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P19687 (GCYA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanylate cyclase soluble subunit alpha-1

Short name=GCS-alpha-1
EC=4.6.1.2
Alternative name(s):
Soluble guanylate cyclase large subunit
Gene names
Name:GUCY1A1
Synonyms:GUC1A1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length691 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Activated by nitric oxide in the presence of magnesium or manganese ions.

Subunit structure

Heterodimer of an alpha and a beta chain.

Subcellular location

Cytoplasm.

Miscellaneous

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

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Contains 1 guanylate cyclase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 691691Guanylate cyclase soluble subunit alpha-1
PRO_0000074108

Regions

Domain482 – 609128Guanylate cyclase

Secondary structure

............................. 691
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19687 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 5D1FE4D2204E8683

FASTA69177,533
        10         20         30         40         50         60 
MFCAKLKDLQ ITGDCPFSLL APGQVPREPL GEATGSGPAS TPGQPGVCPG VPDKNPPGRL 

        70         80         90        100        110        120 
PRRKTSRSRV YLHTLAESIC KLIFPEFERL NLALQRTLAK HKIKENRKSL EREDFEKIVV 

       130        140        150        160        170        180 
DQAIAAGVPV EIIKESLGEE LFKICYEEDE YILGVVGGTL KDFLNSFSTL LKQSSHCQEA 

       190        200        210        220        230        240 
EKKGRFEDAS ILCLDKDPDV LYVYYFFPKR ITSLILPGII KAAARILYET EVEVSSTPSR 

       250        260        270        280        290        300 
FHQDCREFVD QPCELYSVHI RSARPHPPPG KPVSSLVIPA SLFCKTFPFH FMLDRDMSIL 

       310        320        330        340        350        360 
QLGHGIRRLM SRRDVQGKPH FDEYFEILTP KISQTFSGIM TMLNMQFLVR VRRWDNSMKK 

       370        380        390        400        410        420 
SSRVMDLKGQ MIYMVESSSI LFLGSPCVDR LEDFTGRGLY LSDIPIHNAL RDVVLIGEQA 

       430        440        450        460        470        480 
RAQDGLKKRL GKLKATLEQA HQALEEEKRK TVDLLCSIFP SEVARQLWQG HAVQAKRFGN 

       490        500        510        520        530        540 
VTMLFSDIVG FTAICSQCSP LQVITMLNAL YTRFDRQCGE LDVYKVETIG DAYCVAGGLH 

       550        560        570        580        590        600 
KESDTHAVQI ALMALKMMEL SHEVVSPHGE PIKMRIGLHS GSVFAGVVGV KMPRYCLFGN 

       610        620        630        640        650        660 
NVTLANKFES CSVPRKINVS PTTYRLLKDC PGFVFTPRSR EELPPNFPSD IPGICHFLEA 

       670        680        690 
YQQGTTSKPW FQKKDVEEAN ANFLGKASGI D 

« Hide

References

[1]"The primary structure of the larger subunit of soluble guanylyl cyclase from bovine lung. Homology between the two subunits of the enzyme."
Koesling D., Harteneck C., Humbert P., Bosserhoff A., Frank R., Schultz G., Boehme E.
FEBS Lett. 266:128-132(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Adrenal medulla.
[2]"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 472-628.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54014 mRNA. Translation: CAA37960.1.
PIROYBO77. S10713.
RefSeqNP_786972.1. NM_175778.2.
XP_005217696.1. XM_005217639.1.
XP_005217697.1. XM_005217640.1.
XP_005217698.1. XM_005217641.1.
XP_005217699.1. XM_005217642.1.
XP_005217700.1. XM_005217643.1.
XP_005217701.1. XM_005217644.1.
UniGeneBt.4480.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWNmodel-A472-628[»]
ProteinModelPortalP19687.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000019398.

Chemistry

BindingDBP19687.

Proteomic databases

PRIDEP19687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019398; ENSBTAP00000019398; ENSBTAG00000014576.
GeneID281216.
KEGGbta:281216.

Organism-specific databases

CTD2982.

Phylogenomic databases

eggNOGCOG2114.
GeneTreeENSGT00730000110520.
HOGENOMHOG000220903.
HOVERGENHBG106603.
InParanoidP19687.
KOK12318.
OMASEIPGIC.
OrthoDBEOG7VX8Z6.
TreeFamTF351403.

Family and domain databases

Gene3D3.30.70.1230. 1 hit.
InterProIPR001054. 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]
PfamPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805268.

Entry information

Entry nameGCYA1_BOVIN
AccessionPrimary (citable) accession number: P19687
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references