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F4IAG2

- SSY3_ARATH

UniProt

F4IAG2 - SSY3_ARATH

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Protein

Starch synthase 3, chloroplastic/amyloplastic

Gene
SS3, At1g11720, F25C20.13
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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).UniRule annotation

Pathwayi

Sites

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

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. starch binding Source: InterPro
  3. starch synthase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Starch biosynthesis

Enzyme and pathway databases

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: Chromosome 1

Organism-specific databases

TAIRiAT1G11720.

Subcellular locationi

Plastidchloroplast. Plastidamyloplast Inferred UniRule annotation

GO - Cellular componenti

  1. amyloplast Source: UniProtKB-SubCell
  2. chloroplast Source: UniProtKB-SubCell
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 – 4444Chloroplast Reviewed predictionAdd
BLAST
Chaini45 – 1042998Starch synthase 3, chloroplastic/amyloplasticUniRule annotationPRO_0000419770Add
BLAST

Proteomic databases

PRIDEiF4IAG2.

Expressioni

Tissue specificityi

Expressed in leaves and flowers.1 Publication

Gene expression databases

ArrayExpressiF4IAG2.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

MINTiMINT-7299396.
STRINGi3702.AT1G11720.1-P.

Structurei

3D structure databases

ProteinModelPortaliF4IAG2.
SMRiF4IAG2. Positions 594-1038.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili247 – 30256 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transit peptide

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR005085. CBM_fam25.
IPR001296. Glyco_trans_1.
IPR011835. Glycogen/starch_synth.
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. Align

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

MISYFLNQDF SRKKQGRMAA SGPKSSGPRG FGRRTTVGSA QKRTQKKNGE     50
KDSNATSTAT NEVSGISKLP AAKVDVQKQS SVVLNERNVL DRSDIEDGSD 100
RLDKKTTDDD DLLEQKLKLE RENLRRKEIE TLAAENLARG DRMFVYPVIV 150
KPDEDIEVFL NRNLSTLNNE PDVLIMGAFN EWRWKSFTRR LEKTWIHEDW 200
LSCLLHIPKE AYKMDFVFFN GQSVYDNNDS KDFCVEIKGG MDKVDFENFL 250
LEEKLREQEK LAKEEAERER QKEEKRRIEA QKAAIEADRA QAKAETQKRR 300
ELLQPAIKKA VVSAENVWYI EPSDFKAEDT VKLYYNKRSG PLTNSKELWL 350
HGGFNNWVDG LSIVVKLVNA ELKDVDPKSG NWWFAEVVVP GGALVIDWVF 400
ADGPPKGAFL YDNNGYQDFH ALVPQKLPEE LYWLEEENMI FRKLQEDRRL 450
KEEVMRAKME KTARLKAETK ERTLKKFLLS QKDVVYTEPL EIQAGNPVTV 500
LYNPANTVLN GKPEVWFRGS FNRWTHRLGP LPPQKMEATD DESSHVKTTA 550
KVPLDAYMMD FVFSEKEDGG IFDNKNGLDY HLPVVGGISK EPPLHIVHIA 600
VEMAPIAKVG GLGDVVTSLS RAVQELNHNV DIVFPKYDCI KHNFVKDLQF 650
NRSYHWGGTE IKVWHGKVEG LSVYFLDPQN GLFQRGCVYG CADDAGRFGF 700
FCHAALEFLL QGGFHPDILH CHDWSSAPVS WLFKDHYTQY GLIKTRIVFT 750
IHNLEFGANA IGKAMTFADK ATTVSPTYAK EVAGNSVISA HLYKFHGIIN 800
GIDPDIWDPY NDNFIPVPYT SENVVEGKRA AKEELQNRLG LKSADFPVVG 850
IITRLTHQKG IHLIKHAIWR TLERNGQVVL LGSAPDPRIQ NDFVNLANQL 900
HSSHGDRARL VLTYDEPLSH LIYAGADFIL VPSIFEPCGL TQLIAMRYGA 950
VPVVRKTGGL FDTVFDVDHD KERAQAQVLE PNGFSFDGAD APGVDYALNR 1000
AISAWYDGRE WFNSLCKTVM EQDWSWNRPA LEYLELYHSA RK 1042
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti741 – 7411G → D in ABB46391. 1 Publication
Sequence conflicti1041 – 10411R → C in ABB46391. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi H86250.
RefSeqi NP_172637.2. NM_101044.3. [F4IAG2-1 ]
UniGenei At.42115.

3D structure databases

ProteinModelPortali F4IAG2.
SMRi F4IAG2. Positions 594-1038.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-7299396.
STRINGi 3702.AT1G11720.1-P.

Proteomic databases

PRIDEi F4IAG2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G11720.1 ; AT1G11720.1 ; AT1G11720 . [F4IAG2-1 ]
GeneIDi 837716.
KEGGi ath:AT1G11720.

Organism-specific databases

TAIRi AT1G11720.

Enzyme and pathway databases

UniPathwayi UPA00152 .

Gene expression databases

ArrayExpressi F4IAG2.

Family and domain databases

HAMAPi MF_00484. Glycogen_synth.
InterProi IPR005085. CBM_fam25.
IPR001296. Glyco_trans_1.
IPR011835. Glycogen/starch_synth.
IPR013534. Starch_synth_cat_dom.
[Graphical view ]
Pfami PF03423. CBM_25. 3 hits.
PF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view ]
SMARTi SM01066. CBM_25. 3 hits.
[Graphical view ]
ProtoNeti Search...

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 11, 2014
This is version 28 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

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