ID   SSY21_ORYSJ             Reviewed;         749 AA.
AC   Q7XE48; Q109M8; Q94F83;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Soluble starch synthase 2-1, chloroplastic/amyloplastic;
DE            EC=2.4.1.21;
DE   AltName: Full=Soluble starch synthase II-1;
DE   Flags: Precursor;
GN   Name=SSII-1; OrderedLocusNames=Os10g0437600, LOC_Os10g30156;
GN   ORFNames=OSJNBb0016G17.2;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=14740212; DOI=10.1007/s00425-003-1189-y;
RA   Jiang H.W., Dian W.M., Liu F., Wu P.;
RT   "Molecular cloning and expression analysis of three genes encoding starch
RT   synthase II in rice.";
RL   Planta 218:1062-1070(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX   PubMed=15232694; DOI=10.1007/s00425-004-1314-6;
RA   Hirose T., Terao T.;
RT   "A comprehensive expression analysis of the starch synthase gene family in
RT   rice (Oryza sativa L.).";
RL   Planta 220:9-16(2004).
CC   -!- FUNCTION: May be involved in starch synthesis in endosperm amyloplasts
CC       and contribute to the deposition of transient starch in chloroplasts of
CC       leaves. {ECO:0000269|PubMed:14740212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast. Plastid, chloroplast.
CC       Note=Amyloplast or chloroplast, granule-bound and soluble.
CC   -!- TISSUE SPECIFICITY: Expressed in endosperm, leaves, and weakly in
CC       roots. {ECO:0000269|PubMed:14740212, ECO:0000269|PubMed:15232694}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing caryopsis at 1 to 20 days
CC       after flowering. Expressed in the pericarp and endosperm at 5 and 5 to
CC       10 days after flowering respectively. {ECO:0000269|PubMed:14740212}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; AF383878; AAK64284.1; -; mRNA.
DR   EMBL; DP000086; ABG66094.1; -; Genomic_DNA.
DR   EMBL; AP008216; BAF26592.1; -; Genomic_DNA.
DR   EMBL; AP014966; BAT11006.1; -; Genomic_DNA.
DR   RefSeq; XP_015614561.1; XM_015759075.1.
DR   AlphaFoldDB; Q7XE48; -.
DR   SMR; Q7XE48; -.
DR   STRING; 39947.Q7XE48; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   PaxDb; 39947-Q7XE48; -.
DR   EnsemblPlants; Os10t0437600-01; Os10t0437600-01; Os10g0437600.
DR   GeneID; 4348711; -.
DR   Gramene; Os10t0437600-01; Os10t0437600-01; Os10g0437600.
DR   KEGG; osa:4348711; -.
DR   eggNOG; ENOG502QT35; Eukaryota.
DR   HOGENOM; CLU_009583_31_1_1; -.
DR   InParanoid; Q7XE48; -.
DR   OMA; CYSPGCH; -.
DR   OrthoDB; 141134at2759; -.
DR   PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   ExpressionAtlas; Q7XE48; baseline and differential.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   HAMAP; MF_00484; Glycogen_synth; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR011835; GS/SS.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   NCBIfam; TIGR02095; glgA; 1.
DR   PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR45825:SF2; STARCH SYNTHASE 2, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   Genevisible; Q7XE48; OS.
PE   2: Evidence at transcript level;
KW   Amyloplast; Chloroplast; Glycosyltransferase; Plastid; Reference proteome;
KW   Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..44
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..749
FT                   /note="Soluble starch synthase 2-1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011139"
FT   BINDING         272
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        215
FT                   /note="R -> H (in Ref. 1; AAK64284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="A -> S (in Ref. 1; AAK64284)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   749 AA;  83312 MW;  59E0B829E39509A3 CRC64;
     MAAAAVSSLL APSGSCYSPG CHSCWGPGPG GGRRLPSPRR RPITAAARPT WAVPRRSRLE
     WGRVEAQNSG ARTSCRAALQ WLSSTARSHV NVGYGSPLVF PGLTKPGSSR CLCVVGMVGN
     AGNQVGDDSD DGIKVTNEKL RAVIRKSKEV LEIHRNLLEK ISASERKKIT SIIEDSSIYN
     EQDPFGQRDS SFYHLDEVPD DDEFSYDLQM YLDRRPDQSE VVATQDYEAQ LSQISEMGQS
     VAEGTSDDPS ASAAVDLINI ILVAAECAPW SKTGGLGDVA GALPKALARR GHRVMVVVPM
     YKNYAEPQQL GEPRRYQVAG QDMEVIYYHA YIDGVDFVFI DNPIFHHVEN DIYGGDRTDI
     LKRMVLLCKA AIEVPWYVPC GGYCYGDGNL VFLANDWHTA LLPVYLKAYY HDNGFMIYAR
     SVLVIHNIAH QGRGPLDDFS YLDLPVDYMD LFKLYDPFGG DHLNIFAAGI KAADRLLTVS
     HGYAWELKTA EGGWGLHGII NESDWKFQGI VNGIDTTDWN PRCDIHLKSD GYTNYSLETV
     QAGKQQCKAA LQKELGLPVR GDVPVIAFIG RLDHQKGVDL IAEAMPWIAG QDVQLIMLGT
     GRQDLEDTLR RLESQHYDRV RGWVGFSIRL AHRMTAGADI LLMPSRFEPC GLNQLYAMMY
     GTVPVVHAVG GLRDTVEHYN PYEESGLGWT FEKAEANRLI DALGHCLNTY RNYRTSWEGL
     QKRGMMQDLS WDNAAKLYEE VLLAAKYQW
//