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P19687

- GCYA1_BOVIN

UniProt

P19687 - GCYA1_BOVIN

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Protein
Guanylate cyclase soluble subunit alpha-1
Gene
GUCY1A1, GUC1A1
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. guanylate cyclase activity Source: UniProtKB-EC
  3. heme binding Source: InterPro

GO - Biological processi

  1. intracellular signal transduction Source: InterPro
  2. positive regulation of cGMP biosynthetic process Source: Ensembl
  3. regulation of blood pressure Source: Ensembl
  4. relaxation of vascular smooth muscle Source: Ensembl
  5. response to defense-related host nitric oxide production Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_208097. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase soluble subunit alpha-1 (EC:4.6.1.2)
Short name:
GCS-alpha-1
Alternative name(s):
Soluble guanylate cyclase large subunit
Gene namesi
Name:GUCY1A1
Synonyms:GUC1A1
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 – 691691Guanylate cyclase soluble subunit alpha-1
PRO_0000074108Add
BLAST

Proteomic databases

PRIDEiP19687.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019398.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi484 – 4874
Helixi490 – 4945
Beta strandi497 – 4993
Helixi502 – 51514
Beta strandi521 – 5244
Beta strandi535 – 5373
Beta strandi540 – 5434
Helixi545 – 56521
Turni566 – 5683
Beta strandi575 – 5784
Beta strandi584 – 5885
Beta strandi590 – 5923
Beta strandi594 – 5996
Helixi600 – 61112
Helixi622 – 6276

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWNmodel-A472-628[»]
ProteinModelPortaliP19687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini482 – 609128Guanylate cyclase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00730000110520.
HOGENOMiHOG000220903.
HOVERGENiHBG106603.
InParanoidiP19687.
KOiK12318.
OMAiSEIPGIC.
OrthoDBiEOG7VX8Z6.
TreeFamiTF351403.

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.

P19687-1 [UniParc]FASTAAdd to Basket

« Hide

MFCAKLKDLQ ITGDCPFSLL APGQVPREPL GEATGSGPAS TPGQPGVCPG    50
VPDKNPPGRL PRRKTSRSRV YLHTLAESIC KLIFPEFERL NLALQRTLAK 100
HKIKENRKSL EREDFEKIVV DQAIAAGVPV EIIKESLGEE LFKICYEEDE 150
YILGVVGGTL KDFLNSFSTL LKQSSHCQEA EKKGRFEDAS ILCLDKDPDV 200
LYVYYFFPKR ITSLILPGII KAAARILYET EVEVSSTPSR FHQDCREFVD 250
QPCELYSVHI RSARPHPPPG KPVSSLVIPA SLFCKTFPFH FMLDRDMSIL 300
QLGHGIRRLM SRRDVQGKPH FDEYFEILTP KISQTFSGIM TMLNMQFLVR 350
VRRWDNSMKK SSRVMDLKGQ MIYMVESSSI LFLGSPCVDR LEDFTGRGLY 400
LSDIPIHNAL RDVVLIGEQA RAQDGLKKRL GKLKATLEQA HQALEEEKRK 450
TVDLLCSIFP SEVARQLWQG HAVQAKRFGN VTMLFSDIVG FTAICSQCSP 500
LQVITMLNAL YTRFDRQCGE LDVYKVETIG DAYCVAGGLH KESDTHAVQI 550
ALMALKMMEL SHEVVSPHGE PIKMRIGLHS GSVFAGVVGV KMPRYCLFGN 600
NVTLANKFES CSVPRKINVS PTTYRLLKDC PGFVFTPRSR EELPPNFPSD 650
IPGICHFLEA YQQGTTSKPW FQKKDVEEAN ANFLGKASGI D 691
Length:691
Mass (Da):77,533
Last modified:February 1, 1991 - v1
Checksum:i5D1FE4D2204E8683
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54014 mRNA. Translation: CAA37960.1.
PIRiS10713. OYBO77.
RefSeqiNP_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.
UniGeneiBt.4480.

Genome annotation databases

EnsembliENSBTAT00000019398; ENSBTAP00000019398; ENSBTAG00000014576.
GeneIDi281216.
KEGGibta:281216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54014 mRNA. Translation: CAA37960.1 .
PIRi S10713. OYBO77.
RefSeqi NP_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.
UniGenei Bt.4480.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AWN model - A 472-628 [» ]
ProteinModelPortali P19687.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000019398.

Chemistry

BindingDBi P19687.

Proteomic databases

PRIDEi P19687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000019398 ; ENSBTAP00000019398 ; ENSBTAG00000014576 .
GeneIDi 281216.
KEGGi bta:281216.

Organism-specific databases

CTDi 2982.

Phylogenomic databases

eggNOGi COG2114.
GeneTreei ENSGT00730000110520.
HOGENOMi HOG000220903.
HOVERGENi HBG106603.
InParanoidi P19687.
KOi K12318.
OMAi SEIPGIC.
OrthoDBi EOG7VX8Z6.
TreeFami TF351403.

Enzyme and pathway databases

Reactomei REACT_208097. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

NextBioi 20805268.

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

  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.

Entry informationi

Entry nameiGCYA1_BOVIN
AccessioniPrimary (citable) accession number: P19687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: September 3, 2014
This is version 118 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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