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Q9FNF2 (SSY1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Starch synthase 1, chloroplastic/amyloplastic

Short name=AtSS1
Short name=SSS
EC=2.4.1.21
Alternative name(s):
Soluble starch synthase I
Gene names
Name:SS1
Ordered Locus Names:At5g24300
ORF Names:MOP9.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the synthesis of short glycan chains within amylopectin in leaves. Is required to generate chains up to about a degree of polymerization of 10 (DP10). Ref.6 Ref.8

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 Ref.6.

Tissue specificity

Expressed in roots, leaves, stems, buds and flowers. Ref.6 Ref.7

Induction

Circadian-regulation with the lowest levels at the end of the dark period. Ref.6

Disruption phenotype

No visible phenotype under normal growth conditions, but mutant plants have reduced starch content in leaves. Ref.6

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4949Chloroplast Potential
Chain50 – 652603Starch synthase 1, chloroplastic/amyloplastic HAMAP-Rule MF_00484
PRO_0000011137

Sites

Binding site1561ADP-glucose By similarity

Experimental info

Sequence conflict78 – 858LGFQLTPP → MNSIFPCT in AAF24126. Ref.5
Sequence conflict891Q → E in AAF24126. Ref.5
Sequence conflict2221Y → H in AAF24126. Ref.5
Sequence conflict5841T → A in AAF24126. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9FNF2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 91E5069DCD1B2B5B

FASTA65272,099
        10         20         30         40         50         60 
MASLQISGSV KFEPFVGFNR IRHFRPIASL GFPRFRRRFS IGRSLLLRRS SSFSGDSRES 

        70         80         90        100        110        120 
DEERFITDAE RDGSGSVLGF QLTPPGDQQT VSTSTGEITH HEEKKEAIDQ IVMADFGVPG 

       130        140        150        160        170        180 
NRAVEEGAAE VGIPSGKAEV VNNLVFVTSE AAPYSKTGGL GDVCGSLPIA LAGRGHRVMV 

       190        200        210        220        230        240 
ISPRYLNGTA ADKNYARAKD LGIRVTVNCF GGSQEVSFYH EYRDGVDWVF VDHKSYHRPG 

       250        260        270        280        290        300 
NPYGDSKGAF GDNQFRFTLL CHAACEAPLV LPLGGFTYGE KSLFLVNDWH AGLVPILLAA 

       310        320        330        340        350        360 
KYRPYGVYKD ARSILIIHNL AHQGVEPAAT YTNLGLPSEW YGAVGWVFPT WARTHALDTG 

       370        380        390        400        410        420 
EAVNVLKGAI VTSDRIITVS QGYAWEITTV EGGYGLQDLL SSRKSVINGI TNGINVDEWN 

       430        440        450        460        470        480 
PSTDEHIPFH YSADDVSEKI KCKMALQKEL GLPIRPECPM IGFIGRLDYQ KGIDLIQTAG 

       490        500        510        520        530        540 
PDLMVDDIQF VMLGSGDPKY ESWMRSMEET YRDKFRGWVG FNVPISHRIT AGCDILLMPS 

       550        560        570        580        590        600 
RFEPCGLNQL YAMRYGTIPV VHGTGGLRDT VENFNPYAEG GAGTGTGWVF TPLSKDSMVS 

       610        620        630        640        650 
ALRLAAATYR EYKQSWEGLM RRGMTRNYSW ENAAVQYEQV FQWVFMDPPY VS 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones."
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:291-300(1997) [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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Characterization of Arabidopsis soluble starch synthase gene."
Lue W.L., Wang S.M., Yu T.S., Chen J.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-652.
[6]"Soluble starch synthase I: a major determinant for the synthesis of amylopectin in Arabidopsis thaliana leaves."
Delvalle D., Dumez S., Wattebled F., Roldan I., Planchot V., Berbezy P., Colonna P., Vyas D., Chatterjee M., Ball S., Merida A., D'Hulst C.
Plant J. 43:398-412(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
Strain: cv. Columbia.
[7]"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.
[8]"Integrated functions among multiple starch synthases determine both amylopectin chain length and branch linkage location in Arabidopsis leaf starch."
Szydlowski N., Ragel P., Hennen-Bierwagen T.A., Planchot V., Myers A.M., Merida A., d'Hulst C., Wattebled F.
J. Exp. Bot. 62:4547-4559(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006701 Genomic DNA. Translation: BAB10396.1.
CP002688 Genomic DNA. Translation: AED93282.1.
CP002688 Genomic DNA. Translation: AED93283.1.
AY128273 mRNA. Translation: AAM91082.1.
AK226881 mRNA. Translation: BAE98960.1.
AF121673 Genomic DNA. Translation: AAF24126.1.
RefSeqNP_001190378.1. NM_001203449.1.
NP_197818.1. NM_122336.4.
UniGeneAt.22528.

3D structure databases

ProteinModelPortalQ9FNF2.
SMRQ9FNF2. Positions 138-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17772. 1 interaction.

Protein family/group databases

CAZyGT5. Glycosyltransferase Family 5.

Proteomic databases

PaxDbQ9FNF2.
PRIDEQ9FNF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G24300.1; AT5G24300.1; AT5G24300.
AT5G24300.2; AT5G24300.2; AT5G24300.
GeneID832497.
KEGGath:AT5G24300.

Organism-specific databases

TAIRAT5G24300.

Phylogenomic databases

eggNOGCOG0297.
HOGENOMHOG000294940.
InParanoidQ9FNF2.
KOK00703.
OMAPYHDESQ.
PhylomeDBQ9FNF2.

Enzyme and pathway databases

BioCycARA:AT5G24300-MONOMER.
ARA:GQT-442-MONOMER.
MetaCyc:AT5G24300-MONOMER.
UniPathwayUPA00152.

Gene expression databases

ArrayExpressQ9FNF2.
GenevestigatorQ9FNF2.

Family and domain databases

HAMAPMF_00484. Glycogen_synth.
InterProIPR001296. Glyco_trans_1.
IPR011835. Glycogen/starch_synth.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR02095. glgA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSSY1_ARATH
AccessionPrimary (citable) accession number: Q9FNF2
Secondary accession number(s): Q0WV88, Q9SEI7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 92 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