SSY3_ARATH
ID SSY3_ARATH Reviewed; 1042 AA.
AC F4IAG2; Q1WAB7; Q306T0; Q9SAA5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Starch synthase 3, chloroplastic/amyloplastic;
DE Short=AtSS3;
DE EC=2.4.1.21;
DE AltName: Full=Soluble starch synthase III;
DE Flags: Precursor;
GN Name=SS3; OrderedLocusNames=At1g11720; ORFNames=F25C20.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-1042, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15908598; DOI=10.1104/pp.105.060319;
RA Zhang X., Myers A.M., James M.G.;
RT "Mutations affecting starch synthase III in Arabidopsis alter leaf starch
RT structure and increase the rate of starch synthesis.";
RL Plant Physiol. 138:663-674(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-1042 AND 595-1042.
RC STRAIN=cv. Columbia;
RX PubMed=18260645; DOI=10.1021/bi702418h;
RA Valdez H.A., Busi M.V., Wayllace N.Z., Parisi G., Ugalde R.A.,
RA Gomez-Casati D.F.;
RT "Role of the N-terminal starch-binding domains in the kinetic properties of
RT starch synthase III from Arabidopsis thaliana.";
RL Biochemistry 47:3026-3032(2008).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17217470; DOI=10.1111/j.1365-313x.2006.02968.x;
RA Roldan I., Wattebled F., Mercedes Lucas M., Delvalle D., Planchot V.,
RA Jimenez S., Perez R., Ball S., D'Hulst C., Merida A.;
RT "The phenotype of soluble starch synthase IV defective mutants of
RT Arabidopsis thaliana suggests a novel function of elongation enzymes in the
RT control of starch granule formation.";
RL Plant J. 49:492-504(2007).
RN [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=18811962; DOI=10.1186/1471-2229-8-96;
RA Zhang X., Szydlowski N., Delvalle D., D'Hulst C., James M.G., Myers A.M.;
RT "Overlapping functions of the starch synthases SSII and SSIII in
RT amylopectin biosynthesis in Arabidopsis.";
RL BMC Plant Biol. 8:96-96(2008).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=19666739; DOI=10.1105/tpc.109.066522;
RA Szydlowski N., Ragel P., Raynaud S., Lucas M.M., Roldan I., Montero M.,
RA Munoz F.J., Ovecka M., Bahaji A., Planchot V., Pozueta-Romero J.,
RA D'Hulst C., Merida A.;
RT "Starch granule initiation in Arabidopsis requires the presence of either
RT class IV or class III starch synthases.";
RL Plant Cell 21:2443-2457(2009).
CC -!- FUNCTION: Involved in the synthesis of glycan chains within amylopectin
CC in leaves. May play a regulatory role in the control of starch
CC accumulation in plastids. {ECO:0000269|PubMed:15908598,
CC ECO:0000269|PubMed:18811962, ECO:0000269|PubMed:19666739}.
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 -!- INTERACTION:
CC F4IAG2; F4IAG2: SS3; NbExp=4; IntAct=EBI-7661720, EBI-7661720;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4IAG2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC {ECO:0000269|PubMed:17217470}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants accumulate increased levels of starch and
CC have starch granules with alterated morphology.
CC {ECO:0000269|PubMed:15908598, ECO:0000269|PubMed:17217470}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30251.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AC007296; AAD30251.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE28774.1; -; Genomic_DNA.
DR EMBL; DQ241810; ABB46391.1; -; mRNA.
DR EMBL; EF636491; ABU96740.1; -; mRNA.
DR EMBL; DQ415727; ABD77100.1; -; mRNA.
DR PIR; H86250; H86250.
DR RefSeq; NP_172637.2; NM_101044.3. [F4IAG2-1]
DR AlphaFoldDB; F4IAG2; -.
DR SMR; F4IAG2; -.
DR BioGRID; 22956; 2.
DR MINT; F4IAG2; -.
DR STRING; 3702.AT1G11720.2; -.
DR CAZy; CBM53; Carbohydrate-Binding Module Family 53.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR iPTMnet; F4IAG2; -.
DR PaxDb; F4IAG2; -.
DR PRIDE; F4IAG2; -.
DR ProMEX; F4IAG2; -.
DR ProteomicsDB; 228259; -. [F4IAG2-1]
DR EnsemblPlants; AT1G11720.1; AT1G11720.1; AT1G11720. [F4IAG2-1]
DR GeneID; 837716; -.
DR Gramene; AT1G11720.1; AT1G11720.1; AT1G11720. [F4IAG2-1]
DR KEGG; ath:AT1G11720; -.
DR Araport; AT1G11720; -.
DR eggNOG; ENOG502QQTU; Eukaryota.
DR HOGENOM; CLU_002856_0_0_1; -.
DR InParanoid; F4IAG2; -.
DR OMA; DCLNFSH; -.
DR BRENDA; 2.4.1.21; 399.
DR UniPathway; UPA00152; -.
DR PRO; PR:F4IAG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IAG2; baseline and differential.
DR Genevisible; F4IAG2; AT.
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:0042802; F:identical protein binding; IPI:IntAct.
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; IGI:UniProtKB.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR005085; CBM25.
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 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..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..1042
FT /note="Starch synthase 3, chloroplastic/amyloplastic"
FT /id="PRO_0000419770"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..302
FT /evidence="ECO:0000255"
FT BINDING 608
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250"
FT CONFLICT 741
FT /note="G -> D (in Ref. 3; ABB46391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="R -> C (in Ref. 3; ABB46391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1042 AA; 118512 MW; C0481F694FCDC7D2 CRC64;
MISYFLNQDF SRKKQGRMAA SGPKSSGPRG FGRRTTVGSA QKRTQKKNGE KDSNATSTAT
NEVSGISKLP AAKVDVQKQS SVVLNERNVL DRSDIEDGSD RLDKKTTDDD DLLEQKLKLE
RENLRRKEIE TLAAENLARG DRMFVYPVIV KPDEDIEVFL NRNLSTLNNE PDVLIMGAFN
EWRWKSFTRR LEKTWIHEDW LSCLLHIPKE AYKMDFVFFN GQSVYDNNDS KDFCVEIKGG
MDKVDFENFL LEEKLREQEK LAKEEAERER QKEEKRRIEA QKAAIEADRA QAKAETQKRR
ELLQPAIKKA VVSAENVWYI EPSDFKAEDT VKLYYNKRSG PLTNSKELWL HGGFNNWVDG
LSIVVKLVNA ELKDVDPKSG NWWFAEVVVP GGALVIDWVF ADGPPKGAFL YDNNGYQDFH
ALVPQKLPEE LYWLEEENMI FRKLQEDRRL KEEVMRAKME KTARLKAETK ERTLKKFLLS
QKDVVYTEPL EIQAGNPVTV LYNPANTVLN GKPEVWFRGS FNRWTHRLGP LPPQKMEATD
DESSHVKTTA KVPLDAYMMD FVFSEKEDGG IFDNKNGLDY HLPVVGGISK EPPLHIVHIA
VEMAPIAKVG GLGDVVTSLS RAVQELNHNV DIVFPKYDCI KHNFVKDLQF NRSYHWGGTE
IKVWHGKVEG LSVYFLDPQN GLFQRGCVYG CADDAGRFGF FCHAALEFLL QGGFHPDILH
CHDWSSAPVS WLFKDHYTQY GLIKTRIVFT IHNLEFGANA IGKAMTFADK ATTVSPTYAK
EVAGNSVISA HLYKFHGIIN GIDPDIWDPY NDNFIPVPYT SENVVEGKRA AKEELQNRLG
LKSADFPVVG IITRLTHQKG IHLIKHAIWR TLERNGQVVL LGSAPDPRIQ NDFVNLANQL
HSSHGDRARL VLTYDEPLSH LIYAGADFIL VPSIFEPCGL TQLIAMRYGA VPVVRKTGGL
FDTVFDVDHD KERAQAQVLE PNGFSFDGAD APGVDYALNR AISAWYDGRE WFNSLCKTVM
EQDWSWNRPA LEYLELYHSA RK
