Gucy1a1 guanylate cyclase 1 soluble subunit alpha 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Gucy1a1provided by RGD
Official Full Name: guanylate cyclase 1 soluble subunit alpha 1provided by RGD
Primary source: RGD:68436
See related: EnsemblRapid:ENSRNOG00000012302 AllianceGenome:RGD:68436
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: SGC; Gucy1a3
Summary: Enables nitric oxide binding activity. Contributes to adenylate cyclase activity and cytidylate cyclase activity. Involved in response to herbicide and response to organic cyclic compound. Part of guanylate cyclase complex, soluble. Biomarker of withdrawal disorder. Human ortholog(s) of this gene implicated in Moyamoya disease. Orthologous to human GUCY1A1 (guanylate cyclase 1 soluble subunit alpha 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Lung (RPKM 322.0), Thymus (RPKM 151.8) and 9 other tissues See more
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 2q34

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	2	NC_086020.1 (169716684..169780360, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	2	NC_051337.1 (167418615..167482293, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	2	NC_005101.4 (181045694..181103321, complement)

Chromosome 2 - NC_086020.1 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?

FoxO4 controls sGCbeta transcription in vascular smooth muscle.
Title: FoxO4 controls sGCβ transcription in vascular smooth muscle.
GAPDH delivers heme to soluble guanylyl cyclase.
Title: GAPDH delivers heme to soluble guanylyl cyclase.
These studies identify MEK/ERK signaling as an important pathway by which TGFbeta regulates sGC expression in pulmonary artery smooth muscle cell.
Title: Transforming growth factor-β downregulates sGC subunit expression in pulmonary artery smooth muscle cells via MEK and ERK signaling.
Hence, SO2 exerted its vasodilatory effects at least partly by promoting disulfide-dependent dimerization of sGC and PKG, resulting in an activated sGC/cGMP/PKG pathway in blood vessels. These findings revealed a new mode of action and mechanisms by which SO2 regulated the vascular tone.
Title: The vasodilatory effect of sulfur dioxide via SGC/cGMP/PKG pathway in association with sulfhydryl-dependent dimerization.
rhoA/rho-kinase and sGC/cGMP/PKG pathways play pivotal roles in cerebral vasospasm after subarachnoid hemorrhage.
Title: Alteration of basilar artery rho-kinase and soluble guanylyl cyclase protein expression in a rat model of cerebral vasospasm following subarachnoid hemorrhage.
The effect of glucagon-like peptide-2 on the expression of the alpha1, alpha2, and beta1 subunits of soluble guanylyl cyclase, was studied.
Title: Glucagon-like peptide-2 (GLP-2) modulates the cGMP signalling pathway by regulating the expression of the soluble guanylyl cyclase receptor subunits in cultured rat astrocytes.
sGC undergoes a reductive nitrosylation reaction that is coupled to the S-nitrosation of sGC cysteines.
Title: Heme-assisted S-nitrosation desensitizes ferric soluble guanylate cyclase to nitric oxide.
Mechanisms of sGC activation are investigated by electronic absorption and resonance Raman spectroscopy, confirming that stoichiometrically bound 1-nitric oxide (1-NO) contains five-coordinate NO-heme cofactor.
Title: Soluble guanylate cyclase is activated differently by excess NO and by YC-1: resonance Raman spectroscopic evidence.
Soluble guanylate cyclase is activated by binding of carbon monoxide and YC-1.
Title: Probing soluble guanylate cyclase activation by CO and YC-1 using resonance Raman spectroscopy.
Based on these findings, we concluded that sGC immunoreactivity was specifically distributed in capillary pericytes
Title: The expression of soluble guanylate cyclase in the vasculature of rat skeletal muscle.

Submit: New GeneRIF Correction See all GeneRIFs (28)

General gene information

Go to the top of the page Help

Markers

RH133297 (e-PCR)
- UniSTS:216580

Gucy1a3 (e-PCR), detects polymorphism
- UniSTS:506963

Gucy1a3 (e-PCR), detects polymorphism
- UniSTS:525449

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables GTP binding	IEA Inferred from Electronic Annotation more info
contributes_to adenylate cyclase activity	IDA Inferred from Direct Assay more info	PubMed
contributes_to cytidylate cyclase activity	IDA Inferred from Direct Assay more info	PubMed
enables guanylate cyclase activity	IBA Inferred from Biological aspect of Ancestor more info
enables guanylate cyclase activity	IEA Inferred from Electronic Annotation more info
enables guanylate cyclase activity	ISO Inferred from Sequence Orthology more info
enables guanylate cyclase activity	TAS Traceable Author Statement more info	PubMed
enables heme binding	IEA Inferred from Electronic Annotation more info
enables nitric oxide binding	IDA Inferred from Direct Assay more info	PubMed
enables protein-containing complex binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in cGMP biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in cGMP biosynthetic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within cGMP biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in cGMP biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in cGMP-mediated signaling	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of nitric oxide mediated signal transduction	ISO Inferred from Sequence Orthology more info
involved_in nitric oxide-cGMP-mediated signaling	IEA Inferred from Electronic Annotation more info
involved_in nitric oxide-cGMP-mediated signaling	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of nitric oxide mediated signal transduction	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within positive regulation of nitric oxide mediated signal transduction	ISO Inferred from Sequence Orthology more info
involved_in regulation of blood pressure	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within regulation of blood pressure	ISO Inferred from Sequence Orthology more info
involved_in relaxation of vascular associated smooth muscle	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within relaxation of vascular associated smooth muscle	ISO Inferred from Sequence Orthology more info
involved_in response to herbicide	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to organic cyclic compound	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to oxygen levels	IBA Inferred from Biological aspect of Ancestor more info
involved_in retrograde trans-synaptic signaling by nitric oxide, modulating synaptic transmission	IEA Inferred from Electronic Annotation more info
involved_in retrograde trans-synaptic signaling by nitric oxide, modulating synaptic transmission	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in GABA-ergic synapse	IEA Inferred from Electronic Annotation more info
is_active_in GABA-ergic synapse	ISO Inferred from Sequence Orthology more info
located_in glutamatergic synapse	IEA Inferred from Electronic Annotation more info
is_active_in glutamatergic synapse	ISO Inferred from Sequence Orthology more info
part_of guanylate cyclase complex, soluble	IBA Inferred from Biological aspect of Ancestor more info
part_of guanylate cyclase complex, soluble	IDA Inferred from Direct Assay more info	PubMed
part_of guanylate cyclase complex, soluble	IEA Inferred from Electronic Annotation more info
part_of guanylate cyclase complex, soluble	ISO Inferred from Sequence Orthology more info
part_of guanylate cyclase complex, soluble	TAS Traceable Author Statement more info	PubMed
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: guanylate cyclase soluble subunit alpha-1

Names: GCS-alpha-1; GCS-alpha-3; Guanylate cyclase, soluble, alpha 1 (GTP pyrophosphate - lyase); guanylate cyclase 1 soluble subunit alpha 3; guanylate cyclase 1, soluble, alpha 3; guanylate cyclase soluble subunit alpha-3; soluble guanylate cyclase large subunit

NP_058786.2

EC 4.6.1.2

XP_006232580.1

EC 4.6.1.2

XP_008759329.1

EC 4.6.1.2

XP_017446500.1

EC 4.6.1.2

XP_063138383.1

EC 4.6.1.2

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_017090.2 → NP_058786.2 guanylate cyclase soluble subunit alpha-1

See identical proteins and their annotated locations for NP_058786.2

Status: PROVISIONAL

Source sequence(s)

BC085746

UniProtKB/Swiss-Prot

P19686

UniProtKB/TrEMBL

A6J5U0, F7ESJ1, Q5U330

Related

ENSRNOP00000017190.2, ENSRNOT00000017190.6

Conserved Domains (4) summary

smart00044
Location:444 → 633

CYCc; Adenylyl- / guanylyl cyclase, catalytic domain

pfam00211
Location:471 → 642

Guanylate_cyc; Adenylate and Guanylate cyclase catalytic domain

pfam07700
Location:111 → 234

HNOB; Haem-NO-binding

pfam07701
Location:276 → 465

HNOBA; Heme NO binding associated

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_086020.1 Reference GRCr8

Range

169716684..169780360 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_008761107.4 → XP_008759329.1 guanylate cyclase soluble subunit alpha-1 isoform X1

See identical proteins and their annotated locations for XP_008759329.1

UniProtKB/Swiss-Prot

P19686

UniProtKB/TrEMBL

A6J5U0, F7ESJ1, Q5U330

Conserved Domains (4) summary

smart00044
Location:444 → 633

CYCc; Adenylyl- / guanylyl cyclase, catalytic domain

pfam00211
Location:471 → 642

Guanylate_cyc; Adenylate and Guanylate cyclase catalytic domain

pfam07700
Location:111 → 234

HNOB; Haem-NO-binding

pfam07701
Location:276 → 465

HNOBA; Heme NO binding associated
XM_006232518.5 → XP_006232580.1 guanylate cyclase soluble subunit alpha-1 isoform X1

See identical proteins and their annotated locations for XP_006232580.1

UniProtKB/Swiss-Prot

P19686

UniProtKB/TrEMBL

A6J5U0, F7ESJ1, Q5U330

Conserved Domains (4) summary

smart00044
Location:444 → 633

CYCc; Adenylyl- / guanylyl cyclase, catalytic domain

pfam00211
Location:471 → 642

Guanylate_cyc; Adenylate and Guanylate cyclase catalytic domain

pfam07700
Location:111 → 234

HNOB; Haem-NO-binding

pfam07701
Location:276 → 465

HNOBA; Heme NO binding associated
XM_063282313.1 → XP_063138383.1 guanylate cyclase soluble subunit alpha-1 isoform X1

UniProtKB/Swiss-Prot

P19686

UniProtKB/TrEMBL

A6J5U0, F7ESJ1, Q5U330
XM_017591011.3 → XP_017446500.1 guanylate cyclase soluble subunit alpha-1 isoform X1

UniProtKB/Swiss-Prot

P19686

UniProtKB/TrEMBL

A6J5U0, F7ESJ1, Q5U330

Conserved Domains (4) summary

smart00044
Location:444 → 633

CYCc; Adenylyl- / guanylyl cyclase, catalytic domain

pfam00211
Location:471 → 642

Guanylate_cyc; Adenylate and Guanylate cyclase catalytic domain

pfam07700
Location:111 → 234

HNOB; Haem-NO-binding

pfam07701
Location:276 → 465

HNOBA; Heme NO binding associated