SSY3A_ORYSJ
ID SSY3A_ORYSJ Reviewed; 1875 AA.
AC A0A0P0XCU3; Q6Z1D6;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Soluble starch synthase 3a, chloroplastic/amyloplastic {ECO:0000305};
DE EC=2.4.1.21 {ECO:0000305};
DE AltName: Full=Protein FLOURY ENDOSPERM 5 {ECO:0000303|PubMed:17297616};
DE AltName: Full=Soluble starch synthase IIIa {ECO:0000303|PubMed:17297616};
DE Short=OsSSIIIa {ECO:0000303|PubMed:17297616};
DE Flags: Precursor;
GN Name=SSIIIA {ECO:0000303|PubMed:17297616};
GN Synonyms=FLO5 {ECO:0000303|PubMed:17297616}, SS3A {ECO:0000305},
GN SSIII-2 {ECO:0000303|PubMed:15232694};
GN OrderedLocusNames=Os08g0191433 {ECO:0000312|EMBL:BAT04174.1},
GN LOC_Os08g09230 {ECO:0000305};
GN ORFNames=OSJNBa0056O06.4-1 {ECO:0000312|EMBL:BAD05589.1};
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 [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 [2]
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 [3]
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15642712; DOI=10.1093/jxb/eri065;
RA Dian W., Jiang H., Wu P.;
RT "Evolution and expression analysis of starch synthase III and IV in rice.";
RL J. Exp. Bot. 56:623-632(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Dongjin;
RX PubMed=17297616; DOI=10.1007/s00299-007-0309-8;
RA Ryoo N., Yu C., Park C.S., Baik M.Y., Park I.M., Cho M.H., Bhoo S.H.,
RA An G., Hahn T.R., Jeon J.S.;
RT "Knockout of a starch synthase gene OsSSIIIa/Flo5 causes white-core floury
RT endosperm in rice (Oryza sativa L.).";
RL Plant Cell Rep. 26:1083-1095(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17586688; DOI=10.1104/pp.107.102533;
RA Fujita N., Yoshida M., Kondo T., Saito K., Utsumi Y., Tokunaga T.,
RA Nishi A., Satoh H., Park J.H., Jane J.L., Miyao A., Hirochika H.,
RA Nakamura Y.;
RT "Characterization of SSIIIa-deficient mutants of rice: the function of
RT SSIIIa and pleiotropic effects by SSIIIa deficiency in the rice
RT endosperm.";
RL Plant Physiol. 144:2009-2023(2007).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=21595523; DOI=10.1139/g11-010;
RA Zhang G., Cheng Z., Zhang X., Guo X., Su N., Jiang L., Mao L., Wan J.;
RT "Double repression of soluble starch synthase genes SSIIa and SSIIIa in
RT rice (Oryza sativa L.) uncovers interactive effects on the physicochemical
RT properties of starch.";
RL Genome 54:448-459(2011).
RN [10]
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).
RN [11]
RP BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RX PubMed=27791174; DOI=10.1073/pnas.1615104113;
RA Zhou H., Wang L., Liu G., Meng X., Jing Y., Shu X., Kong X., Sun J., Yu H.,
RA Smith S.M., Wu D., Li J.;
RT "Critical roles of soluble starch synthase SSIIIa and granule-bound starch
RT synthase Waxy in synthesizing resistant starch in rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:12844-12849(2016).
CC -!- FUNCTION: Involved in starch synthesis in endosperm amyloplasts
CC (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523,
CC PubMed:21730357). Plays an important role in the elongation of
CC amylopectin B chains (PubMed:17297616, PubMed:17586688,
CC PubMed:21417378, PubMed:21595523, PubMed:21730357).
CC {ECO:0000269|PubMed:17297616, ECO:0000269|PubMed:17586688,
CC ECO:0000269|PubMed:21417378, ECO:0000269|PubMed:21595523,
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 {ECO:0000305}. Plastid,
CC amyloplast {ECO:0000305}. Note=Amyloplast or chloroplast, soluble.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A0P0XCU3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A0P0XCU3-2; Sequence=VSP_059965, VSP_059966;
CC -!- TISSUE SPECIFICITY: Expressed in the endosperm.
CC {ECO:0000269|PubMed:15232694, ECO:0000269|PubMed:15642712}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing caryopsis from 5 to 15
CC days after flowering. {ECO:0000269|PubMed:15232694,
CC ECO:0000269|PubMed:15642712}.
CC -!- DISRUPTION PHENOTYPE: White-core floury endosperm (PubMed:17297616,
CC PubMed:27791174). Increased content of resistant starch (RS)
CC (PubMed:27791174). Endosperm containing increased levels of amylose
CC (PubMed:17297616, PubMed:21417378). Reduced content of long amylopectin
CC chains with a degree of polymerization (DP) of 30 or greater
CC (PubMed:17297616, PubMed:17586688). Reduced content of amylopectin
CC chains with a DP of 6 to 8 and a DP of 16 to 20, but increased content
CC of chains with a DP of 9 to 15 and a DP of 22 to 29 (PubMed:17297616,
CC PubMed:17586688). Decrease in average length of amylopectin chains
CC (PubMed:21417378). {ECO:0000269|PubMed:17297616,
CC ECO:0000269|PubMed:17586688, ECO:0000269|PubMed:21417378,
CC ECO:0000269|PubMed:27791174}.
CC -!- BIOTECHNOLOGY: Selection of varieties with reduced SSIIIA activity may
CC be a tool to increase resistant starch (RS) content of rice grain.
CC {ECO:0000269|PubMed:27791174}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD05589.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAT04174.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005441; BAD05589.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; BAT04174.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015650668.1; XM_015795182.1. [A0A0P0XCU3-2]
DR RefSeq; XP_015650669.1; XM_015795183.1. [A0A0P0XCU3-2]
DR RefSeq; XP_015650670.1; XM_015795184.1. [A0A0P0XCU3-2]
DR RefSeq; XP_015650671.1; XM_015795185.1. [A0A0P0XCU3-2]
DR AlphaFoldDB; A0A0P0XCU3; -.
DR SMR; A0A0P0XCU3; -.
DR STRING; 4530.OS08T0191433-00; -.
DR CAZy; CBM53; Carbohydrate-Binding Module Family 53.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; A0A0P0XCU3; -.
DR GeneID; 9268758; -.
DR KEGG; osa:9268758; -.
DR eggNOG; ENOG502QQTU; Eukaryota.
DR HOGENOM; CLU_002856_1_0_1; -.
DR OrthoDB; 409403at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
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:2001070; F:starch binding; 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 Gene3D; 2.60.40.10; -; 2.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR011835; GS/SS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR Pfam; PF16760; CBM53; 3.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SMART; SM01066; CBM_25; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Amyloplast; Chloroplast; Coiled coil;
KW Glycosyltransferase; Plastid; Reference proteome; Starch biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..1875
FT /note="Soluble starch synthase 3a,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000445783"
FT REGION 1014..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1007..1065
FT /evidence="ECO:0000255"
FT VAR_SEQ 1746..1788
FT /note="QQSLLGLKPAVGSTPSAKGSWSKTGPGTGLPWTTLNCTIQLTN -> AISSW
FT FEARGWFHSLCKRVMEQDWSWNRPALDYIELYHSAHKF (in isoform 2)"
FT /id="VSP_059965"
FT VAR_SEQ 1789..1875
FT /note="Missing (in isoform 2)"
FT /id="VSP_059966"
SQ SEQUENCE 1875 AA; 210833 MW; 07E6DBD2B16A23F0 CRC64;
MEMALRPQSL LCPRSRLKVV IRPASSASGG GLAQYFLMTR RYTGSRIVRC MVSSSDCPNR
KAKRTISLHT EVASSRGYAP RIAAESSIQE REHINSDEET FDTYNRLLRN ESTEWKKLDT
TEVDLSQDVS SSSMRKVDAT DEAKLDILED DLPRNLLNGV TMGEVDMLDE AGAEDDVFEV
DLSALHNSTV GKMDAVNEVG TENDLFEVDL SALHSAAVGK VDVVDGAKAK EDLFEMDSLA
LHSVTMGKVD AINAAGAEGD KFEVDLSALA SNNSMIEAVN VMDEAKAIED TLEVDLSGNA
TSSSTYGEVK FEVDSLGNTS STVMYGPADG AYEPRSDEVT FKVDSSENAS NNVMYGRADV
VDESWADEGI FEVDFFTNAS SGAEYGKVDV VDEAKTDDFT FEIDSLEKDS NNKMHGKAHM
VDEAWDDEAI FEVDLFGNAS SIPIYGEVNV LDEARADDGK FEVDLLGNTS SNSTHEEVDV
VDEAQTGEAT FEVDLLGNAL SSAIYKEVPV MGGAQDDEVD VDFSINASIT ETEKEADAVD
EARVEDETFD MDLVGKQISI DSMNDDVVEE GTKHHRYPML SSAFIEVKTI HETPVSLKPE
LMSVVMDQEQ DKPISSVYQQ EGSIFNLHAE NQSTVDFHER EQMAITFDKQ KESVAKLSKE
DQQTAGLPEQ NMSFDGVHRK SQSIIGLPFQ HQSIVSSPEK YRSIVGFHGQ NQSIISSHKQ
DKSIVGVPKK IQSIVGSTKH DDSIVGFRKQ DRSIVSVPEQ KQSIVGFHKQ DLSIVAVSEQ
NLSIVAIPRE SQSKQISIVR RHDPLHLKEV ETKDRDGISK KSGGDDDLPH MLFEEELSQV
EDVARAIAYK KQHEVDVISL TPDIQESPQD NIDPQELRRM LQELADQNCS MGNKLFVFPE
AVKANSTIDV YLNRNLSALA NEPDVHIKGA FNSWRWRPFT ERLHKSELSG DWWSCKLHIP
KEAYRLDFVF FNGRLVYDNN DSNDFVLQVE STMDEDSFEE FLVEEKKREL ERVATEEAER
RRHAEEQQRM GEQRAAEQAA REQAKKEIEL KKNKLQNLLS SARTHVDNLW HIEPSTYRQG
DTVRLYYNRN SRPLMHSTEI WMHGGCNSWT DGLSIVERLV ECDDENGDWW YANVHIPEKA
FVLDWVFADG PPGNARNYDN NGRQDFHAIL PNAMTNEEYW VEEENCIYTR LLHEIREREE
AIKIKVEKRA KMKSEMKEKT MRMFLLSQKH IVYTEPLEIR AGTTVDVLYN PSNTVLNGKP
EVWFRWSFNR WMHPSGVLPP KKMVKTEDGC HLKATVSVPS DAYMMDFVFS ESEEGGIYDN
RNGTDYHIPV SGSNAKEPPI HIVHIAVEMA PIAKVGGLAD VVTSLSRAIQ ELGHHVEVIL
PKYNFMNQSN VKNLHVRQSF SLGGTEIKVW FGLVEDLSVY FLEPQNGMFG GGWVYGGNDA
GRFGLFCQSA LEFLLQSGSS PHIIHCHDWS SAPVAWLYKE HYAESRLATA RIIFTIHNLE
FGAHFIGKAM TYCDKATTVS HTYSKEVAGH GAIAPHRGKF YGILNGIDPD IWDPYTDNFI
PMHYTSENVV EGKNAAKRAL QQRFGLQQTD VPIVGIITRL TAQKGIHLIK HALHRTLERN
GQVVLLGSAP DPRIQSDFCR LADSLHGENH GRVRLCLTYD EPLSHLIYAG SDFILVPSIF
EPCGLTQLVA MRYGSIPIVR KTGGLYDTVF DVDHDKDRAR VLGLEPNGFS FDGADCNGVD
YALNRQQSLL GLKPAVGSTP SAKGSWSKTG PGTGLPWTTL NCTIQLTNFE APIQRWQEKA
SIGRYYKLNE TWLKVKIFYL SCRYKLTQTW FKVKIFYLSY TYICRIKTLY SMHKQLWEYV
SAMFPILSFN YEYLI
