F4IAG2 (SSY3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	1042 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 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	Plastid › chloroplast. Plastid › amyloplast 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 process	Starch biosynthesis
Cellular component	Amyloplast Chloroplast Plastid
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Transit peptide
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	amylopectin biosynthetic process Inferred from genetic interaction Ref.6. Source: UniProtKB starch biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	starch binding Inferred from electronic annotation. Source: InterPro starch synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 44	44	Chloroplast Potential
	Chain	45 – 1042	998	Starch synthase 3, chloroplastic/amyloplastic HAMAP-Rule MF_00484		PRO_0000419770
Regions
	Coiled coil	247 – 302	56	Potential
Sites
	Binding site	608	1	ADP-glucose By similarity
Experimental info
	Sequence conflict	741	1	G → D in ABB46391. Ref.3
	Sequence conflict	1041	1	R → C in ABB46391. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 28, 2011. Version 1. Checksum: C0481F694FCDC7D2	FASTA	1,042	118,512
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00542163.
PIR	H86250.
RefSeq	NP_172637.2. NM_101044.3.
UniGene	At.42115.
3D structure databases
ProteinModelPortal	F4IAG2.
SMR	F4IAG2. Positions 594-1038.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G11720.1-P.
Proteomic databases
PRIDE	F4IAG2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G11720.1; AT1G11720.1; AT1G11720.
GeneID	837716.
KEGG	ath:AT1G11720.
Organism-specific databases
TAIR	At1g11720.
Phylogenomic databases
ProtClustDB	PLN02316.
Enzyme and pathway databases
UniPathway	UPA00152.
Gene expression databases
ArrayExpress	F4IAG2.
Family and domain databases
HAMAP	MF_00484. Glycogen_synth.
InterPro	IPR005085. CBM_fam25. IPR001296. Glyco_trans_1. IPR011835. Glycogen/starch_synth. IPR013534. Starch_synth_cat_dom. [Graphical view]
Pfam	PF03423. CBM_25. 3 hits. PF08323. Glyco_transf_5. 1 hit. PF00534. Glycos_transf_1. 1 hit. [Graphical view]
SMART	SM01066. CBM_25. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SSY3_ARATH

Accession

Primary (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:	May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program