GLGS2_ORYSJ
ID GLGS2_ORYSJ Reviewed; 514 AA.
AC P15280; A3BS75; A8ASG3; Q0J698; Q7EZW3; Q84QT8; Q94JM6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit 2, chloroplastic/amyloplastic/cytosolic {ECO:0000305};
DE Short=OsAGPS2 {ECO:0000303|PubMed:17406793};
DE Short=OsAPS2 {ECO:0000303|PubMed:15821022};
DE EC=2.7.7.27 {ECO:0000269|PubMed:24747952};
DE AltName: Full=ADP-glucose pyrophosphorylase AGPS2 {ECO:0000305};
DE AltName: Full=ADP-glucose synthase AGPS2 {ECO:0000305};
DE AltName: Full=AGPase B;
DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE AltName: Full=OsAGPS2a {ECO:0000303|PubMed:17406793};
DE AltName: Full=OsAGPS2b {ECO:0000303|PubMed:17406793};
DE Flags: Precursor;
GN Name=AGPS2 {ECO:0000303|PubMed:17406793};
GN Synonyms=APS2 {ECO:0000303|PubMed:15821022};
GN OrderedLocusNames=Os08g0345800 {ECO:0000312|EMBL:BAT05035.1},
GN LOC_Os08g25734 {ECO:0000305};
GN ORFNames=OsJ_26991 {ECO:0000312|EMBL:EAZ42414.1},
GN P0410E11.123-1 {ECO:0000312|EMBL:BAC75439.1},
GN P0410E11.123-2 {ECO:0000312|EMBL:BAD01700.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Endosperm;
RX PubMed=2545704; DOI=10.1016/s0021-9258(18)63847-5;
RA Anderson J.M., Hnilo J., Larson R., Okita T.W., Morell M., Preiss J.;
RT "The encoded primary sequence of a rice seed ADP-glucose pyrophosphorylase
RT subunit and its homology to the bacterial enzyme.";
RL J. Biol. Chem. 264:12238-12242(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Endosperm;
RX PubMed=1847888; DOI=10.1016/0378-1119(91)90052-d;
RA Anderson J.M., Larsen R., Laudencia D., Kim W.T., Morrow D., Okita T.W.,
RA Preiss J.;
RT "Molecular characterization of the gene encoding a rice endosperm-specific
RT ADPglucose pyrophosphorylase subunit and its developmental pattern of
RT transcription.";
RL Gene 97:199-205(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Nipponbare;
RA Satozawa T., Akagi H., Sakamoto M., Kawasaki T., Shimada H., Fujimura T.;
RT "Isolation of cDNAs for a large and small subunits of an ADP-glucose
RT pyrophosphorylase in rice: structure, expression and evolution.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of ADP-glucose pyrophosphorylase genes in rice seeds.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H., Lee G.S., Lee J.S., Hahn J.H., Kim C.K., Lee J.H., Kim Y.H.;
RT "Oryza sativa japonica group ADP-glucose pyrophosphorylase mRNA.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [8]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 204-293.
RA Lee D.-S., Hur Y.;
RT "Expression and regulation of genes involved in carbohydrate metabolism in
RT rice.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15821022; DOI=10.1093/pcp/pci101;
RA Akihiro T., Mizuno K., Fujimura T.;
RT "Gene expression of ADP-glucose pyrophosphorylase and starch contents in
RT rice cultured cells are cooperatively regulated by sucrose and ABA.";
RL Plant Cell Physiol. 46:937-946(2005).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17406793; DOI=10.1007/s11103-007-9153-z;
RA Lee S.K., Hwang S.K., Han M., Eom J.S., Kang H.G., Han Y., Choi S.B.,
RA Cho M.H., Bhoo S.H., An G., Hahn T.R., Okita T.W., Jeon J.S.;
RT "Identification of the ADP-glucose pyrophosphorylase isoforms essential for
RT starch synthesis in the leaf and seed endosperm of rice (Oryza sativa
RT L.).";
RL Plant Mol. Biol. 65:531-546(2007).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=24747952; DOI=10.1093/pcp/pcu057;
RA Tuncel A., Kawaguchi J., Ihara Y., Matsusaka H., Nishi A., Nakamura T.,
RA Kuhara S., Hirakawa H., Nakamura Y., Cakir B., Nagamine A., Okita T.W.,
RA Hwang S.K., Satoh H.;
RT "The rice endosperm ADP-glucose pyrophosphorylase large subunit is
RT essential for optimal catalysis and allosteric regulation of the
RT heterotetrameric enzyme.";
RL Plant Cell Physiol. 55:1169-1183(2014).
CC -!- FUNCTION: Involved in synthesis of starch. Catalyzes the synthesis of
CC ADP-glucose, a molecule that serves as an activated glycosyl donor for
CC alpha-1,4-glucan synthesis. The chloroplastic isoform 1 is essential
CC for starch synthesis in leaf chloroplasts and the cytosolic isoform 2
CC for synthesis in seed endosperm. {ECO:0000269|PubMed:17406793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:58601; EC=2.7.7.27;
CC Evidence={ECO:0000269|PubMed:24747952};
CC -!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by
CC orthophosphate. Allosteric regulation. Inhibited by inorganic phosphate
CC (Pi). {ECO:0000269|PubMed:24747952}.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer composed of two small and two large subunits.
CC {ECO:0000269|PubMed:24747952}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast
CC {ECO:0000269|PubMed:17406793}. Plastid, amyloplast
CC {ECO:0000305|PubMed:17406793}. Note=Found in the chloroplast in leaf.
CC Found in the plastid in the developing endosperm.
CC {ECO:0000305|PubMed:17406793}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:17406793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=OSAGPS2A {ECO:0000303|PubMed:17406793};
CC IsoId=P15280-1; Sequence=Displayed;
CC Name=2; Synonyms=OSAGPS2B {ECO:0000303|PubMed:17406793};
CC IsoId=P15280-2; Sequence=VSP_017511;
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:15821022}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 1 to 15 days
CC after flowering (DAF). {ECO:0000269|PubMed:15821022}.
CC -!- DISRUPTION PHENOTYPE: Shrunken seed endosperm due to a strong reduction
CC in starch synthesis. {ECO:0000269|PubMed:17406793}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33890.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA33891.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J04960; AAA33890.1; ALT_FRAME; mRNA.
DR EMBL; M31616; AAA33891.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D83539; BAF80188.1; -; mRNA.
DR EMBL; EF122437; ABL74524.1; -; mRNA.
DR EMBL; FJ940194; ADB84616.1; -; mRNA.
DR EMBL; AP004459; BAC75439.1; -; Genomic_DNA.
DR EMBL; AP004459; BAD01700.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23517.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05034.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05035.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ42414.1; -; Genomic_DNA.
DR EMBL; AK071826; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK103906; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF378188; AAK54859.1; -; mRNA.
DR PIR; A34318; A34318.
DR PIR; JU0444; JU0444.
DR RefSeq; XP_015650970.1; XM_015795484.1. [P15280-1]
DR RefSeq; XP_015650971.1; XM_015795485.1. [P15280-2]
DR AlphaFoldDB; P15280; -.
DR SMR; P15280; -.
DR BioGRID; 814376; 1.
DR STRING; 4530.OS08T0345800-02; -.
DR PaxDb; P15280; -.
DR PRIDE; P15280; -.
DR EnsemblPlants; Os08t0345800-01; Os08t0345800-01; Os08g0345800. [P15280-2]
DR EnsemblPlants; Os08t0345800-02; Os08t0345800-02; Os08g0345800. [P15280-1]
DR GeneID; 4345339; -.
DR Gramene; Os08t0345800-01; Os08t0345800-01; Os08g0345800. [P15280-2]
DR Gramene; Os08t0345800-02; Os08t0345800-02; Os08g0345800. [P15280-1]
DR KEGG; osa:4345339; -.
DR eggNOG; KOG1322; Eukaryota.
DR InParanoid; P15280; -.
DR OMA; QEWDVDE; -.
DR OrthoDB; 806744at2759; -.
DR BRENDA; 2.7.7.27; 4460.
DR PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; P15280; baseline and differential.
DR Genevisible; P15280; OS.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005982; P:starch metabolic process; IEP:Gramene.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR02091; glgC; 1.
DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Alternative splicing; Amyloplast; ATP-binding;
KW Chloroplast; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW Plastid; Reference proteome; Starch biosynthesis; Transferase;
KW Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..514
FT /note="Glucose-1-phosphate adenylyltransferase small
FT subunit 2, chloroplastic/amyloplastic/cytosolic"
FT /id="PRO_0000011154"
FT REGION 35..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..82
FT /note="MAMAAAMGVASPYHAAHAAASTSCDSLRLLVAEGRPRRPRGVASSSSSSSSA
FT GRRRRPLVFSPRAVSDSKSSQTCLDPDAST -> MNVLASKIFPSRSNVASEQQQSKRE
FT KATIDDAKNSSKNKNLDRSVDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764,
FT ECO:0000303|PubMed:2545704, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.4"
FT /id="VSP_017511"
FT CONFLICT 144
FT /note="L -> P (in Ref. 1; AAA33890)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> V (in Ref. 2; AAA33891)"
FT /evidence="ECO:0000305"
FT CONFLICT P15280-2:16
FT /note="A -> V (in Ref. 1; AAA33890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 56104 MW; 821C1931321C7E52 CRC64;
MAMAAAMGVA SPYHAAHAAA STSCDSLRLL VAEGRPRRPR GVASSSSSSS SAGRRRRPLV
FSPRAVSDSK SSQTCLDPDA STSVLGIILG GGAGTRLYPL TKKRAKPAVP LGANYRLIDI
PVSNCLNSNI SKIYVLTQFN SASLNRHLSR AYGNNIGGYK NEGFVEVLAA QQSPDNPNWF
QGTADAVRQY LWLFEEHNVM EFLILAGDHL YRMDYEKFIQ AHRETDSDIT VAALPMDEKR
ATAFGLMKID EEGRIVEFAE KPKGEQLKAM MVDTTILGLD DVRAKEMPYI ASMGIYVISK
NVMLQLLREQ FPGANDFGSE VIPGATNIGM RVQAYLYDGY WEDIGTIEAF YNANLGITKK
PVPDFSFYDR SAPIYTQPRH LPPSKVLDAD VTDSVIGEGC VIKNCKIHHS VVGLRSCISE
GAIIEDSLLM GADYYETEAD KKLLGEKGGI PIGIGKNCHI RRAIIDKNAR IGDNVKIINV
DNVQEAARET DGYFIKSGIV TVIKDALLPS GTVI
