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

GUCY1B1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

hemeNote: Binds 1 or 2 heme groups per heterodimer.

Enzyme regulationi

Activated by nitric oxide in the presence of magnesium or manganese ions, binding of NO to the heme iron increases catalytic activity up to 400 folds.

Sites

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

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. guanylate cyclase activity Source: UniProtKB-EC
  3. heme binding Source: AgBase
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. intracellular signal transduction Source: InterPro
  2. ion transport Source: UniProtKB-KW
  3. iron ion homeostasis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis, Ion transport, Iron transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi4.6.1.2. 908.
ReactomeiREACT_299550. 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:GUCY1B1
Synonyms:GUC1B3, GUCY1B3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 17

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Guanylate cyclase soluble subunit beta-1PRO_0000074115Add
BLAST

Proteomic databases

PRIDEiP16068.

Expressioni

Tissue specificityi

Lung and brain.

Gene expression databases

ExpressionAtlasiP16068. baseline.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWNmodel-B412-572[»]
ProteinModelPortaliP16068.
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.
InParanoidiP16068.
KOiK12319.
OMAiQYGFVNH.

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.

P16068-1 [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 RCTDADKGKG 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 KEGLLDVEKS 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 CLMTPENSDP QFHLEHRGPV SMKGKKEPMQ
610
VWFLSRKNTG TEETEQDEN
Length:619
Mass (Da):70,502
Last modified:March 31, 1990 - v1
Checksum:i8EFB14952B80F344
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00770 mRNA. Translation: CAA68739.1.
BC133308 mRNA. Translation: AAI33309.1.
PIRiS01653. OYBO70.
RefSeqiNP_777066.1. NM_174641.1.
UniGeneiBt.109786.

Genome annotation databases

EnsembliENSBTAT00000005009; ENSBTAP00000005009; ENSBTAG00000003840.
GeneIDi282433.
KEGGibta:282433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00770 mRNA. Translation: CAA68739.1.
BC133308 mRNA. Translation: AAI33309.1.
PIRiS01653. OYBO70.
RefSeqiNP_777066.1. NM_174641.1.
UniGeneiBt.109786.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWNmodel-B412-572[»]
ProteinModelPortaliP16068.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP16068.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005009; ENSBTAP00000005009; ENSBTAG00000003840.
GeneIDi282433.
KEGGibta:282433.

Organism-specific databases

CTDi2983.

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiP16068.
KOiK12319.
OMAiQYGFVNH.

Enzyme and pathway databases

BRENDAi4.6.1.2. 908.
ReactomeiREACT_299550. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

NextBioi20806209.

Gene expression databases

ExpressionAtlasiP16068. baseline.

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

« Hide 'large scale' publications
  1. "The primary structure of the 70 kDa subunit of bovine soluble guanylate cyclase."
    Koesling D., Herz J., Gausepohl H., Niroomand F., Hinsch K.-D., Muelsch A., Boehme E., Schultz G., Frank R.
    FEBS Lett. 239:29-34(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lung.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Brain cortex.
  3. "Mutation of His-105 in the beta 1 subunit yields a nitric oxide-insensitive form of soluble guanylyl cyclase."
    Wedel B., Humbert P., Harteneck C., Foerster J., Malkewitz J., Bohme E., Schultz G., Koesling D.
    Proc. Natl. Acad. Sci. U.S.A. 91:2592-2596(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HISTIDINE RESIDUES.
  4. "Identification of histidine 105 in the beta1 subunit of soluble guanylate cyclase as the heme proximal ligand."
    Zhao Y., Schelvis J.P., Babcock G.T., Marletta M.A.
    Biochemistry 37:4502-4509(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEME PROXIMAL LIGAND.
  5. "Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis."
    Liu Y., Ruoho A.E., Rao V.D., Hurley J.H.
    Proc. Natl. Acad. Sci. U.S.A. 94:13414-13419(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 412-572.

Entry informationi

Entry nameiGCYB1_BOVIN
AccessioniPrimary (citable) accession number: P16068
Secondary accession number(s): A2VDM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1990
Last sequence update: March 31, 1990
Last modified: March 31, 2015
This is version 135 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

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.