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Protein

Starch synthase 3, chloroplastic/amyloplastic

Gene

SS3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the synthesis of glycan chains within amylopectin in leaves. May play a regulatory role in the control of starch accumulation in plastids.3 Publications

Catalytic activityi

ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1).

Pathway: starch biosynthesis

This protein is involved in the pathway starch biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway starch biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei608 – 6081ADP-glucoseBy similarity

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • starch binding Source: InterPro
  • starch synthase activity Source: UniProtKB-EC

GO - Biological processi

  • amylopectin biosynthetic process Source: UniProtKB
  • starch biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Starch biosynthesis

Enzyme and pathway databases

BRENDAi2.4.1.21. 399.
UniPathwayiUPA00152.

Names & Taxonomyi

Protein namesi
Recommended name:
Starch synthase 3, chloroplastic/amyloplastic (EC:2.4.1.21)
Short name:
AtSS3
Alternative name(s):
Soluble starch synthase III
Gene namesi
Name:SS3
Ordered Locus Names:At1g11720
ORF Names:F25C20.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G11720.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Amyloplast, Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but mutant plants accumulate increased levels of starch and have starch granules with alterated morphology.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4444ChloroplastSequence AnalysisAdd
BLAST
Chaini45 – 1042998Starch synthase 3, chloroplastic/amyloplasticPRO_0000419770Add
BLAST

Proteomic databases

PRIDEiF4IAG2.
ProMEXiF4IAG2.

Expressioni

Tissue specificityi

Expressed in leaves and flowers.1 Publication

Gene expression databases

ExpressionAtlasiF4IAG2. baseline and differential.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-7661720,EBI-7661720

Protein-protein interaction databases

BioGridi22956. 1 interaction.
MINTiMINT-7299396.
STRINGi3702.AT1G11720.2.

Structurei

3D structure databases

ProteinModelPortaliF4IAG2.
SMRiF4IAG2. Positions 594-1038.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili247 – 30256Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

HOGENOMiHOG000294940.
InParanoidiF4IAG2.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR005085. CBM_fam25.
IPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF03423. CBM_25. 3 hits.
PF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
SMARTiSM01066. CBM_25. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: F4IAG2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MISYFLNQDF SRKKQGRMAA SGPKSSGPRG FGRRTTVGSA QKRTQKKNGE
60 70 80 90 100
KDSNATSTAT NEVSGISKLP AAKVDVQKQS SVVLNERNVL DRSDIEDGSD
110 120 130 140 150
RLDKKTTDDD DLLEQKLKLE RENLRRKEIE TLAAENLARG DRMFVYPVIV
160 170 180 190 200
KPDEDIEVFL NRNLSTLNNE PDVLIMGAFN EWRWKSFTRR LEKTWIHEDW
210 220 230 240 250
LSCLLHIPKE AYKMDFVFFN GQSVYDNNDS KDFCVEIKGG MDKVDFENFL
260 270 280 290 300
LEEKLREQEK LAKEEAERER QKEEKRRIEA QKAAIEADRA QAKAETQKRR
310 320 330 340 350
ELLQPAIKKA VVSAENVWYI EPSDFKAEDT VKLYYNKRSG PLTNSKELWL
360 370 380 390 400
HGGFNNWVDG LSIVVKLVNA ELKDVDPKSG NWWFAEVVVP GGALVIDWVF
410 420 430 440 450
ADGPPKGAFL YDNNGYQDFH ALVPQKLPEE LYWLEEENMI FRKLQEDRRL
460 470 480 490 500
KEEVMRAKME KTARLKAETK ERTLKKFLLS QKDVVYTEPL EIQAGNPVTV
510 520 530 540 550
LYNPANTVLN GKPEVWFRGS FNRWTHRLGP LPPQKMEATD DESSHVKTTA
560 570 580 590 600
KVPLDAYMMD FVFSEKEDGG IFDNKNGLDY HLPVVGGISK EPPLHIVHIA
610 620 630 640 650
VEMAPIAKVG GLGDVVTSLS RAVQELNHNV DIVFPKYDCI KHNFVKDLQF
660 670 680 690 700
NRSYHWGGTE IKVWHGKVEG LSVYFLDPQN GLFQRGCVYG CADDAGRFGF
710 720 730 740 750
FCHAALEFLL QGGFHPDILH CHDWSSAPVS WLFKDHYTQY GLIKTRIVFT
760 770 780 790 800
IHNLEFGANA IGKAMTFADK ATTVSPTYAK EVAGNSVISA HLYKFHGIIN
810 820 830 840 850
GIDPDIWDPY NDNFIPVPYT SENVVEGKRA AKEELQNRLG LKSADFPVVG
860 870 880 890 900
IITRLTHQKG IHLIKHAIWR TLERNGQVVL LGSAPDPRIQ NDFVNLANQL
910 920 930 940 950
HSSHGDRARL VLTYDEPLSH LIYAGADFIL VPSIFEPCGL TQLIAMRYGA
960 970 980 990 1000
VPVVRKTGGL FDTVFDVDHD KERAQAQVLE PNGFSFDGAD APGVDYALNR
1010 1020 1030 1040
AISAWYDGRE WFNSLCKTVM EQDWSWNRPA LEYLELYHSA RK
Length:1,042
Mass (Da):118,512
Last modified:June 28, 2011 - v1
Checksum:iC0481F694FCDC7D2
GO

Sequence cautioni

The sequence AAD30251.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti741 – 7411G → D in ABB46391 (PubMed:15908598).Curated
Sequence conflicti1041 – 10411R → C in ABB46391 (PubMed:15908598).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007296 Genomic DNA. Translation: AAD30251.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE28774.1.
DQ241810 mRNA. Translation: ABB46391.1.
EF636491 mRNA. Translation: ABU96740.1.
DQ415727 mRNA. Translation: ABD77100.1.
PIRiH86250.
RefSeqiNP_172637.2. NM_101044.3. [F4IAG2-1]
UniGeneiAt.42115.

Genome annotation databases

EnsemblPlantsiAT1G11720.1; AT1G11720.1; AT1G11720. [F4IAG2-1]
GeneIDi837716.
KEGGiath:AT1G11720.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007296 Genomic DNA. Translation: AAD30251.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE28774.1.
DQ241810 mRNA. Translation: ABB46391.1.
EF636491 mRNA. Translation: ABU96740.1.
DQ415727 mRNA. Translation: ABD77100.1.
PIRiH86250.
RefSeqiNP_172637.2. NM_101044.3. [F4IAG2-1]
UniGeneiAt.42115.

3D structure databases

ProteinModelPortaliF4IAG2.
SMRiF4IAG2. Positions 594-1038.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22956. 1 interaction.
MINTiMINT-7299396.
STRINGi3702.AT1G11720.2.

Proteomic databases

PRIDEiF4IAG2.
ProMEXiF4IAG2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G11720.1; AT1G11720.1; AT1G11720. [F4IAG2-1]
GeneIDi837716.
KEGGiath:AT1G11720.

Organism-specific databases

TAIRiAT1G11720.

Phylogenomic databases

HOGENOMiHOG000294940.
InParanoidiF4IAG2.

Enzyme and pathway databases

UniPathwayiUPA00152.
BRENDAi2.4.1.21. 399.

Miscellaneous databases

PROiF4IAG2.

Gene expression databases

ExpressionAtlasiF4IAG2. baseline and differential.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR005085. CBM_fam25.
IPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF03423. CBM_25. 3 hits.
PF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
SMARTiSM01066. CBM_25. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Mutations affecting starch synthase III in Arabidopsis alter leaf starch structure and increase the rate of starch synthesis."
    Zhang X., Myers A.M., James M.G.
    Plant Physiol. 138:663-674(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-1042, FUNCTION, DISRUPTION PHENOTYPE.
  4. "Role of the N-terminal starch-binding domains in the kinetic properties of starch synthase III from Arabidopsis thaliana."
    Valdez H.A., Busi M.V., Wayllace N.Z., Parisi G., Ugalde R.A., Gomez-Casati D.F.
    Biochemistry 47:3026-3032(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-1042 AND 595-1042.
    Strain: cv. Columbia.
  5. "The phenotype of soluble starch synthase IV defective mutants of Arabidopsis thaliana suggests a novel function of elongation enzymes in the control of starch granule formation."
    Roldan I., Wattebled F., Mercedes Lucas M., Delvalle D., Planchot V., Jimenez S., Perez R., Ball S., D'Hulst C., Merida A.
    Plant J. 49:492-504(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  6. "Overlapping functions of the starch synthases SSII and SSIII in amylopectin biosynthesis in Arabidopsis."
    Zhang X., Szydlowski N., Delvalle D., D'Hulst C., James M.G., Myers A.M.
    BMC Plant Biol. 8:96-96(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Columbia.
  7. "Starch granule initiation in Arabidopsis requires the presence of either class IV or class III starch synthases."
    Szydlowski N., Ragel P., Raynaud S., Lucas M.M., Roldan I., Montero M., Munoz F.J., Ovecka M., Bahaji A., Planchot V., Pozueta-Romero J., D'Hulst C., Merida A.
    Plant Cell 21:2443-2457(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Wassilewskija.

Entry informationi

Entry nameiSSY3_ARATH
AccessioniPrimary (citable) accession number: F4IAG2
Secondary accession number(s): Q1WAB7, Q306T0, Q9SAA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: June 28, 2011
Last modified: June 24, 2015
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.