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Protein

Guanylate cyclase soluble subunit beta-1

Gene

Gucy1b3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

hemeBy similarityNote: Binds 1 or 2 heme groups per heterodimer.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

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

ReactomeiREACT_282024. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase soluble subunit beta-1 (EC:4.6.1.2)
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1860604. Gucy1b3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Guanylate cyclase soluble subunit beta-1PRO_0000074117Add
BLAST

Proteomic databases

MaxQBiO54865.
PaxDbiO54865.
PRIDEiO54865.

PTM databases

PhosphoSiteiO54865.

Expressioni

Gene expression databases

BgeeiO54865.
CleanExiMM_GUCY1B3.
ExpressionAtlasiO54865. baseline and differential.
GenevisibleiO54865. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

IntActiO54865. 1 interaction.
MINTiMINT-4105057.
STRINGi10090.ENSMUSP00000029635.

Structurei

3D structure databases

ProteinModelPortaliO54865.
SMRiO54865. Positions 1-182, 212-334, 348-408, 411-608.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiCOG2114.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiO54865.
OMAiQYGFVNH.
OrthoDBiEOG7BS48T.
PhylomeDBiO54865.
TreeFamiTF351403.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011645. Haem_no_assoc-bd.
IPR011644. Heme_NO-bd.
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.

O54865-1 [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 NEECDHTQFL IEEKESKEED FYEDLDRFEE
210 220 230 240 250
NGTQESRISP YTFCKAFPFH IIFDRNLVVT QCGNAIYRVL PQLQPGNCSL
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 LFHLEHRGPV SMKGKKEPMQ
610 620
VWFLSRKNTG TEETNEEDEN
Length:620
Mass (Da):70,598
Last modified:June 1, 1998 - v1
Checksum:iEED89ABF539F4EF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020339 mRNA. Translation: AAB94876.1.
AF297083 mRNA. Translation: AAG17447.1.
CCDSiCCDS38460.1.
RefSeqiNP_059497.1. NM_017469.4.
UniGeneiMm.9445.

Genome annotation databases

EnsembliENSMUST00000029635; ENSMUSP00000029635; ENSMUSG00000028005.
GeneIDi54195.
UCSCiuc008por.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020339 mRNA. Translation: AAB94876.1.
AF297083 mRNA. Translation: AAG17447.1.
CCDSiCCDS38460.1.
RefSeqiNP_059497.1. NM_017469.4.
UniGeneiMm.9445.

3D structure databases

ProteinModelPortaliO54865.
SMRiO54865. Positions 1-182, 212-334, 348-408, 411-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54865. 1 interaction.
MINTiMINT-4105057.
STRINGi10090.ENSMUSP00000029635.

PTM databases

PhosphoSiteiO54865.

Proteomic databases

MaxQBiO54865.
PaxDbiO54865.
PRIDEiO54865.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029635; ENSMUSP00000029635; ENSMUSG00000028005.
GeneIDi54195.
UCSCiuc008por.2. mouse.

Organism-specific databases

CTDi2983.
MGIiMGI:1860604. Gucy1b3.

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiO54865.
OMAiQYGFVNH.
OrthoDBiEOG7BS48T.
PhylomeDBiO54865.
TreeFamiTF351403.

Enzyme and pathway databases

ReactomeiREACT_282024. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

NextBioi311038.
PROiO54865.
SOURCEiSearch...

Gene expression databases

BgeeiO54865.
CleanExiMM_GUCY1B3.
ExpressionAtlasiO54865. baseline and differential.
GenevisibleiO54865. MM.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011645. Haem_no_assoc-bd.
IPR011644. Heme_NO-bd.
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

  1. "Murine soluble guanylate cyclase, beta-1 subunit."
    Gansemans Y., Brouckaert P., Fiers W.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. "Genomic organization of alpha 1 and beta 1 subunits of the mammalian soluble guanylyl cyclase genes."
    Sharina I.G., Krumenacker J.S., Martin E., Murad F.
    Proc. Natl. Acad. Sci. U.S.A. 97:10878-10883(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/10.

Entry informationi

Entry nameiGCYB1_MOUSE
AccessioniPrimary (citable) accession number: O54865
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 1998
Last modified: July 22, 2015
This is version 112 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.