Q9FNF2 (SSY1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	652 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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).
Pathway	Glycan biosynthesis; starch biosynthesis.
Subcellular location	Plastid › chloroplast. Plastid › amyloplast 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.

Ontologies

Keywords
Biological process	Starch biosynthesis
Cellular component	Amyloplast Chloroplast Plastid
Domain	Transit peptide
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	amylopectin biosynthetic process Inferred from direct assay Ref.6. Source: TAIR starch biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast stroma Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR
Molecular_function	starch synthase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 49	49	Chloroplast Potential
	Chain	50 – 652	603	Starch synthase 1, chloroplastic/amyloplastic		PRO_0000011137
Sites
	Binding site	156	1	ADP-glucose By similarity
Experimental info
	Sequence conflict	78 – 85	8	LGFQLTPP → MNSIFPCT in AAF24126. Ref.5
	Sequence conflict	89	1	Q → E in AAF24126. Ref.5
	Sequence conflict	222	1	Y → H in AAF24126. Ref.5
	Sequence conflict	584	1	T → A in AAF24126. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9FNF2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 91E5069DCD1B2B5B	FASTA	652	72,099
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.
IPI	IPI00518916.
RefSeq	NP_001190378.1. NM_001203449.1. NP_197818.1. NM_122336.4.
UniGene	At.22528.
3D structure databases
ProteinModelPortal	Q9FNF2.
SMR	Q9FNF2. Positions 143-641.
ModBase	Search...
Protein family/group databases
CAZy	GT5. Glycosyltransferase Family 5.
Proteomic databases
PaxDb	Q9FNF2.
PRIDE	Q9FNF2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G24300.1; AT5G24300.1; AT5G24300. AT5G24300.2; AT5G24300.2; AT5G24300.
GeneID	832497.
KEGG	ath:AT5G24300.
Organism-specific databases
TAIR	At5g24300.
Phylogenomic databases
eggNOG	COG0297.
HOGENOM	HOG000294940.
InParanoid	Q9FNF2.
KO	K00703.
OMA	ADVIMVP.
PhylomeDB	Q9FNF2.
ProtClustDB	CLSN2686324.
Enzyme and pathway databases
UniPathway	UPA00152.
Gene expression databases
ArrayExpress	Q9FNF2.
Genevestigator	Q9FNF2.
GermOnline	AT5G24300. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001296. Glyco_trans_1. IPR011835. Glycogen/starch_synth. IPR013534. Starch_synth_cat_dom. [Graphical view]
Pfam	PF08323. Glyco_transf_5. 1 hit. PF00534. Glycos_transf_1. 1 hit. [Graphical view]
TIGRFAMs	TIGR02095. glgA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SSY1_ARATH

Accession

Primary (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 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program