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F4IAG2 (SSY3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Starch synthase 3, chloroplastic/amyloplastic

Short name=AtSS3
EC=2.4.1.21
Alternative name(s):
Soluble starch synthase III
Gene names
Name:SS3
Ordered Locus Names:At1g11720
ORF Names:F25C20.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1042 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the synthesis of glycan chains within amylopectin in leaves. May play a regulatory role in the control of starch accumulation in plastids. Ref.3 Ref.6 Ref.7

Catalytic activity

ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1). HAMAP-Rule MF_00484

Pathway

Glycan biosynthesis; starch biosynthesis. HAMAP-Rule MF_00484

Subcellular location

Plastidchloroplast. Plastidamyloplast Probable HAMAP-Rule MF_00484.

Tissue specificity

Expressed in leaves and flowers. Ref.5

Disruption phenotype

No visible phenotype under normal growth conditions, but mutant plants accumulate increased levels of starch and have starch granules with alterated morphology. Ref.3 Ref.5

Sequence similarities

Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.

Sequence caution

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

Ontologies

Keywords
   Biological processStarch biosynthesis
   Cellular componentAmyloplast
Chloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Transit peptide
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamylopectin biosynthetic process

Inferred from genetic interaction Ref.6. Source: UniProtKB

starch biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentamyloplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 19968859. Source: IntAct

starch binding

Inferred from electronic annotation. Source: InterPro

starch synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-7661720,EBI-7661720

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: F4IAG2-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Chloroplast Potential
Chain45 – 1042998Starch synthase 3, chloroplastic/amyloplastic HAMAP-Rule MF_00484
PRO_0000419770

Regions

Coiled coil247 – 30256 Potential

Sites

Binding site6081ADP-glucose By similarity

Experimental info

Sequence conflict7411G → D in ABB46391. Ref.3
Sequence conflict10411R → C in ABB46391. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: C0481F694FCDC7D2

FASTA1,042118,512
        10         20         30         40         50         60 
MISYFLNQDF SRKKQGRMAA SGPKSSGPRG FGRRTTVGSA QKRTQKKNGE KDSNATSTAT 

        70         80         90        100        110        120 
NEVSGISKLP AAKVDVQKQS SVVLNERNVL DRSDIEDGSD RLDKKTTDDD DLLEQKLKLE 

       130        140        150        160        170        180 
RENLRRKEIE TLAAENLARG DRMFVYPVIV KPDEDIEVFL NRNLSTLNNE PDVLIMGAFN 

       190        200        210        220        230        240 
EWRWKSFTRR LEKTWIHEDW LSCLLHIPKE AYKMDFVFFN GQSVYDNNDS KDFCVEIKGG 

       250        260        270        280        290        300 
MDKVDFENFL LEEKLREQEK LAKEEAERER QKEEKRRIEA QKAAIEADRA QAKAETQKRR 

       310        320        330        340        350        360 
ELLQPAIKKA VVSAENVWYI EPSDFKAEDT VKLYYNKRSG PLTNSKELWL HGGFNNWVDG 

       370        380        390        400        410        420 
LSIVVKLVNA ELKDVDPKSG NWWFAEVVVP GGALVIDWVF ADGPPKGAFL YDNNGYQDFH 

       430        440        450        460        470        480 
ALVPQKLPEE LYWLEEENMI FRKLQEDRRL KEEVMRAKME KTARLKAETK ERTLKKFLLS 

       490        500        510        520        530        540 
QKDVVYTEPL EIQAGNPVTV LYNPANTVLN GKPEVWFRGS FNRWTHRLGP LPPQKMEATD 

       550        560        570        580        590        600 
DESSHVKTTA KVPLDAYMMD FVFSEKEDGG IFDNKNGLDY HLPVVGGISK EPPLHIVHIA 

       610        620        630        640        650        660 
VEMAPIAKVG GLGDVVTSLS RAVQELNHNV DIVFPKYDCI KHNFVKDLQF NRSYHWGGTE 

       670        680        690        700        710        720 
IKVWHGKVEG LSVYFLDPQN GLFQRGCVYG CADDAGRFGF FCHAALEFLL QGGFHPDILH 

       730        740        750        760        770        780 
CHDWSSAPVS WLFKDHYTQY GLIKTRIVFT IHNLEFGANA IGKAMTFADK ATTVSPTYAK 

       790        800        810        820        830        840 
EVAGNSVISA HLYKFHGIIN GIDPDIWDPY NDNFIPVPYT SENVVEGKRA AKEELQNRLG 

       850        860        870        880        890        900 
LKSADFPVVG IITRLTHQKG IHLIKHAIWR TLERNGQVVL LGSAPDPRIQ NDFVNLANQL 

       910        920        930        940        950        960 
HSSHGDRARL VLTYDEPLSH LIYAGADFIL VPSIFEPCGL TQLIAMRYGA VPVVRKTGGL 

       970        980        990       1000       1010       1020 
FDTVFDVDHD KERAQAQVLE PNGFSFDGAD APGVDYALNR AISAWYDGRE WFNSLCKTVM 

      1030       1040 
EQDWSWNRPA LEYLELYHSA RK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRH86250.
RefSeqNP_172637.2. NM_101044.3.
UniGeneAt.42115.

3D structure databases

ProteinModelPortalF4IAG2.
SMRF4IAG2. Positions 496-584, 594-1038.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-7299396.
STRING3702.AT1G11720.1-P.

Proteomic databases

PRIDEF4IAG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G11720.1; AT1G11720.1; AT1G11720. [F4IAG2-1]
GeneID837716.
KEGGath:AT1G11720.

Organism-specific databases

TAIRAT1G11720.

Phylogenomic databases

ProtClustDBPLN02316.

Enzyme and pathway databases

UniPathwayUPA00152.

Gene expression databases

ArrayExpressF4IAG2.

Family and domain databases

HAMAPMF_00484. Glycogen_synth.
InterProIPR005085. CBM_fam25.
IPR001296. Glyco_trans_1.
IPR011835. Glycogen/starch_synth.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamPF03423. CBM_25. 3 hits.
PF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
SMARTSM01066. CBM_25. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSSY3_ARATH
AccessionPrimary (citable) accession number: F4IAG2
Secondary accession number(s): Q1WAB7, Q306T0, Q9SAA5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: June 28, 2011
Last modified: April 16, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names