SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00001940 
UniProt Accession
Theoretical PI
5.23  
Molecular Weight
70456 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gucy1b3 
Gene Synonyms/Alias
Guc1b3, Gucy1b1 
Protein Name
Guanylate cyclase soluble subunit beta-1 
Protein Synonyms/Alias
GCS-beta-1EC=4.6.1.2 Guanylate cyclase soluble subunit beta-3;GCS-beta-3 Soluble guanylate cyclase small subunit; 
Organism
Rattus norvegicus (Rat) 
NCBI Taxonomy ID
10116 
Chromosome Location
chr:2;173683154-173735298;-1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. O. Sarkar, W. Xia and D. D. Mruk (2006) Adjudin-mediated junction restructuring in the seminiferous epithelium leads to displacement of soluble guanylate cyclase from adherens junctions. J Cell Physiol 208(1): 175-87. 

Abstract
A plethora of evidence supports the role of cyclic nucleotides in junction restructuring. For instance, studies have shown cGMP to be a key regulator of junction assembly and disassembly in different in vitro and in vivo systems. In this study, we examine the role of soluble guanylate cyclase (sGC) in junction restructuring in the seminiferous epithelium of the rat testis. First, the interaction of soluble guanylate cyclase beta1 (sGCbeta1; sGC is a heterodimer comprised of an alpha and a beta subunit) with proteins that constitute adherens and tight junctions in the testis was demonstrated. By immunoprecipitation, sGCbeta1 was found to associate with occludin, JAM-A, and ZO-1, as well as with cadherin, catenin, nectin, afadin, ponsin, and espin, suggestive of its role in cell junction dynamics. These results were corroborated in part by immunohistochemistry experiments, which revealed that the localization of sGCbeta1 was largely restricted to the site of the apical and basal ectoplasmic specialization. Next, the role of sGC in junction dynamics was addressed by using an in vivo model of junction restructuring. Administration of Adjudin--a chemical entity known to specifically perturb adhesion between Sertoli and germ cells (i.e., round and elongate(ing) spermatids and most spermatocytes)--resulted in a approximately 1.5-fold increase in sGCbeta1, coinciding with the loss of germ cells from the epithelium. More importantly, the ability of sGCbeta1 to associate with cadherin increased approximately three-fold during Adjudin-mediated restructuring of Sertoli-germ cell junctions, whereas its interaction with tight junction proteins (i.e., occludin and ZO-1) decreased. Taken collectively, these results suggest that sGC participates in the remodeling of cell junctions during spermatogenesis. PMID: [16547975] 

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Figures for illustrating the function of this protein/gene
Ref: O. Sarkar, W. Xia and D. D. Mruk (2006) Adjudin-mediated junction restructuring in the seminiferous epithelium leads to displacement of soluble guanylate cyclase from adherens junctions. J Cell Physiol 208(1): 175-87. PMID: [16547975]
Ref: O. Sarkar, W. Xia and D. D. Mruk (2006) Adjudin-mediated junction restructuring in the seminiferous epithelium leads to displacement of soluble guanylate cyclase from adherens junctions. J Cell Physiol 208(1): 175-87. PMID: [16547975]
Ref: O. Sarkar, W. Xia and D. D. Mruk (2006) Adjudin-mediated junction restructuring in the seminiferous epithelium leads to displacement of soluble guanylate cyclase from adherens junctions. J Cell Physiol 208(1): 175-87. PMID: [16547975]
Ref: O. Sarkar, W. Xia and D. D. Mruk (2006) Adjudin-mediated junction restructuring in the seminiferous epithelium leads to displacement of soluble guanylate cyclase from adherens junctions. J Cell Physiol 208(1): 175-87. PMID: [16547975]
Function
 
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Subcellular Location
Cytoplasm. 
Tissue Specificity
Lung and brain. 
Gene Ontology
GO IDGO termEvidence
GO:0008074 C:guanylate cyclase complex, soluble IDA:RGD.
GO:0043231 C:intracellular membrane-bounded organelle IEA:Compara.
GO:0005525 F:GTP binding IEA:UniProtKB-KW.
GO:0004383 F:guanylate cyclase activity IDA:RGD.
GO:0020037 F:heme binding IDA:RGD.
GO:0007263 P:nitric oxide mediated signal transduction IDA:RGD.
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Interpro
IPR001054;    A/G_cyclase.
IPR018297;    A/G_cyclase_CS.
IPR011645;    Haem_no_assoc-bd.
IPR011644;    Heme_NO-bd.
IPR024096;    NO_sig/Golgi_transp_ligand-bd.
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Pfam
PF00211;    Guanylate_cyc;    1.
PF07700;    HNOB;    1.
PF07701;    HNOBA;    1.
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SMART
SM00044;    CYCc;    1.
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PROSITE
PS00452;    GUANYLATE_CYCLASE_1;    1.
PS50125;    GUANYLATE_CYCLASE_2;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1    619       Guanylate cyclase soluble subunit beta-1.
                             /FTId=PRO_0000074118.
DOMAIN      421    554       Guanylate cyclase.
METAL       105    105       Iron (heme proximal ligand) (By
                             similarity).
CONFLICT     33     33       E -> Q (in Ref. 1; AAA41204).
CONFLICT     45     45       D -> H (in Ref. 1; AAA41204).
HELIX       349    396
HELIX       400    407
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Nucleotide Sequence
Length: 3047 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 619 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Dlg4MINT 
Other Protein-Protein interaction resources
String database  
View Microarray data
Temporarily unavailable 
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