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Protein

Guanylate cyclase soluble subunit beta-1

Gene

GUCY1B3

Organism
Homo sapiens (Human)
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 similarity1 Publication

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.1 Publication

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi105Iron (heme proximal ligand)By similarity1

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: UniProtKB
  • heme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • receptor activity Source: ProtInc

GO - Biological processi

  • blood circulation Source: ProtInc
  • cellular response to nitric oxide Source: UniProtKB
  • cGMP biosynthetic process Source: UniProtKB
  • nitric oxide-cGMP-mediated signaling pathway Source: UniProtKB
  • nitric oxide mediated signal transduction Source: ProtInc
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

BioCyciZFISH:HS00761-MONOMER.
ReactomeiR-HSA-392154. Nitric oxide stimulates guanylate cyclase.
SIGNORiQ02153.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase soluble subunit beta-1 (EC:4.6.1.23 Publications)
Short name:
GCS-beta-1
Alternative name(s):
Guanylate cyclase soluble subunit beta-31 Publication
Short name:
GCS-beta-3
Soluble guanylate cyclase small subunit
Gene namesi
Name:GUCY1B3
Synonyms:GUC1B3, GUCSB3, GUCY1B1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:4687. GUCY1B3.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi2983.
OpenTargetsiENSG00000061918.
PharmGKBiPA29068.

Chemistry databases

ChEMBLiCHEMBL3137281.

Polymorphism and mutation databases

BioMutaiGUCY1B3.
DMDMi399328.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000741161 – 619Guanylate cyclase soluble subunit beta-1Add BLAST619

Proteomic databases

MaxQBiQ02153.
PaxDbiQ02153.
PeptideAtlasiQ02153.
PRIDEiQ02153.

PTM databases

iPTMnetiQ02153.
PhosphoSitePlusiQ02153.

Expressioni

Tissue specificityi

Detected in brain cortex and cerebellum (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000061918.
CleanExiHS_GUCY1B3.
ExpressionAtlasiQ02153. baseline and differential.
GenevisibleiQ02153. HS.

Organism-specific databases

HPAiCAB010890.
HPA020870.

Interactioni

Subunit structurei

The active enzyme is formed by a heterodimer of an alpha and a beta subunit. Heterodimer with GUCY1A3 (PubMed:1352257, PubMed:23505436, PubMed:24669844). Can also form inactive homodimers in vitro (PubMed:23505436, PubMed:24669844).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GUCY1A3Q021082EBI-6911707,EBI-3910037

Protein-protein interaction databases

BioGridi109238. 15 interactors.
IntActiQ02153. 2 interactors.
STRINGi9606.ENSP00000264424.

Structurei

Secondary structure

1619
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi415 – 427Combined sources13
Helixi430 – 436Combined sources7
Helixi443 – 461Combined sources19
Turni463 – 465Combined sources3
Beta strandi470 – 472Combined sources3
Beta strandi479 – 487Combined sources9
Helixi492 – 507Combined sources16
Beta strandi519 – 533Combined sources15
Beta strandi535 – 537Combined sources3
Beta strandi539 – 544Combined sources6
Helixi545 – 555Combined sources11
Beta strandi561 – 565Combined sources5
Helixi566 – 571Combined sources6
Turni575 – 577Combined sources3
Beta strandi582 – 590Combined sources9
Beta strandi599 – 607Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WZ1X-ray1.63A/B408-619[»]
3UVJX-ray2.08B/D408-619[»]
4NI2X-ray1.90B408-608[»]
ProteinModelPortaliQ02153.
SMRiQ02153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02153.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini421 – 554Guanylate cyclasePROSITE-ProRule annotationAdd BLAST134

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.
InParanoidiQ02153.
KOiK12319.
PhylomeDBiQ02153.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform HSGC-1 (identifier: Q02153-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 IIFDRDLVVT QCGNAIYRVL PQLQPGNCSL
260 270 280 290 300
LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKL ECEDELTGTE
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 TEETKQDDD
Length:619
Mass (Da):70,514
Last modified:July 1, 1993 - v1
Checksum:i231E4E660DE02AA1
GO
Isoform HSGC-2 (identifier: Q02153-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-425: Missing.

Show »
Length:586
Mass (Da):66,738
Checksum:i59818154086FD4A3
GO
Isoform 3 (identifier: Q02153-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MYGFVNHALELLVIRNYGPEVWEDIK → MLMCFI

Note: No experimental confirmation available.
Show »
Length:599
Mass (Da):68,165
Checksum:i93F6129D51BECB23
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0543651 – 26MYGFV…WEDIK → MLMCFI in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_001813393 – 425Missing in isoform HSGC-2. 1 PublicationAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66533 mRNA. Translation: CAA47144.1.
AF020340 mRNA. Translation: AAB94877.1.
AK296680 mRNA. Translation: BAH12412.1.
AC114761 Genomic DNA. No translation available.
BC047620 mRNA. Translation: AAH47620.2.
CCDSiCCDS47154.1. [Q02153-1]
CCDS77976.1. [Q02153-2]
CCDS77977.1. [Q02153-3]
PIRiS23097.
RefSeqiNP_000848.1. NM_000857.3. [Q02153-1]
NP_001278881.1. NM_001291952.1. [Q02153-3]
NP_001278882.1. NM_001291953.1.
NP_001278883.1. NM_001291954.1. [Q02153-2]
UniGeneiHs.77890.

Genome annotation databases

EnsembliENST00000264424; ENSP00000264424; ENSG00000061918. [Q02153-1]
ENST00000503520; ENSP00000420842; ENSG00000061918. [Q02153-2]
ENST00000505764; ENSP00000426319; ENSG00000061918. [Q02153-3]
GeneIDi2983.
KEGGihsa:2983.
UCSCiuc003ipc.4. human. [Q02153-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66533 mRNA. Translation: CAA47144.1.
AF020340 mRNA. Translation: AAB94877.1.
AK296680 mRNA. Translation: BAH12412.1.
AC114761 Genomic DNA. No translation available.
BC047620 mRNA. Translation: AAH47620.2.
CCDSiCCDS47154.1. [Q02153-1]
CCDS77976.1. [Q02153-2]
CCDS77977.1. [Q02153-3]
PIRiS23097.
RefSeqiNP_000848.1. NM_000857.3. [Q02153-1]
NP_001278881.1. NM_001291952.1. [Q02153-3]
NP_001278882.1. NM_001291953.1.
NP_001278883.1. NM_001291954.1. [Q02153-2]
UniGeneiHs.77890.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WZ1X-ray1.63A/B408-619[»]
3UVJX-ray2.08B/D408-619[»]
4NI2X-ray1.90B408-608[»]
ProteinModelPortaliQ02153.
SMRiQ02153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109238. 15 interactors.
IntActiQ02153. 2 interactors.
STRINGi9606.ENSP00000264424.

Chemistry databases

ChEMBLiCHEMBL3137281.

PTM databases

iPTMnetiQ02153.
PhosphoSitePlusiQ02153.

Polymorphism and mutation databases

BioMutaiGUCY1B3.
DMDMi399328.

Proteomic databases

MaxQBiQ02153.
PaxDbiQ02153.
PeptideAtlasiQ02153.
PRIDEiQ02153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264424; ENSP00000264424; ENSG00000061918. [Q02153-1]
ENST00000503520; ENSP00000420842; ENSG00000061918. [Q02153-2]
ENST00000505764; ENSP00000426319; ENSG00000061918. [Q02153-3]
GeneIDi2983.
KEGGihsa:2983.
UCSCiuc003ipc.4. human. [Q02153-1]

Organism-specific databases

CTDi2983.
DisGeNETi2983.
GeneCardsiGUCY1B3.
HGNCiHGNC:4687. GUCY1B3.
HPAiCAB010890.
HPA020870.
MIMi139397. gene.
neXtProtiNX_Q02153.
OpenTargetsiENSG00000061918.
PharmGKBiPA29068.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiQ02153.
KOiK12319.
PhylomeDBiQ02153.
TreeFamiTF351403.

Enzyme and pathway databases

BioCyciZFISH:HS00761-MONOMER.
ReactomeiR-HSA-392154. Nitric oxide stimulates guanylate cyclase.
SIGNORiQ02153.

Miscellaneous databases

EvolutionaryTraceiQ02153.
GeneWikiiGUCY1B3.
GenomeRNAii2983.
PROiQ02153.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000061918.
CleanExiHS_GUCY1B3.
ExpressionAtlasiQ02153. baseline and differential.
GenevisibleiQ02153. HS.

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...

Entry informationi

Entry nameiGCYB1_HUMAN
AccessioniPrimary (citable) accession number: Q02153
Secondary accession number(s): B7Z426, Q86WY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.