ID   SSY1_ORYSJ              Reviewed;         641 AA.
AC   Q0DEC8; B7F2B2; O24206; Q40739; Q5WA90; Q7Y044;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Soluble starch synthase 1, chloroplastic/amyloplastic {ECO:0000305};
DE            EC=2.4.1.21 {ECO:0000305};
DE   AltName: Full=Starch synthase I {ECO:0000303|PubMed:20018713};
DE   Flags: Precursor;
GN   Name=SS1 {ECO:0000303|PubMed:20018713};
GN   Synonyms=SSS1 {ECO:0000303|PubMed:7610165};
GN   OrderedLocusNames=Os06g0160700 {ECO:0000312|EMBL:BAS96282.1},
GN   LOC_Os06g06560 {ECO:0000305};
GN   ORFNames=P0681F10.13 {ECO:0000312|EMBL:BAD67625.1};
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], PROTEIN SEQUENCE OF 114-131, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Seed;
RX   PubMed=7518089; DOI=10.1104/pp.103.2.565;
RA   Baba T., Nishihara M., Mizuno K., Kawasaki T., Shimada H., Kobayashi E.,
RA   Ohnishi S., Tanaka K., Arai Y.;
RT   "Identification, cDNA cloning, and gene expression of soluble starch
RT   synthase in rice (Oryza sativa L.) immature seeds.";
RL   Plant Physiol. 103:565-573(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7610165; DOI=10.1104/pp.108.2.677;
RA   Tanaka K., Ohnishi S., Kishimoto N., Kawasaki T., Baba T.;
RT   "Structure, organization and chromosomal location of the gene encoding a
RT   form of rice soluble starch synthase.";
RL   Plant Physiol. 108:677-683(1995).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nanjing 37;
RA   Junwang X., Zhen Z.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [7]
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   [8]
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   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16443699; DOI=10.1104/pp.105.071845;
RA   Fujita N., Yoshida M., Asakura N., Ohdan T., Miyao A., Hirochika H.,
RA   Nakamura Y.;
RT   "Function and characterization of starch synthase I using mutants in
RT   rice.";
RL   Plant Physiol. 140:1070-1084(2006).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21417378; DOI=10.1021/bm200019q;
RA   Hanashiro I., Higuchi T., Aihara S., Nakamura Y., Fujita N.;
RT   "Structures of starches from rice mutants deficient in the starch synthase
RT   isozyme SSI or SSIIIa.";
RL   Biomacromolecules 12:1621-1628(2011).
RN   [11]
RP   FUNCTION.
RX   PubMed=21730357; DOI=10.1093/jxb/err125;
RA   Fujita N., Satoh R., Hayashi A., Kodama M., Itoh R., Aihara S.,
RA   Nakamura Y.;
RT   "Starch biosynthesis in rice endosperm requires the presence of either
RT   starch synthase I or IIIa.";
RL   J. Exp. Bot. 62:4819-4831(2011).
CC   -!- FUNCTION: Involved in starch synthesis in endosperm amyloplasts
CC       (PubMed:16443699, PubMed:21417378, PubMed:21730357). Plays a role in
CC       the elongation of amylopectin chains (PubMed:16443699, PubMed:21417378,
CC       PubMed:21730357). Synthesizes preferentially amylopectin chains with a
CC       degree of polymerization (DP) of 7 to 11 by elongating chains with a DP
CC       of 4 to 7 (PubMed:16443699). Generates distincly chains with a DP of 8
CC       to 12 chains from short chains with a DP of 6 to 7 (PubMed:16443699).
CC       {ECO:0000269|PubMed:16443699, ECO:0000269|PubMed:21417378,
CC       ECO:0000269|PubMed:21730357}.
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         Evidence={ECO:0000305};
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC       Note=Amyloplast or chloroplast, soluble. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Leaves and immature seeds.
CC       {ECO:0000269|PubMed:7518089}.
CC   -!- DISRUPTION PHENOTYPE: Decrease in average length of amylopectin chains
CC       (PubMed:21417378). Reduced content of amylopectin chains with a degree
CC       of polymerization (DP) of 8 to 12, but increased content of chains with
CC       a DP of 6 to 7 and a DP of 16 to 19 (PubMed:16443699).
CC       {ECO:0000269|PubMed:16443699, ECO:0000269|PubMed:21417378}.
CC   -!- MISCELLANEOUS: Three forms of soluble starch synthase were purified:
CC       RSS1, RSS2 and RSS3. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD49850.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA03739.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA07396.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D16202; BAA03739.1; ALT_FRAME; mRNA.
DR   EMBL; D38221; BAA07396.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; GQ150941; ACY56156.1; -; Genomic_DNA.
DR   EMBL; GQ150946; ACY56161.1; -; Genomic_DNA.
DR   EMBL; GQ150942; ACY56157.1; -; Genomic_DNA.
DR   EMBL; GQ150943; ACY56158.1; -; Genomic_DNA.
DR   EMBL; GQ150944; ACY56159.1; -; Genomic_DNA.
DR   EMBL; GQ150945; ACY56160.1; -; Genomic_DNA.
DR   EMBL; AF165890; AAD49850.1; ALT_FRAME; mRNA.
DR   EMBL; AB026295; BAD67625.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF18795.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS96282.1; -; Genomic_DNA.
DR   EMBL; AK109458; BAG98759.1; -; mRNA.
DR   PIR; JQ2322; JQ2322.
DR   RefSeq; XP_015644241.1; XM_015788755.1.
DR   AlphaFoldDB; Q0DEC8; -.
DR   SMR; Q0DEC8; -.
DR   STRING; 39947.Q0DEC8; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   PaxDb; 39947-Q0DEC8; -.
DR   EnsemblPlants; Os06t0160700-01; Os06t0160700-01; Os06g0160700.
DR   GeneID; 9269493; -.
DR   Gramene; Os06t0160700-01; Os06t0160700-01; Os06g0160700.
DR   KEGG; osa:9269493; -.
DR   eggNOG; ENOG502QTWM; Eukaryota.
DR   HOGENOM; CLU_009583_18_2_1; -.
DR   InParanoid; Q0DEC8; -.
DR   OMA; TWCPWYM; -.
DR   OrthoDB; 141134at2759; -.
DR   PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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:0010021; P:amylopectin biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009960; P:endosperm development; IMP:UniProtKB.
DR   GO; GO:0019252; P:starch biosynthetic process; IMP:UniProtKB.
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:SF11; STARCH SYNTHASE 1, 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; Q0DEC8; OS.
PE   1: Evidence at protein level;
KW   Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW   Plastid; Reference proteome; Starch biosynthesis; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..113
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:7518089"
FT   CHAIN           114..641
FT                   /note="Soluble starch synthase 1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011138"
FT   REGION          62..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..90
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         147
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        46..47
FT                   /note="QR -> HG (in Ref. 1; BAA03739)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   641 AA;  70952 MW;  EF851A03C7349076 CRC64;
     MATAAGMGIG AACLVAPQVR PGRRLRLQRV RRRCVAELSR DGGSAQRPLA PAPLVKQPVL
     PTFLVPTSTP PAPTQSPAPA PTPPPLPDSG VGEIEPDLEG LTEDSIDKTI FVASEQESEI
     MDVKEQAQAK VTRSVVFVTG EASPYAKSGG LGDVCGSLPI ALALRGHRVM VVMPRYMNGA
     LNKNFANAFY TEKHIKIPCF GGEHEVTFFH EYRDSVDWVF VDHPSYHRPG NLYGDNFGAF
     GDNQFRYTLL CYAACEAPLI LELGGYIYGQ KCMFVVNDWH ASLVPVLLAA KYRPYGVYRD
     ARSVLVIHNL AHQGVEPAST YPDLGLPPEW YGALEWVFPE WARRHALDKG EAVNFLKGAV
     VTADRIVTVS QGYSWEVTTA EGGQGLNELL SSRKSVLNGI VNGIDINDWN PSTDKFLPYH
     YSVDDLSGKA KCKAELQKEL GLPIRPDVPL IGFIGRLDYQ KGIDLIKLAI PDLMRDNIQF
     VMLGSGDPGF EGWMRSTESG YRDKFRGWVG FSVPVSHRIT AGCDILLMPS RFEPCGLNQL
     YAMQYGTVPV VHGTGGLRDT VENFNPFAEK GEQGTGWAFS PLTIEKMLWA LRMAISTYRE
     HKSSWEGLMK RGMSSDFTWD HAASQYEQIF EWAFMDQPYV M
//