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Glucose-1-phosphate adenylyltransferase small subunit 2, chloroplastic/amyloplastic/cytosolic (OsAGPS2) (OsAPS2) (EC 2.7.7.27) (ADP-glucose pyrophosphorylase AGPS2) (ADP-glucose synthase AGPS2) (AGPase B) (Alpha-D-glucose-1-phosphate adenyl transferase) (OsAGPS2a) (OsAGPS2b)

 GLGS2_ORYSJ             Reviewed;         514 AA.
P15280; A3BS75; A8ASG3; Q0J698; Q7EZW3; Q84QT8; Q94JM6;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 4.
12-SEP-2018, entry version 143.
RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit 2, chloroplastic/amyloplastic/cytosolic {ECO:0000305};
Short=OsAGPS2 {ECO:0000303|PubMed:17406793};
Short=OsAPS2 {ECO:0000303|PubMed:15821022};
EC=2.7.7.27 {ECO:0000269|PubMed:24747952};
AltName: Full=ADP-glucose pyrophosphorylase AGPS2 {ECO:0000305};
AltName: Full=ADP-glucose synthase AGPS2 {ECO:0000305};
AltName: Full=AGPase B;
AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
AltName: Full=OsAGPS2a {ECO:0000303|PubMed:17406793};
AltName: Full=OsAGPS2b {ECO:0000303|PubMed:17406793};
Flags: Precursor;
Name=AGPS2 {ECO:0000303|PubMed:17406793};
Synonyms=APS2 {ECO:0000303|PubMed:15821022};
OrderedLocusNames=Os08g0345800 {ECO:0000312|EMBL:BAT05035.1},
LOC_Os08g25734 {ECO:0000305};
ORFNames=OsJ_26991 {ECO:0000312|EMBL:EAZ42414.1},
P0410E11.123-1 {ECO:0000312|EMBL:BAC75439.1},
P0410E11.123-2 {ECO:0000312|EMBL:BAD01700.1};
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Endosperm;
PubMed=2545704;
Anderson J.M., Hnilo J., Larson R., Okita T.W., Morell M., Preiss J.;
"The encoded primary sequence of a rice seed ADP-glucose
pyrophosphorylase subunit and its homology to the bacterial enzyme.";
J. Biol. Chem. 264:12238-12242(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Endosperm;
PubMed=1847888; DOI=10.1016/0378-1119(91)90052-D;
Anderson J.M., Larsen R., Laudencia D., Kim W.T., Morrow D.,
Okita T.W., Preiss J.;
"Molecular characterization of the gene encoding a rice endosperm-
specific ADPglucose pyrophosphorylase subunit and its developmental
pattern of transcription.";
Gene 97:199-205(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Nipponbare;
Satozawa T., Akagi H., Sakamoto M., Kawasaki T., Shimada H.,
Fujimura T.;
"Isolation of cDNAs for a large and small subunits of an ADP-glucose
pyrophosphorylase in rice: structure, expression and evolution.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
Yoon U.H., Kim Y.H.;
"Molecular cloning of ADP-glucose pyrophosphorylase genes in rice
seeds.";
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
Yoon U.H., Lee G.S., Lee J.S., Hahn J.H., Kim C.K., Lee J.H.,
Kim Y.H.;
"Oryza sativa japonica group ADP-glucose pyrophosphorylase mRNA.";
Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[7]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[8]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Nipponbare;
PubMed=12869764; DOI=10.1126/science.1081288;
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from
japonica rice.";
Science 301:376-379(2003).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 204-293.
Lee D.-S., Hur Y.;
"Expression and regulation of genes involved in carbohydrate
metabolism in rice.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[12]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15821022; DOI=10.1093/pcp/pci101;
Akihiro T., Mizuno K., Fujimura T.;
"Gene expression of ADP-glucose pyrophosphorylase and starch contents
in rice cultured cells are cooperatively regulated by sucrose and
ABA.";
Plant Cell Physiol. 46:937-946(2005).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=17406793; DOI=10.1007/s11103-007-9153-z;
Lee S.K., Hwang S.K., Han M., Eom J.S., Kang H.G., Han Y., Choi S.B.,
Cho M.H., Bhoo S.H., An G., Hahn T.R., Okita T.W., Jeon J.S.;
"Identification of the ADP-glucose pyrophosphorylase isoforms
essential for starch synthesis in the leaf and seed endosperm of rice
(Oryza sativa L.).";
Plant Mol. Biol. 65:531-546(2007).
[14]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
PubMed=24747952; DOI=10.1093/pcp/pcu057;
Tuncel A., Kawaguchi J., Ihara Y., Matsusaka H., Nishi A.,
Nakamura T., Kuhara S., Hirakawa H., Nakamura Y., Cakir B.,
Nagamine A., Okita T.W., Hwang S.K., Satoh H.;
"The rice endosperm ADP-glucose pyrophosphorylase large subunit is
essential for optimal catalysis and allosteric regulation of the
heterotetrameric enzyme.";
Plant Cell Physiol. 55:1169-1183(2014).
-!- FUNCTION: Involved in synthesis of starch. Catalyzes the synthesis
of ADP-glucose, a molecule that serves as an activated glycosyl
donor for alpha-1,4-glucan synthesis. The chloroplastic isoform 1
is essential for starch synthesis in leaf chloroplasts and the
cytosolic isoform 2 for synthesis in seed endosperm.
{ECO:0000269|PubMed:17406793}.
-!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate =
diphosphate + ADP-glucose. {ECO:0000269|PubMed:24747952}.
-!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by
orthophosphate. Allosteric regulation. Inhibited by inorganic
phosphate (Pi). {ECO:0000269|PubMed:24747952}.
-!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
-!- SUBUNIT: Heterotetramer composed of two small and two large
subunits. {ECO:0000269|PubMed:24747952}.
-!- SUBCELLULAR LOCATION: Isoform 1: Plastid, chloroplast
{ECO:0000269|PubMed:17406793}. Plastid, amyloplast
{ECO:0000305|PubMed:17406793}. Note=Found in the chloroplast in
leaf. Found in the plastid in the developing endosperm.
{ECO:0000305|PubMed:17406793}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol
{ECO:0000269|PubMed:17406793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=OSAGPS2A {ECO:0000303|PubMed:17406793};
IsoId=P15280-1; Sequence=Displayed;
Name=2; Synonyms=OSAGPS2B {ECO:0000303|PubMed:17406793};
IsoId=P15280-2; Sequence=VSP_017511;
Note=Ref.1 (AAA33890) sequence is in conflict in position:
16:A->V. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in leaves.
{ECO:0000269|PubMed:15821022}.
-!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 1 to 15
days after flowering (DAF). {ECO:0000269|PubMed:15821022}.
-!- DISRUPTION PHENOTYPE: Shrunken seed endosperm due to a strong
reduction in starch synthesis. {ECO:0000269|PubMed:17406793}.
-!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
adenylyltransferase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA33890.1; Type=Frameshift; Positions=509; Evidence={ECO:0000305};
Sequence=AAA33891.1; Type=Frameshift; Positions=509; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J04960; AAA33890.1; ALT_FRAME; mRNA.
EMBL; M31616; AAA33891.1; ALT_FRAME; Genomic_DNA.
EMBL; D83539; BAF80188.1; -; mRNA.
EMBL; EF122437; ABL74524.1; -; mRNA.
EMBL; FJ940194; ADB84616.1; -; mRNA.
EMBL; AP004459; BAC75439.1; -; Genomic_DNA.
EMBL; AP004459; BAD01700.1; -; Genomic_DNA.
EMBL; AP008214; BAF23517.1; -; Genomic_DNA.
EMBL; AP014964; BAT05034.1; -; Genomic_DNA.
EMBL; AP014964; BAT05035.1; -; Genomic_DNA.
EMBL; CM000145; EAZ42414.1; -; Genomic_DNA.
EMBL; AK071826; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK103906; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF378188; AAK54859.1; -; mRNA.
PIR; A34318; A34318.
PIR; JU0444; JU0444.
RefSeq; XP_015650970.1; XM_015795484.1. [P15280-1]
RefSeq; XP_015650971.1; XM_015795485.1. [P15280-2]
UniGene; Os.178; -.
ProteinModelPortal; P15280; -.
SMR; P15280; -.
STRING; 39947.LOC_Os08g25734.1; -.
PaxDb; P15280; -.
EnsemblPlants; Os08t0345800-01; Os08t0345800-01; Os08g0345800. [P15280-2]
EnsemblPlants; Os08t0345800-02; Os08t0345800-02; Os08g0345800. [P15280-1]
GeneID; 4345339; -.
Gramene; Os08t0345800-01; Os08t0345800-01; Os08g0345800. [P15280-2]
Gramene; Os08t0345800-02; Os08t0345800-02; Os08g0345800. [P15280-1]
KEGG; osa:4345339; -.
eggNOG; ENOG410IMYM; Eukaryota.
eggNOG; COG0448; LUCA.
HOGENOM; HOG000278604; -.
InParanoid; P15280; -.
KO; K00975; -.
OMA; PAQMRTG; -.
OrthoDB; EOG093606WL; -.
BRENDA; 2.7.7.27; 4460.
UniPathway; UPA00152; -.
Proteomes; UP000059680; Chromosome 8.
ExpressionAtlas; P15280; differential.
Genevisible; P15280; OS.
GO; GO:0009501; C:amyloplast; IEP:Gramene.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0005982; P:starch metabolic process; IEP:Gramene.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR011831; ADP-Glc_PPase.
InterPro; IPR005836; ADP_Glu_pyroP_CS.
InterPro; IPR005835; NTP_transferase_dom.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00483; NTP_transferase; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 2.
TIGRFAMs; TIGR02091; glgC; 1.
PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
1: Evidence at protein level;
Allosteric enzyme; Alternative splicing; Amyloplast; ATP-binding;
Chloroplast; Complete proteome; Cytoplasm; Nucleotide-binding;
Nucleotidyltransferase; Plastid; Reference proteome;
Starch biosynthesis; Transferase; Transit peptide.
TRANSIT 1 64 Chloroplast. {ECO:0000255}.
CHAIN 65 514 Glucose-1-phosphate adenylyltransferase
small subunit 2,
chloroplastic/amyloplastic/cytosolic.
/FTId=PRO_0000011154.
VAR_SEQ 1 82 MAMAAAMGVASPYHAAHAAASTSCDSLRLLVAEGRPRRPRG
VASSSSSSSSAGRRRRPLVFSPRAVSDSKSSQTCLDPDAST
-> MNVLASKIFPSRSNVASEQQQSKREKATIDDAKNSSKN
KNLDRSVDE (in isoform 2).
{ECO:0000303|PubMed:12869764,
ECO:0000303|PubMed:2545704,
ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
/FTId=VSP_017511.
CONFLICT 144 144 L -> P (in Ref. 1; AAA33890).
{ECO:0000305}.
CONFLICT 169 169 A -> V (in Ref. 2; AAA33891).
{ECO:0000305}.
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


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