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P16068

- GCYB1_BOVIN

UniProt

P16068 - GCYB1_BOVIN

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Protein
Guanylate cyclase soluble subunit beta-1
Gene
GUCY1B1, GUC1B3, GUCY1B3
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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

ReactomeiREACT_208097. 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: 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-1
PRO_0000074115Add
BLAST

Proteomic databases

PRIDEiP16068.

Expressioni

Tissue specificityi

Lung and brain.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi415 – 42612
Helixi428 – 4314
Beta strandi437 – 4404
Helixi441 – 4433
Helixi444 – 46219
Beta strandi469 – 4757
Beta strandi478 – 4836
Helixi490 – 4923
Helixi493 – 50614
Turni507 – 5093
Beta strandi520 – 53314
Beta strandi539 – 5413
Helixi545 – 55612
Helixi566 – 5694

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWNmodel-B412-572[»]
ProteinModelPortaliP16068.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini421 – 554134Guanylate cyclase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00750000117642.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiP16068.
KOiK12319.
OMAiVLMSEQF.

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.
[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

MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD    50
LVAAASKVLN LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN 100
LDALHDHLAT IYPGMRAPSF RCTDADKGKG LILHYYSERE GLQDIVIGII 150
KTVAQQIHGT EIDMKVIQQR NEECDHTQFL IEEKESKEED FYEDLDRFEE 200
NGTQESRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL PQLQPGNCSL 250
LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKS ECEDELTGTE 300
ISCLRLKGQM IYLPEADSIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR 350
DLVLLGEQFR EEYKLTQELE ILTDRLQLTL RALEDEKKKT DTLLYSVLPP 400
SVANELRHKR PVPAKRYDNV TILFSGIVGF NAFCSKHASG EGAMKIVNLL 450
NDLYTRFDTL TDSRKNPFVY KVETVGDKYM TVSGLPEPCI HHARSICHLA 500
LDMMEIAGQV QVDGESVQIT IGIHTGEVVT GVIGQRMPRY CLFGNTVNLT 550
SRTETTGEKG KINVSEYTYR CLMTPENSDP QFHLEHRGPV SMKGKKEPMQ 600
VWFLSRKNTG TEETEQDEN 619
Length:619
Mass (Da):70,502
Last modified:April 1, 1990 - v1
Checksum:i8EFB14952B80F344
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Y00770 mRNA. Translation: CAA68739.1 .
BC133308 mRNA. Translation: AAI33309.1 .
PIRi S01653. OYBO70.
RefSeqi NP_777066.1. NM_174641.1.
UniGenei Bt.109786.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AWN model - B 412-572 [» ]
ProteinModelPortali P16068.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P16068.

Proteomic databases

PRIDEi P16068.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000005009 ; ENSBTAP00000005009 ; ENSBTAG00000003840 .
GeneIDi 282433.
KEGGi bta:282433.

Organism-specific databases

CTDi 2983.

Phylogenomic databases

eggNOGi COG2114.
GeneTreei ENSGT00750000117642.
HOGENOMi HOG000220903.
HOVERGENi HBG051715.
InParanoidi P16068.
KOi K12319.
OMAi VLMSEQF.

Enzyme and pathway databases

Reactomei REACT_208097. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

NextBioi 20806209.

Family and domain databases

Gene3Di 3.30.70.1230. 1 hit.
InterProi IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011645. Haem_no_assoc-bd.
IPR011644. Heme_NO-bd.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
[Graphical view ]
Pfami PF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view ]
SMARTi SM00044. CYCc. 1 hit.
[Graphical view ]
SUPFAMi SSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEi PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lung.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-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(1994) [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(1998) [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(1997) [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: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 130 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

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