GPCRDB: Swiss-Prot entry
ID GPA1_ARATH STANDARD; PRT; 383 AA.
AC P18064;
DT 01-NOV-1990 (Rel. 16, Created)
DT 01-NOV-1990 (Rel. 16, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Guanine nucleotide-binding protein alpha-1 subunit (GP-alpha-1).
GN Name=GPA1; OrderedLocusNames=At2g26300; ORFNames=T1D16.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=90251649; PubMed=2111018 [NCBI, ExPASy, EBI, Israel, Japan];
RA Ma H., Yanofsky M.F., Meyerowitz E.M.;
RT "Molecular cloning and characterization of GPA1, a G protein alpha
RT subunit gene from Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3821-3825(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=20083487; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=22954850; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INTERACTION WITH PRN1.
RX PubMed=12837948 [NCBI, ExPASy, EBI, Israel, Japan];
RA Lapik Y.R., Kaufman L.S.;
RT "The Arabidopsis cupin domain protein AtPirin1 interacts with the G
RT protein alpha-subunit GPA1 and regulates seed germination and early
RT seedling development.";
RL Plant Cell 15:1578-1590(2003).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as modulators or transducers in various transmembrane
CC signaling systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC gamma. The alpha chain contains the guanine nucleotide binding
CC site. Interacts with the pirin protein PRN1.
CC -!- INTERACTION:
CC O04714:GCR1; NbExp=2; IntAct=EBI-443890, EBI-443899;
CC -!- TISSUE SPECIFICITY: More abundant in roots and/or leaves.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; M32887; AAA32805.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AC004484; AAC14520.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY093966; AAM16227.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF385704; AAK60296.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; A35864; RGMUOA.
DR HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR IntAct; P18064; -.
DR InterPro; IPR001019; Gprotein_alpha.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR002976; GproteinA_plant.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00503; G-alpha; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01242; GPROTEINAPLT.
DR ProDom; PD000281; Gprotein_alpha; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR CMR; P18064.
DR BLOCKS; P18064.
DR ProtoNet; P18064.
DR ProtoMap; P18064.
DR PRESAGE; P18064.
DR DIP; P18064.
DR ModBase; P18064.
DR TAIR; At2g26300.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW ADP-ribosylation; GTP-binding; Transducer.
FT NP_BIND 45 52 GTP (By similarity).
FT NP_BIND 218 222 GTP (By similarity).
FT NP_BIND 287 290 GTP (By similarity).
FT MOD_RES 190 190 ADP-ribosylarginine (by cholera toxin).
SQ SEQUENCE 383 AA; 44546 MW; 46BF8650E067F968 CRC64;
MGLLCSRSRH HTEDTDENTQ AAEIERRIEQ EAKAEKHIRK LLLLGAGESG KSTIFKQIKL
LFQTGFDEGE LKSYVPVIHA NVYQTIKLLH DGTKEFAQNE TDSAKYMLSS ESIAIGEKLS
EIGGRLDYPR LTKDIAEGIE TLWKDPAIQE TCARGNELQV PDCTKYLMEN LKRLSDINYI
PTKEDVLYAR VRTTGVVEIQ FSPVGENKKS GEVYRLFDVG GQRNERRKWI HLFEGVTAVI
FCAAISEYDQ TLFEDEQKNR MMETKELFDW VLKQPCFEKT SFMLFLNKFD IFEKKVLDVP
LNVCEWFRDY QPVSSGKQEI EHAYEFVKKK FEELYYQNTA PDRVDRVFKI YRTTALDQKL
VKKTFKLVDE TLRRRNLLEA GLL
//