Q0WVX5 (SSY4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable starch synthase 4, chloroplastic/amyloplastic
Short name=AtSS4
EC=2.4.1.21

Alternative name(s):
Soluble starch synthase IV

Gene names

Name:	SS4
Ordered Locus Names:	At4g18240
ORF Names:	T9A21.90

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	1040 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	Probably involved in the priming of starch granule formation. May play a regulatory role in the control of starch accumulation in plastids. Is necessary and sufficient to establish the correct number of starch granules observed in chloroplasts. Ref.4 Ref.5 Ref.6
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 Ref.5 Ref.6.
Tissue specificity	Expressed in leaves and flowers. Ref.4
Disruption phenotype	Severe reduced growth, reduced number of starch granules, altered structure of starch granules. Ref.4
Miscellaneous	Plants over-expressing SS4 have increased levels of starch in leaves and display a higher growth rate than wild-type (Ref.6). HAMAP-Rule MF_00484
Sequence similarities	Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.
Sequence caution	The sequence CAA16796.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78826.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Starch biosynthesis
Cellular component	Amyloplast Chloroplast Plastid
Domain	Coiled coil Transit peptide
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	starch biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway starch metabolic process Inferred from mutant phenotype Ref.4. Source: TAIR
Cellular_component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR
Molecular_function	starch synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Chloroplast Potential
	Chain	43 – 1040	998	Probable starch synthase 4, chloroplastic/amyloplastic HAMAP-Rule MF_00484		PRO_0000419771
Regions
	Coiled coil	187 – 466	280	Potential
Sites
	Binding site	556	1	ADP-glucose By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0WVX5 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: A89327E598D01165	FASTA	1,040	117,747
	10 20 30 40 50 60 MTTKLSSFCF LTHGLAGISC EREHGSSRRF FYLPSRRLVS TSCKMRQQRG FDSSKRQEVK 70 80 90 100 110 120 KGSPKPILSI NSGLQSNNDE ESDLENGSAD SVPSLKSDAE KGSSIHGSID MNHADENLEK 130 140 150 160 170 180 KDDIQTTEVT RRKSKTAKKK GESIHATIDI GHDDGKNLDN ITVPEVAKAL SLNKSEGEQI 190 200 210 220 230 240 SDGQFGELMT MIRSAEKNIL RLDEARATAL DDLNKILSDK EALQGEINVL EMKLSETDER 250 260 270 280 290 300 IKTAAQEKAH VELLEEQLEK LRHEMISPIE SDGYVLALSK ELETLKLENL SLRNDIEMLK 310 320 330 340 350 360 SELDSVKDTG ERVVVLEKEC SGLESSVKDL ESKLSVSQED VSQLSTLKIE CTDLWAKVET 370 380 390 400 410 420 LQLLLDRATK QAEQAVIVLQ QNQDLRNKVD KIEESLKEAN VYKESSEKIQ QYNELMQHKV 430 440 450 460 470 480 TLLEERLEKS DAEIFSYVQL YQESIKEFQE TLESLKEESK KKSRDEPVDD MPWDYWSRLL 490 500 510 520 530 540 LTVDGWLLEK KIASNDADLL RDMVWKKDRR IHDTYIDVKD KNERDAISAF LKLVSSPTSS 550 560 570 580 590 600 GLYVVHIAAE MAPVAKVGGL GDVVAGLGKA LQRKGHLVEI ILPKYDCMQY DRVRDLRALD 610 620 630 640 650 660 TVVESYFDGK LYKNKIWIGT VEGLPVHFIE PQHPSKFFWR GQFYGEQDDF RRFSYFSRAA 670 680 690 700 710 720 LELLLQSGKK PDIIHCHDWQ TAFVAPLYWD LYAPKGLDSA RICFTCHNFE YQGTASASEL 730 740 750 760 770 780 GSCGLDVNQL NRPDRMQDHS SGDRVNPVKG AIIFSNIVTT VSPTYAQEVR TAEGGKGLHS 790 800 810 820 830 840 TLNFHSKKFI GILNGIDTDS WNPATDPFLK AQFNAKDLQG KEENKHALRK QLGLSSAESR 850 860 870 880 890 900 RPLVGCITRL VPQKGVHLIR HAIYRTLELG GQFVLLGSSP VPHIQREFEG IEQQFKSHDH 910 920 930 940 950 960 VRLLLKYDEA LSHTIYAASD LFIIPSIFEP CGLTQMIAMR YGSIPIARKT GGLNDSVFDI 970 980 990 1000 1010 1020 DDDTIPTQFQ NGFTFQTADE QGFNYALERA FNHYKKDEEK WMRLVEKVMS IDFSWGSSAT 1030 1040 QYEELYTRSV SRARAVPNRT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [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]	"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.
[4]	"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: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. Strain: cv. Columbia.
[5]	"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, SUBCELLULAR LOCATION.
[6]	"Enhancing the expression of starch synthase class IV results in increased levels of both transitory and long-term storage starch." Gamez-Arjona F.M., Li J., Raynaud S., Baroja-Fernandez E., Munoz F.J., Ovecka M., Ragel P., Bahaji A., Pozueta-Romero J., Merida A. Plant Biotechnol. J. 9:1049-1060(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL021713 Genomic DNA. Translation: CAA16796.1. Sequence problems. AL161548 Genomic DNA. Translation: CAB78826.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE84015.1. AK226610 mRNA. Translation: BAE98723.1.
IPI	IPI00524471.
PIR	T04926.
RefSeq	NP_193558.3. NM_117934.4.
UniGene	At.46236.
3D structure databases
ProteinModelPortal	Q0WVX5.
SMR	Q0WVX5. Positions 542-1028.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G18240.1-P.
Proteomic databases
PRIDE	Q0WVX5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G18240.1; AT4G18240.1; AT4G18240.
GeneID	827550.
KEGG	ath:AT4G18240.
Organism-specific databases
TAIR	At4g18240.
Phylogenomic databases
InParanoid	Q0WVX5.
OMA	LVGCITR.
PhylomeDB	Q0WVX5.
ProtClustDB	PLN02939.
Enzyme and pathway databases
UniPathway	UPA00152.
Gene expression databases
ArrayExpress	Q0WVX5.
Genevestigator	Q0WVX5.
Family and domain databases
HAMAP	MF_00484. Glycogen_synth.
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

SSY4_ARATH

Accession

Primary (citable) accession number: Q0WVX5
Secondary accession number(s): O49727

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2012
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program