SSY21_ORYSJ
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 03-AUG-2022, entry version 111.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 4530.OS10T0437600-00; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; Q7XE48; -.
DR PRIDE; Q7XE48; -.
DR EnsemblPlants; Os10t0437600-00; Os10t0437600-00; Os10g0437600.
DR GeneID; 4348711; -.
DR Gramene; Os10t0437600-00; Os10t0437600-00; Os10g0437600.
DR KEGG; osa:4348711; -.
DR eggNOG; ENOG502QT35; Eukaryota.
DR HOGENOM; CLU_009583_31_1_1; -.
DR InParanoid; Q7XE48; -.
DR OMA; DYAEPQQ; -.
DR OrthoDB; 732319at2759; -.
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 Genevisible; Q7XE48; OS.
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 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 Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02095; glgA; 1.
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