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Protein

Starch synthase 1, chloroplastic/amyloplastic

Gene

SS1

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

Functioni

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).2 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 sitei156 – 1561ADP-glucoseBy similarity

GO - Molecular functioni

  • starch synthase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Starch biosynthesis

Enzyme and pathway databases

BioCyciARA:AT5G24300-MONOMER.
ARA:GQT-442-MONOMER.
MetaCyc:AT5G24300-MONOMER.
UniPathwayiUPA00152.

Protein family/group databases

CAZyiGT5. Glycosyltransferase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Starch synthase 1, chloroplastic/amyloplastic (EC:2.4.1.21)
Short name:
AtSS1
Short name:
SSS
Alternative name(s):
Soluble starch synthase I
Gene namesi
Name:SS1
Ordered Locus Names:At5g24300
ORF Names:MOP9.12
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G24300.

Subcellular locationi

GO - Cellular componenti

  • amyloplast Source: UniProtKB-SubCell
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Amyloplast, Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but mutant plants have reduced starch content in leaves.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4949ChloroplastSequence AnalysisAdd
BLAST
Chaini50 – 652603Starch synthase 1, chloroplastic/amyloplasticPRO_0000011137Add
BLAST

Proteomic databases

PaxDbiQ9FNF2.
PRIDEiQ9FNF2.

Expressioni

Tissue specificityi

Expressed in roots, leaves, stems, buds and flowers.2 Publications

Inductioni

Circadian-regulation with the lowest levels at the end of the dark period.1 Publication

Gene expression databases

ExpressionAtlasiQ9FNF2. baseline and differential.

Interactioni

Protein-protein interaction databases

BioGridi17772. 1 interaction.
STRINGi3702.AT5G24300.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FNF2.
SMRiQ9FNF2. Positions 138-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0297.
HOGENOMiHOG000294940.
InParanoidiQ9FNF2.
KOiK00703.
OMAiNAMRCRA.
PhylomeDBiQ9FNF2.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02095. glgA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9FNF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLQISGSV KFEPFVGFNR IRHFRPIASL GFPRFRRRFS IGRSLLLRRS
60 70 80 90 100
SSFSGDSRES DEERFITDAE RDGSGSVLGF QLTPPGDQQT VSTSTGEITH
110 120 130 140 150
HEEKKEAIDQ IVMADFGVPG NRAVEEGAAE VGIPSGKAEV VNNLVFVTSE
160 170 180 190 200
AAPYSKTGGL GDVCGSLPIA LAGRGHRVMV ISPRYLNGTA ADKNYARAKD
210 220 230 240 250
LGIRVTVNCF GGSQEVSFYH EYRDGVDWVF VDHKSYHRPG NPYGDSKGAF
260 270 280 290 300
GDNQFRFTLL CHAACEAPLV LPLGGFTYGE KSLFLVNDWH AGLVPILLAA
310 320 330 340 350
KYRPYGVYKD ARSILIIHNL AHQGVEPAAT YTNLGLPSEW YGAVGWVFPT
360 370 380 390 400
WARTHALDTG EAVNVLKGAI VTSDRIITVS QGYAWEITTV EGGYGLQDLL
410 420 430 440 450
SSRKSVINGI TNGINVDEWN PSTDEHIPFH YSADDVSEKI KCKMALQKEL
460 470 480 490 500
GLPIRPECPM IGFIGRLDYQ KGIDLIQTAG PDLMVDDIQF VMLGSGDPKY
510 520 530 540 550
ESWMRSMEET YRDKFRGWVG FNVPISHRIT AGCDILLMPS RFEPCGLNQL
560 570 580 590 600
YAMRYGTIPV VHGTGGLRDT VENFNPYAEG GAGTGTGWVF TPLSKDSMVS
610 620 630 640 650
ALRLAAATYR EYKQSWEGLM RRGMTRNYSW ENAAVQYEQV FQWVFMDPPY

VS
Length:652
Mass (Da):72,099
Last modified:March 1, 2001 - v1
Checksum:i91E5069DCD1B2B5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 858LGFQLTPP → MNSIFPCT in AAF24126 (Ref. 5) Curated
Sequence conflicti89 – 891Q → E in AAF24126 (Ref. 5) Curated
Sequence conflicti222 – 2221Y → H in AAF24126 (Ref. 5) Curated
Sequence conflicti584 – 5841T → A in AAF24126 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001190378.1. NM_001203449.1.
NP_197818.1. NM_122336.4.
UniGeneiAt.22528.

Genome annotation databases

EnsemblPlantsiAT5G24300.1; AT5G24300.1; AT5G24300.
AT5G24300.2; AT5G24300.2; AT5G24300.
GeneIDi832497.
KEGGiath:AT5G24300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001190378.1. NM_001203449.1.
NP_197818.1. NM_122336.4.
UniGeneiAt.22528.

3D structure databases

ProteinModelPortaliQ9FNF2.
SMRiQ9FNF2. Positions 138-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17772. 1 interaction.
STRINGi3702.AT5G24300.1.

Protein family/group databases

CAZyiGT5. Glycosyltransferase Family 5.

Proteomic databases

PaxDbiQ9FNF2.
PRIDEiQ9FNF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G24300.1; AT5G24300.1; AT5G24300.
AT5G24300.2; AT5G24300.2; AT5G24300.
GeneIDi832497.
KEGGiath:AT5G24300.

Organism-specific databases

TAIRiAT5G24300.

Phylogenomic databases

eggNOGiCOG0297.
HOGENOMiHOG000294940.
InParanoidiQ9FNF2.
KOiK00703.
OMAiNAMRCRA.
PhylomeDBiQ9FNF2.

Enzyme and pathway databases

UniPathwayiUPA00152.
BioCyciARA:AT5G24300-MONOMER.
ARA:GQT-442-MONOMER.
MetaCyc:AT5G24300-MONOMER.

Miscellaneous databases

PROiQ9FNF2.

Gene expression databases

ExpressionAtlasiQ9FNF2. baseline and differential.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02095. glgA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiSSY1_ARATH
AccessioniPrimary (citable) accession number: Q9FNF2
Secondary accession number(s): Q0WV88, Q9SEI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 97 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.