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   27-MAR-2024, entry version 77.
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};
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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.F4IAG2; -.
DR   CAZy; CBM53; Carbohydrate-Binding Module Family 53.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   iPTMnet; F4IAG2; -.
DR   PaxDb; 3702-AT1G11720-2; -.
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   TAIR; AT1G11720; SS3.
DR   eggNOG; ENOG502QQTU; Eukaryota.
DR   HOGENOM; CLU_002856_0_0_1; -.
DR   InParanoid; F4IAG2; -.
DR   OMA; MFWAGCI; -.
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   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   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR46083; -; 1.
DR   PANTHER; PTHR46083:SF5; STARCH SYNTHASE 3, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF16760; CBM53; 3.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   SMART; SM01066; CBM_25; 3.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   Genevisible; F4IAG2; AT.
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
//