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Q0DJ33 (GPA1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein alpha-1 subunit

Short name=GP-alpha-1
Alternative name(s):
Protein Dwarf1
Gene names
Name:GPA1
Synonyms:D1, GA1, RGA1
Ordered Locus Names:Os05g0333200, LOC_Os05g26890
ORF Names:OJ1005_D04.15, OSJNBa0049D13.1
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.

Domain

The helical domain (69-189) is required for self-activation By similarity.

Sequence similarities

Belongs to the G-alpha family.

Sequence caution

The sequence BAF17140.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Myristate
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway, coupled to S1P second messenger

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

L-phenylalanine biosynthetic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

blue light signaling pathway

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cell death

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cellular response to abscisic acid stimulus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

gibberellic acid mediated signaling pathway

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

negative regulation of abscisic acid-activated signaling pathway

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

negative regulation of catalytic activity

Inferred from Biological aspect of Ancestor. Source: GOC

positive regulation of abscisic acid-activated signaling pathway

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

reactive oxygen species metabolic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

regulation of cell proliferation

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to glucose

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to low fluence blue light stimulus by blue low-fluence system

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

seed germination

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

thylakoid membrane organization

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

tyrosine biosynthetic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasmodesma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

G-protein coupled receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTPase inhibitor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

channel regulator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LOC_Os03g46650Q406872EBI-1100098,EBI-1100119

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 380379Guanine nucleotide-binding protein alpha-1 subunit
PRO_0000203622

Regions

Nucleotide binding46 – 538GTP By similarity
Nucleotide binding188 – 1947GTP By similarity
Nucleotide binding219 – 2235GTP By similarity
Nucleotide binding288 – 2914GTP By similarity

Sites

Metal binding531Magnesium By similarity
Metal binding1941Magnesium By similarity
Binding site3561GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity
Lipidation51S-palmitoyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0DJ33 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 4EEFAEDAB4463612

FASTA38044,206
        10         20         30         40         50         60 
MGSSCSRSHS LSEAETTKNA KSADIDRRIL QETKAEQHIH KLLLLGAGES GKSTIFKQIK 

        70         80         90        100        110        120 
LLFQTGFDEA ELRSYTSVIH ANVYQTIKIL YEGAKELSQV ESDSSKYVIS PDNQEIGEKL 

       130        140        150        160        170        180 
SDIDGRLDYP LLNKELVLDV KRLWQDPAIQ ETYLRGSILQ LPDCAQYFME NLDRLAEAGY 

       190        200        210        220        230        240 
VPTKEDVLYA RVRTNGVVQI QFSPVGENKR GGEVYRLYDV GGQRNERRKW IHLFEGVNAV 

       250        260        270        280        290        300 
IFCAAISEYD QMLFEDETKN RMMETKELFD WVLKQRCFEK TSFILFLNKF DIFEKKIQKV 

       310        320        330        340        350        360 
PLSVCEWFKD YQPIAPGKQE VEHAYEFVKK KFEELYFQSS KPDRVDRVFK IYRTTALDQK 

       370        380 
LVKKTFKLID ESMRRSREGT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a cDNA for the alpha subunit of a G protein from rice."
Ishikawa A., Tsubouchi H., Iwasaki Y., Asahi T.
Plant Cell Physiol. 36:353-359(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Nipponbare.
Tissue: Leaf.
[2]"A fine physical map of the rice chromosome 5."
Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J., Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F., Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.
Mol. Genet. Genomics 274:337-345(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[4]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38232 mRNA. Translation: BAA07405.1.
AC117264 Genomic DNA. Translation: AAV43839.1.
AC144739 Genomic DNA. Translation: AAW57778.2.
AP008211 Genomic DNA. Translation: BAF17140.1. Different initiation.
RefSeqNP_001055226.1. NM_001061761.1.
UniGeneOs.5302.

3D structure databases

ProteinModelPortalQ0DJ33.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ0DJ33. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4338448.
KEGGosa:4338448.

Organism-specific databases

GrameneQ0DJ33.

Phylogenomic databases

eggNOGNOG322962.
KOK04640.
ProtClustDBCLSN2683295.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
IPR002976. Plant_Gprotein_alpha.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PTHR10218:SF25. PTHR10218:SF25. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR01242. GPROTEINAPLT.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Entry information

Entry nameGPA1_ORYSJ
AccessionPrimary (citable) accession number: Q0DJ33
Secondary accession number(s): P49083 expand/collapse secondary AC list , Q2HNY6, Q43604, Q5KQF9, Q5W732
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations