GLGL2_ORYSJ
ID GLGL2_ORYSJ Reviewed; 518 AA.
AC Q7G065; B8XEC7; Q5VNT5; Q9ARI0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 2, cytosolic {ECO:0000305};
DE Short=OsAGPL2 {ECO:0000303|PubMed:17406793};
DE Short=OsAPL2 {ECO:0000303|PubMed:15821022};
DE EC=2.7.7.27 {ECO:0000269|PubMed:24747952};
DE AltName: Full=ADP-glucose pyrophosphorylase AGPL2 {ECO:0000305};
DE AltName: Full=ADP-glucose synthase AGPL2 {ECO:0000305};
DE AltName: Full=Protein FLOURY ENDOSPERM 6 {ECO:0000303|Ref.13};
DE AltName: Full=Protein GRAIN INCOMPLETE FILLING 2 {ECO:0000303|PubMed:27957808};
DE AltName: Full=Protein SHRUNKEN 1 {ECO:0000303|PubMed:24747952};
GN Name=AGPL2 {ECO:0000303|PubMed:17406793};
GN Synonyms=APL2 {ECO:0000303|PubMed:15821022}, FLO6 {ECO:0000303|Ref.13},
GN GIF2 {ECO:0000303|PubMed:27957808}, SHR1 {ECO:0000303|PubMed:24747952};
GN OrderedLocusNames=Os01g0633100 {ECO:0000312|EMBL:BAF05568.1},
GN LOC_Os01g44220 {ECO:0000305};
GN ORFNames=P0663E10.9 {ECO:0000312|EMBL:BAD68891.1};
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].
RX DOI=10.1016/S0168-9452(01)00431-9;
RA Sikka V.K., Choi S.-B., Kavakli I.H., Sakulsingharoj C., Gupta S., Ito H.,
RA Okita T.W.;
RT "Subcellular compartmentation and allosteric regulation of the rice
RT endosperm ADPglucose pyrophosphorylase.";
RL Plant Sci. 161:461-468(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20018713; DOI=10.1073/pnas.0912396106;
RA Tian Z., Qian Q., Liu Q., Yan M., Liu X., Yan C., Liu G., Gao Z., Tang S.,
RA Zeng D., Wang Y., Yu J., Gu M., Li J.;
RT "Allelic diversities in rice starch biosynthesis lead to a diverse array of
RT rice eating and cooking qualities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21760-21765(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen M., Lucas J.R., Bennetzen J.L.;
RT "Different rates of divergence in Sh2/A1-homologous regions of rice.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of the ADP-glucose pyrophosphorylase genes in rice.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ma K.-H., Lee G.-A., Gwag J.-G., Lee S.-Y., Lee J.-R., Kim T.-S.,
RA Park Y.-J.;
RT "Development of SNP-based CAPS and dCAPS markers in eight different genes
RT involved in starch biosynthesis in rice.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [7]
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 [8]
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 [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [12]
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 [13]
RP FUNCTION, AND MUTAGENESIS OF GLU-326.
RX DOI=10.1007/s11105-012-0435-5;
RA Zhang D., Wu J., Zhang Y., Shi C.;
RT "Phenotypic and candidate gene analysis of a new floury endosperm mutant
RT (osagpl2-3) in rice.";
RL Plant Mol. Biol. Rep. 30:1303-1312(2012).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF THR-139 AND ALA-171.
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).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27957808; DOI=10.1111/jipb.12510;
RA Wei X., Jiao G., Lin H., Sheng Z., Shao G., Xie L., Tang S., Xu Q., Hu P.;
RT "GRAIN INCOMPLETE FILLING 2 regulates grain filling and starch synthesis
RT during rice caryopsis development.";
RL J. Integr. Plant Biol. 59:134-153(2017).
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. Essential for starch synthesis in seed
CC endosperm (PubMed:17406793, Ref.13, PubMed:24747952, PubMed:27957808).
CC Is essential for both catalytic and allosteric regulatory properties of
CC the cytosolic heterotetramer enzyme (PubMed:24747952).
CC {ECO:0000269|PubMed:17406793, ECO:0000269|PubMed:24747952,
CC ECO:0000269|PubMed:27957808, ECO:0000269|Ref.13}.
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: Cytoplasm, cytosol {ECO:0000269|PubMed:17406793}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 10 to 20 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 ECO:0000269|PubMed:24747952, ECO:0000269|PubMed:27957808}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD68891.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY028314; AAK27727.1; -; mRNA.
DR EMBL; GQ150815; ACY56030.1; -; Genomic_DNA.
DR EMBL; GQ150816; ACY56031.1; -; Genomic_DNA.
DR EMBL; GQ150817; ACY56032.1; -; Genomic_DNA.
DR EMBL; GQ150818; ACY56033.1; -; Genomic_DNA.
DR EMBL; GQ150819; ACY56034.1; -; Genomic_DNA.
DR EMBL; GQ150820; ACY56035.1; -; Genomic_DNA.
DR EMBL; AF101045; AAF21886.1; -; Genomic_DNA.
DR EMBL; EU267956; ACA50478.1; -; mRNA.
DR EMBL; FJ235694; ACJ71331.1; -; Genomic_DNA.
DR EMBL; FJ235702; ACJ71339.1; -; Genomic_DNA.
DR EMBL; FJ235709; ACJ71346.1; -; Genomic_DNA.
DR EMBL; FJ235711; ACJ71348.1; -; Genomic_DNA.
DR EMBL; AP004317; BAD68891.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008207; BAF05568.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS73313.1; -; Genomic_DNA.
DR EMBL; AK071497; BAG92523.1; -; mRNA.
DR RefSeq; XP_015650361.1; XM_015794875.1.
DR RefSeq; XP_015650370.1; XM_015794884.1.
DR RefSeq; XP_015650378.1; XM_015794892.1.
DR RefSeq; XP_015650387.1; XM_015794901.1.
DR RefSeq; XP_015650395.1; XM_015794909.1.
DR RefSeq; XP_015650403.1; XM_015794917.1.
DR AlphaFoldDB; Q7G065; -.
DR SMR; Q7G065; -.
DR STRING; 4530.OS01T0633100-01; -.
DR PaxDb; Q7G065; -.
DR PRIDE; Q7G065; -.
DR EnsemblPlants; Os01t0633100-01; Os01t0633100-01; Os01g0633100.
DR GeneID; 4326594; -.
DR Gramene; Os01t0633100-01; Os01t0633100-01; Os01g0633100.
DR KEGG; osa:4326594; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; Q7G065; -.
DR OMA; HEAKKSP; -.
DR OrthoDB; 806744at2759; -.
DR BRENDA; 2.7.7.27; 4460.
DR PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR PlantReactome; R-OSA-9626305; Regulatory network of nutrient accumulation.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0010170; C:glucose-1-phosphate adenylyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IMP:UniProtKB.
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 PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Starch biosynthesis;
KW Transferase.
FT CHAIN 1..518
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 2, cytosolic"
FT /id="PRO_0000441125"
FT MUTAGEN 139
FT /note="T->V: Reduces activity more than 3-fold."
FT /evidence="ECO:0000269|PubMed:24747952"
FT MUTAGEN 171
FT /note="A->I: Reduces activity more than 3-fold."
FT /evidence="ECO:0000269|PubMed:24747952"
FT MUTAGEN 326
FT /note="E->K: In agpl2-3; white-core endosperm, and round
FT and loosely packed starch granules in the grains."
FT /evidence="ECO:0000269|Ref.13"
FT CONFLICT 2
FT /note="Q -> E (in Ref. 1; AAK27727)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="H -> R (in Ref. 5; ACJ71339)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..517
FT /note="DGTV -> HGPI (in Ref. 1; AAK27727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57575 MW; F32383BA0A3BBFAC CRC64;
MQFMMPLDTN ACAQPMRRAG EGAGTERLME RLNIGGMTQE KALRKRCFGD GVTGTARCVF
TSDADRDTPH LRTQSSRKNY ADASHVSAVI LGGGTGVQLF PLTSTRATPA VPVGGCYRLI
DIPMSNCFNS GINKIFVMTQ FNSASLNRHI HHTYLGGGIN FTDGSVQVLA ATQMPDEPAG
WFQGTADAIR KFMWILEDHY NQNNIEHVVI LCGDQLYRMN YMELVQKHVD DNADITISCA
PIDGSRASDY GLVKFDDSGR VIQFLEKPEG ADLESMKVDT SFLSYAIDDK QKYPYIASMG
IYVLKKDVLL DILKSKYAHL QDFGSEILPR AVLEHNVKAC VFTEYWEDIG TIKSFFDANL
ALTEQPPKFE FYDPKTPFFT SPRYLPPARL EKCKIKDAII SDGCSFSECT IEHSVIGISS
RVSIGCELKD TMMMGADQYE TEEETSKLLF EGKVPIGIGE NTKIRNCIID MNARIGRNVI
IANTQGVQES DHPEEGYYIR SGIVVILKNA TIKDGTVI
