microtubule nucleation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of microtubule nucleation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of microtubule nucleation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of receptor catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in presynaptic modulation of chemical synaptic transmission	IEA Inferred from Electronic Annotation more info
involved_in presynaptic modulation of chemical synaptic transmission	ISO Inferred from Sequence Orthology more info
involved_in regulation of ARF protein signal transduction	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of ARF protein signal transduction	IEA Inferred from Electronic Annotation more info
involved_in regulation of G protein-coupled receptor signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of G protein-coupled receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of cytokinesis	IEA Inferred from Electronic Annotation more info
involved_in regulation of cytokinesis	ISO Inferred from Sequence Orthology more info
involved_in regulation of synaptic vesicle exocytosis	IEA Inferred from Electronic Annotation more info
involved_in regulation of synaptic vesicle exocytosis	ISO Inferred from Sequence Orthology more info
involved_in synaptic vesicle recycling	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in GABA-ergic synapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in GABA-ergic synapse	IMP Inferred from Mutant Phenotype more info	PubMed
located_in calyx of Held	IEA Inferred from Electronic Annotation more info
is_active_in calyx of Held	ISO Inferred from Sequence Orthology more info
located_in centrosome	IEA Inferred from Electronic Annotation more info
located_in centrosome	ISO Inferred from Sequence Orthology more info
located_in centrosome	ISS Inferred from Sequence or Structural Similarity more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in cytosol	TAS Traceable Author Statement more info
located_in dendrite	IDA Inferred from Direct Assay more info	PubMed
located_in endosome	IDA Inferred from Direct Assay more info	PubMed
located_in excitatory synapse	IDA Inferred from Direct Assay more info	PubMed
located_in focal adhesion	IEA Inferred from Electronic Annotation more info
located_in focal adhesion	ISO Inferred from Sequence Orthology more info
located_in focal adhesion	TAS Traceable Author Statement more info	PubMed
is_active_in glutamatergic synapse	IDA Inferred from Direct Assay more info	PubMed
located_in growth cone	IDA Inferred from Direct Assay more info	PubMed
located_in inhibitory synapse	IDA Inferred from Direct Assay more info	PubMed
located_in lamellipodium	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in mitotic spindle pole	IEA Inferred from Electronic Annotation more info
located_in mitotic spindle pole	ISO Inferred from Sequence Orthology more info
located_in mitotic spindle pole	ISS Inferred from Sequence or Structural Similarity more info
is_active_in neuron projection	IBA Inferred from Biological aspect of Ancestor more info
is_active_in postsynapse	IBA Inferred from Biological aspect of Ancestor more info
is_active_in postsynapse	IDA Inferred from Direct Assay more info	PubMed
located_in postsynapse	IEA Inferred from Electronic Annotation more info
located_in postsynapse	ISO Inferred from Sequence Orthology more info
located_in postsynapse	ISS Inferred from Sequence or Structural Similarity more info
located_in postsynaptic density	IEA Inferred from Electronic Annotation more info
is_active_in presynapse	ISO Inferred from Sequence Orthology more info
is_active_in synapse	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: ARF GTPase-activating protein GIT1

Names: ARF GAP GIT1; CAT-1; CAT1; G protein-coupled receptor kinase interacting ArfGAP 1; G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein (GIT1); G protein-coupled receptor kinase-interactor 1; GRK-interacting protein 1; GRK-interactor 1; cool-associated and tyrosine-phosphorylated protein 1

NP_114002.1

EC 3.6.5.2

XP_038942874.1

EC 3.6.5.2

XP_038942875.1

EC 3.6.5.2

XP_063126041.1

EC 3.6.5.2

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.

mRNA and Protein(s)

NM_031814.2 → NP_114002.1 ARF GTPase-activating protein GIT1

See identical proteins and their annotated locations for NP_114002.1

Status: VALIDATED

Source sequence(s)

JAXUCZ010000010

UniProtKB/Swiss-Prot

Q9Z272

UniProtKB/TrEMBL

A0A8I6AGH2

Related

ENSRNOP00000073267.3, ENSRNOT00000078730.3

Conserved Domains (7) summary

smart00105
Location:3 → 124

ArfGap; Putative GTP-ase activating proteins for the small GTPase, ARF

cd00204
Location:123 → 220

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 ...

pfam08518
Location:337 → 365

GIT_SHD; Spa2 homology domain (SHD) of GIT

pfam12205
Location:649 → 763

GIT1_C; G protein-coupled receptor kinase-interacting protein 1 C term

pfam12796
Location:137 → 229

Ank_2; Ankyrin repeats (3 copies)

pfam16559
Location:418 → 482

GIT_CC; GIT coiled-coil Rho guanine nucleotide exchange factor

sd00045
Location:137 → 165

ANK; ANK repeat [structural motif]

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

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

Reference GRCr8

Genomic

NC_086028.1 Reference GRCr8

Range

62840165..62854508

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_039086946.2 → XP_038942874.1 ARF GTPase-activating protein GIT1 isoform X1

UniProtKB/TrEMBL

A0A8I6AGH2

Conserved Domains (6) summary

sd00045
Location:137 → 165

ANK; ANK repeat [structural motif]

cd08846
Location:1 → 111

ArfGap_GIT1; GIT1 GTPase activating protein for Arf

pfam08518
Location:337 → 365

GIT_SHD; Spa2 homology domain (SHD) of GIT

pfam12205
Location:642 → 758

GIT1_C; G protein-coupled receptor kinase-interacting protein 1 C term

pfam12796
Location:137 → 229

Ank_2; Ankyrin repeats (3 copies)

pfam16559
Location:418 → 478

GIT_CC; GIT coiled-coil Rho guanine nucleotide exchange factor
XM_039086947.2 → XP_038942875.1 ARF GTPase-activating protein GIT1 isoform X2

UniProtKB/TrEMBL

A0A8I6AGH2

Related

ENSRNOP00000090288.2, ENSRNOT00000101598.2

Conserved Domains (6) summary

sd00045
Location:137 → 165

ANK; ANK repeat [structural motif]

cd08846
Location:1 → 111

ArfGap_GIT1; GIT1 GTPase activating protein for Arf

pfam08518
Location:328 → 356

GIT_SHD; Spa2 homology domain (SHD) of GIT

pfam12205
Location:638 → 754

GIT1_C; G protein-coupled receptor kinase-interacting protein 1 C term

pfam12796
Location:137 → 229

Ank_2; Ankyrin repeats (3 copies)

pfam16559
Location:409 → 474

GIT_CC; GIT coiled-coil Rho guanine nucleotide exchange factor
XM_063269971.1 → XP_063126041.1 ARF GTPase-activating protein GIT1 isoform X3

UniProtKB/TrEMBL

A0A8I6AGH2