Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Guanylate cyclase soluble subunit beta-1

Gene

Gucy1b3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP.By similarity

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.By similarity

Cofactori

hemeBy similarityNote: Binds 1 or 2 heme groups per heterodimer. Heme is required for responding to nitric oxide, but not for catalytic activity.By similarity

Enzyme regulationi

Activated by nitric oxide in the presence of magnesium or manganese ions.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Iron (heme proximal ligand)By similarity

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: RGD
  • heme binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • ion binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

GTP-binding, Heme, Iron, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.2. 5301.
ReactomeiR-RNO-392154. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase soluble subunit beta-1 (EC:4.6.1.2By similarity)
Short name:
GCS-beta-1
Alternative name(s):
Guanylate cyclase soluble subunit beta-3
Short name:
GCS-beta-3
Soluble guanylate cyclase small subunit
Gene namesi
Name:Gucy1b3
Synonyms:Guc1b3, Gucy1b1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2769. Gucy1b3.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • guanylate cyclase complex, soluble Source: RGD
  • intracellular membrane-bounded organelle Source: Ensembl
  • plasma membrane Source: GO_Central
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Guanylate cyclase soluble subunit beta-1PRO_0000074118Add
BLAST

Proteomic databases

PaxDbiP20595.
PRIDEiP20595.

Expressioni

Tissue specificityi

Lung and brain.

Gene expression databases

GenevisibleiP20595. RN.

Interactioni

Subunit structurei

The active enzyme is formed by a heterodimer of an alpha and a beta subunit. Homotetramer; dimer of dimers (in vitro) (PubMed:20105301). Heterodimer with GUCY1A3. Can also form inactive homodimers in vitro (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4P310162EBI-7980539,EBI-375655

GO - Molecular functioni

  • Hsp90 protein binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP20595. 3 interactions.
MINTiMINT-1782852.
STRINGi10116.ENSRNOP00000062785.

Structurei

Secondary structure

1
619
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi349 – 39648Combined sources
Helixi400 – 4078Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HLSX-ray2.15A/B/C/D/E/F/G/H348-409[»]
ProteinModelPortaliP20595.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20595.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini421 – 554134Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiP20595.
KOiK12319.
OMAiQYGFVNH.
OrthoDBiEOG7BS48T.
PhylomeDBiP20595.
TreeFamiTF351403.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011644. Heme_NO-bd.
IPR011645. HNOB_dom_associated.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20595-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD
60 70 80 90 100
LVAAASKVLN LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN
110 120 130 140 150
LDALHDHLAT IYPGMRAPSF RCTDAEKGKG LILHYYSERE GLQDIVIGII
160 170 180 190 200
KTVAQQIHGT EIDMKVIQQR SEECDHTQFL IEEKESKEED FYEDLDRFEE
210 220 230 240 250
NGTQDSRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL PQLQPGKCSL
260 270 280 290 300
LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKL ECEDELTGAE
310 320 330 340 350
ISCLRLKGQM IYLPEADSIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR
360 370 380 390 400
DLVLLGEQFR EEYKLTQELE ILTDRLQLTL RALEDEKKKT DTLLYSVLPP
410 420 430 440 450
SVANELRHKR PVPAKRYDNV TILFSGIVGF NAFCSKHASG EGAMKIVNLL
460 470 480 490 500
NDLYTRFDTL TDSRKNPFVY KVETVGDKYM TVSGLPEPCI HHARSICHLA
510 520 530 540 550
LDMMEIAGQV QVDGESVQIT IGIHTGEVVT GVIGQRMPRY CLFGNTVNLT
560 570 580 590 600
SRTETTGEKG KINVSEYTYR CLMSPENSDP QFHLEHRGPV SMKGKKEPMQ
610
VWFLSRKNTG TEETNQDEN
Length:619
Mass (Da):70,456
Last modified:January 24, 2006 - v2
Checksum:i9F4B49E341975184
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331E → Q in AAA41204 (PubMed:2905128).Curated
Sequence conflicti45 – 451D → H in AAA41204 (PubMed:2905128).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22562 mRNA. Translation: AAA41204.1.
AB098025 mRNA. Translation: BAC44989.1.
BC081840 mRNA. Translation: AAH81840.1.
PIRiA31871. OYRTB1.
RefSeqiNP_036901.2. NM_012769.2.
UniGeneiRn.87228.

Genome annotation databases

EnsembliENSRNOT00000064930; ENSRNOP00000062785; ENSRNOG00000012060.
GeneIDi25202.
KEGGirno:25202.
UCSCiRGD:2769. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22562 mRNA. Translation: AAA41204.1.
AB098025 mRNA. Translation: BAC44989.1.
BC081840 mRNA. Translation: AAH81840.1.
PIRiA31871. OYRTB1.
RefSeqiNP_036901.2. NM_012769.2.
UniGeneiRn.87228.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HLSX-ray2.15A/B/C/D/E/F/G/H348-409[»]
ProteinModelPortaliP20595.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP20595. 3 interactions.
MINTiMINT-1782852.
STRINGi10116.ENSRNOP00000062785.

Proteomic databases

PaxDbiP20595.
PRIDEiP20595.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000064930; ENSRNOP00000062785; ENSRNOG00000012060.
GeneIDi25202.
KEGGirno:25202.
UCSCiRGD:2769. rat.

Organism-specific databases

CTDi2983.
RGDi2769. Gucy1b3.

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiP20595.
KOiK12319.
OMAiQYGFVNH.
OrthoDBiEOG7BS48T.
PhylomeDBiP20595.
TreeFamiTF351403.

Enzyme and pathway databases

BRENDAi4.6.1.2. 5301.
ReactomeiR-RNO-392154. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

EvolutionaryTraceiP20595.
PROiP20595.

Gene expression databases

GenevisibleiP20595. RN.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011644. Heme_NO-bd.
IPR011645. HNOB_dom_associated.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a cDNA coding for 70 kilodalton subunit of soluble guanylate cyclase from rat lung."
    Nakane M., Saheki S., Kuno T., Ishii K., Murad F.
    Biochem. Biophys. Res. Commun. 157:1139-1147(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Rat soluble guanylyl cyclase beta 1 subunit."
    Nakamura I., Suzuki N.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain cortex.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  4. "Crystal structure of the signaling helix coiled-coil domain of the beta1 subunit of the soluble guanylyl cyclase."
    Ma X., Beuve A., van den Akker F.
    BMC Struct. Biol. 10:2-2(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 348-409, SUBUNIT.

Entry informationi

Entry nameiGCYB1_RAT
AccessioniPrimary (citable) accession number: P20595
Secondary accession number(s): Q8CH88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 24, 2006
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two types of guanylate cyclases: soluble forms and membrane-associated receptor forms.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.