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Protein

Guanylate cyclase soluble subunit alpha-1

Gene

GUCY1A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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

BRENDAi4.6.1.2. 908.
ReactomeiREACT_299550. 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 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 – 691691Guanylate cyclase soluble subunit alpha-1PRO_0000074108Add
BLAST

Proteomic databases

PRIDEiP19687.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019398.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWNmodel-A472-628[»]
ProteinModelPortaliP19687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini482 – 609128Guanylate 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.
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.
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.

P19687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFCAKLKDLQ ITGDCPFSLL APGQVPREPL GEATGSGPAS TPGQPGVCPG
60 70 80 90 100
VPDKNPPGRL PRRKTSRSRV YLHTLAESIC KLIFPEFERL NLALQRTLAK
110 120 130 140 150
HKIKENRKSL EREDFEKIVV DQAIAAGVPV EIIKESLGEE LFKICYEEDE
160 170 180 190 200
YILGVVGGTL KDFLNSFSTL LKQSSHCQEA EKKGRFEDAS ILCLDKDPDV
210 220 230 240 250
LYVYYFFPKR ITSLILPGII KAAARILYET EVEVSSTPSR FHQDCREFVD
260 270 280 290 300
QPCELYSVHI RSARPHPPPG KPVSSLVIPA SLFCKTFPFH FMLDRDMSIL
310 320 330 340 350
QLGHGIRRLM SRRDVQGKPH FDEYFEILTP KISQTFSGIM TMLNMQFLVR
360 370 380 390 400
VRRWDNSMKK SSRVMDLKGQ MIYMVESSSI LFLGSPCVDR LEDFTGRGLY
410 420 430 440 450
LSDIPIHNAL RDVVLIGEQA RAQDGLKKRL GKLKATLEQA HQALEEEKRK
460 470 480 490 500
TVDLLCSIFP SEVARQLWQG HAVQAKRFGN VTMLFSDIVG FTAICSQCSP
510 520 530 540 550
LQVITMLNAL YTRFDRQCGE LDVYKVETIG DAYCVAGGLH KESDTHAVQI
560 570 580 590 600
ALMALKMMEL SHEVVSPHGE PIKMRIGLHS GSVFAGVVGV KMPRYCLFGN
610 620 630 640 650
NVTLANKFES CSVPRKINVS PTTYRLLKDC PGFVFTPRSR EELPPNFPSD
660 670 680 690
IPGICHFLEA YQQGTTSKPW FQKKDVEEAN ANFLGKASGI D
Length:691
Mass (Da):77,533
Last modified:February 1, 1991 - v1
Checksum:i5D1FE4D2204E8683
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54014 mRNA. Translation: CAA37960.1.
PIRiS10713. OYBO77.
RefSeqiNP_786972.1. NM_175778.2.
XP_005217697.1. XM_005217640.2.
XP_005217698.1. XM_005217641.2.
XP_005217699.1. XM_005217642.2.
XP_005217700.1. XM_005217643.2.
XP_010812116.1. XM_010813814.1.
XP_010812117.1. XM_010813815.1.
UniGeneiBt.4480.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54014 mRNA. Translation: CAA37960.1.
PIRiS10713. OYBO77.
RefSeqiNP_786972.1. NM_175778.2.
XP_005217697.1. XM_005217640.2.
XP_005217698.1. XM_005217641.2.
XP_005217699.1. XM_005217642.2.
XP_005217700.1. XM_005217643.2.
XP_010812116.1. XM_010813814.1.
XP_010812117.1. XM_010813815.1.
UniGeneiBt.4480.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWNmodel-A472-628[»]
ProteinModelPortaliP19687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019398.

Proteomic databases

PRIDEiP19687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2982.

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG106603.
InParanoidiP19687.
KOiK12318.
OMAiSEIPGIC.
OrthoDBiEOG7VX8Z6.
TreeFamiTF351403.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20805268.

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

  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: April 1, 2015
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

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.