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Protein

Guanylate cyclase soluble subunit beta-2

Gene

Gucy1b2

Organism
Rattus norvegicus (Rat)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi43Iron (heme proximal ligand)By similarity1

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: GO_Central
  • heme binding Source: InterPro
  • ion binding Source: RGD
  • metal ion binding Source: UniProtKB-KW

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

ReactomeiR-RNO-392154. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase soluble subunit beta-2 (EC:4.6.1.2)
Short name:
GCS-beta-2
Gene namesi
Name:Gucy1b2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2770. Gucy1b2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000741201 – 682Guanylate cyclase soluble subunit beta-2Add BLAST682

Proteomic databases

PaxDbiP22717.
PRIDEiP22717.

Expressioni

Tissue specificityi

Kidney and liver.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012948.

Structurei

3D structure databases

ProteinModelPortaliP22717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini408 – 536Guanylate cyclasePROSITE-ProRule annotationAdd BLAST129

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.
HOVERGENiHBG051715.
InParanoidiP22717.
KOiK12319.
PhylomeDBiP22717.

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.

P22717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAILKLFGE YFFKFCKMSG YDRMLRTLGG NLTEFIENLD ALHSYLALSY
60 70 80 90 100
QEMNAPSFRV EEGADGAMLL HYYSDRHGLC HIVPGIIEAV AKDFFDTDVA
110 120 130 140 150
MSILDMNEEV ERTGKKEHVV FLVVQKAHRQ IRGAKASRPQ GSEDSQADQE
160 170 180 190 200
ALQGTLLRMK ERYLNIPVCP GEKSHSTAVR ASVLFGKGPL RDTFQPVYPE
210 220 230 240 250
RLWVEEEVFC DAFPFHIVFD EALRVKQAGV NIQKYVPGIL TQKFALDEYF
260 270 280 290 300
SIIHPQVTFN ISSICKFINS QFVLKTRKEM MPKARKSQPM LKLRGQMIWM
310 320 330 340 350
ESLRCMIFMC SPNVRSLQEL EESKMHLSDI APHDTTRDLI LLNQQRLAEM
360 370 380 390 400
ELSCQLEKKK EELRVLSNHL AIEKKKTETL LYAMLPEHVA NQLKEGRKVA
410 420 430 440 450
AGEFETCTIL FSDVVTFTNI CAACEPIQIV NMLNSMYSKF DRLTSVHDVY
460 470 480 490 500
KVETIGDAYM VVGGVPVPVE SHAQRVANFA LGMRISAKEV MNPVTGEPIQ
510 520 530 540 550
IRVGIHTGPV LAGVVGDKMP RYCLFGDTVN TASRMESHGL PSKVHLSPTA
560 570 580 590 600
HRALKNKGFE IVRRGEIEVK GKGKMTTYFL IQNLNATEDE IMGRPSAPAD
610 620 630 640 650
GKEVCTPGNQ VRKSPAVPRN TDHQQQVYKG DPADASNEVT LAGSPVAGRN
660 670 680
STDAVNNQPS PDETKTSVVA SGPVLSAFCV VL
Length:682
Mass (Da):76,197
Last modified:August 1, 1991 - v1
Checksum:i98C173C1A1CC7715
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57507 mRNA. Translation: AAA41207.1.
PIRiA36228. OYRTB2.
RefSeqiNP_001257640.1. NM_001270711.1.
NP_036902.2. NM_012770.2.
UniGeneiRn.10933.

Genome annotation databases

GeneIDi25206.
KEGGirno:25206.
UCSCiRGD:2770. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57507 mRNA. Translation: AAA41207.1.
PIRiA36228. OYRTB2.
RefSeqiNP_001257640.1. NM_001270711.1.
NP_036902.2. NM_012770.2.
UniGeneiRn.10933.

3D structure databases

ProteinModelPortaliP22717.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012948.

Proteomic databases

PaxDbiP22717.
PRIDEiP22717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25206.
KEGGirno:25206.
UCSCiRGD:2770. rat.

Organism-specific databases

CTDi2974.
RGDi2770. Gucy1b2.

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
HOVERGENiHBG051715.
InParanoidiP22717.
KOiK12319.
PhylomeDBiP22717.

Enzyme and pathway databases

ReactomeiR-RNO-392154. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

PROiP22717.

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 nameiGCYB2_RAT
AccessioniPrimary (citable) accession number: P22717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 6, 2016
This is version 124 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. 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.